Robert Glickman, M.D.

Case presentations of salivary gland infections
Turner, Michael D; Glickman, Robert
2009 Aug;21(3):359-362, Oral & maxillofacial surgery clinics of North America
Salivary gland infections arise from a wide variety of etiologies: bacteria, localized viruses, systemic viruses, autoimmune diseases, secondary to sialoliths and strictures, and congenital disorders. When dealing with these entities, the diagnosis of the majority of them can be made quickly, although some of the rarer diseases are more difficult to recognize, particularly when they have a more obvious secondary bacterial infection. This article presents six cases and describes their management
— id: 105042, year: 2009, vol: 21, page: 359, stat: Journal Article,

Preface. Salivary gland infections
Turner, Michael D; Glickman, Robert
2009 Aug;21(3):ix-ix, Oral & maxillofacial surgery clinics of North America
— id: 105040, year: 2009, vol: 21, page: ix, stat: Journal Article,

Salivary gland infections
Turner, Michael D; Glickman, Robert; Haug, Richard H
Philadelphia, PA : Saunders, 2009,
— id: 1976, year: 2009, vol: , page: , stat: ,

AGA Institute Future Trends Committee Report: The Future of Gastroenterology Training Programs in the United States
Wang, TC; Cominelli, F; Fleischer, DE; Gordon, JM; Glickman, RM; Limsui, D; McQuaid, KR; Montrose, M; Pasricha, PJ; Powell, DW; Rowe, WA; Sandborn, WJ; Todisco, A
2008 NOV ;135(5):1764-1789, Gastroenterology
— id: 90774, year: 2008, vol: 135, page: 1764, stat: Journal Article,

Clinical implications of cyclo-oxygenase-2 inhibitors for acute dental pain management - Benefits and risks
Spink, M; Bahn, S; Glickman, R
2005 OCT ;136(10):1439-1448, Journal of the American Dental Association
Background. Cyclo-oxygenase-2 inhibitors (COX-2(i)) demonstrate analgesic efficacy for patients who require gastrointestinal safety. The authors discuss the potential benefits and risks of these novel, but expensive, analgesics when used in dentistry. Methods. The authors conducted a MED-LINE search focused on the subject headings of common analgesic drugs and COX-2(i), using peer-reviewing journals limited to the English language. They selected for review 127 articles that met the criteria. They also tried to identify any randomized controlled trials pertinent to dentistry and indicative of evidence-based medicine. Results. When comparing COX isoforms (COX-1 and COX-2), the authors found that overlapping and mutually exclusively properties coexist. COX-2(i) originally were developed to minimize interference with the gastroprotective properties of COX-1 isoform, while selectively preventing prostanoid synthesis expressed solely at sites of bodily trauma or other inflammation. COX-2(i) were found to provide pain relief equal to or slightly exceeding that offered by many mild narcotics. They may avoid some of the serious side effects that can occur with even short-term use of nonselective nonsteroidal anti-inflammatory drugs. Conclusions. The Pharmacodynamics of COX-2(i) reveal an agent that includes analgesic, anti-inflammatory and gastroprotective properties but also allows for an undesirable disruption of the delicate hemodynamic balance. Clinical Implications. Symptomatic and asymptomatic gastroparietic patients who do not have severe cardiovascular, cerebral or renal ischemic disease benefit from use of COX-2(i). Long-term use of these agents in medically compromised patients may prove disastrous
— id: 98037, year: 2005, vol: 136, page: 1439, stat: Journal Article,

Severe corneal edema after temporomandibular joint reconstruction: report of a case
Fleisher, Kenneth E; Hirsch, David L; Pahlavi, Iman Ali; Glickman, Robert
2004 Oct;62(10):1324-1326, Journal of oral & maxillofacial surgery
— id: 91047, year: 2004, vol: 62, page: 1324, stat: Journal Article,

Allelic loss at the GPx-1 locus in cancer of the head and neck
Hu, Ya Jun; Dolan, M Eileen; Bae, Richard; Yee, Herman; Roy, Martin; Glickman, Robert; Kiremidjian-Schumacher, Lidia; Diamond, Alan M
2004 Nov;101(2):97-106, Biological trace element research
Glutathione peroxidase is a selenium-containing, antioxidant enzyme previously implicated in the risk and development of lung and breast cancer, in part the result of allelic loss at the GPx-1 locus. This study examined allelic loss at the same locus in squamous cell carcinomas of the head and neck. The frequency of a polymorphism at codon 198 resulting in either a leucine or a proline at that position was surveyed by comparing 133 DNA samples obtained from head and neck tumors and 517 samples obtained from cancer-free individuals. Tumor DNAs exhibited fewer pro/leu heterozygotes as compared to DNA obtained from the cancer-free population. Fewer GPx-1 heterozygotes were verified by determining the frequency of highly polymorphic alanine repeat sequences in the same gene. The analysis revealed an approximately 42% reduction in heterozygosity in the DNA from the tumor samples. In order to assess loss of heterozygosity (LOH) at the GPx-1 locus, DNA was genotyped from peripheral lymphocytes, tumor tissue, and microscopically normal tissues adjacent to the tumor, derived from the same patients. These studies indicated LOH at the GPx-1 locus in each of the three tumor/normal tissues sample sets examined. Furthermore, LOH in the microscopically normal tissues at the tumor margin occurred in two of the three sample sets examined. These data implicate GPx-1 in the development of squamous cell carcinoma the head and neck and suggest that allelic loss of this gene, or one tightly linked to it, is an early event in the development of this type of malignancy
— id: 114161, year: 2004, vol: 101, page: 97, stat: Journal Article,

Why the physician-scientist? Why the Association of American Physicians?
Glickman RM
1999 Sep-Oct;111(5):463-466, Proceedings of the Association of American Physicians
— id: 11948, year: 1999, vol: 111, page: 463, stat: Journal Article,

Intestinal transcription and synthesis of apolipoprotein AI is regulated by five natural polymorphisms upstream of the apolipoprotein CIII gene
Naganawa S; Ginsberg HN; Glickman RM; Ginsburg GS
1997 Apr 15;99(8):1958-1965, Journal of clinical investigation
To understand the factors contributing to the synthesis of human apolipoprotein AI (apoAI), relative apoAI synthesis was measured from endoscopic biopsy samples obtained from 18 healthy volunteers. The relative amount of apoAI synthesis was directly correlated with steady state intestinal apoAI mRNA levels and a 10-fold within-group variability was observed. Analysis of genomic DNA from the subjects revealed five polymorphic sites which defined two haplotypes in the intestinal enhancer region of the apoAI gene located upstream of the apolipoprotein CIII gene transcriptional start site (+ 1): (-641 C to A, -630 G to A, -625 T to deletion, -482 C to T, and -455 T to C). The population frequencies of the wild-type and mutant alleles were 0.53 and 0.44, respectively. Mean steady state apoAI mRNA levels and mean relative apoAI synthesis were 49 and 37% lower, respectively, in homozygotes for the mutant allele and 28 and 41% lower, respectively, in heterozygotes than in homozygotes for the wild-type allele (P < 0.05 for both). Site-directed mutants of apoAI gene promoter/reporter constructs containing the above mutations were transfected into Caco-2 cells and showed a 46% decrease in transcriptional activity compared with the wild type (P < 0.001); however, no significant differences were observed in HepG2 cells. Electrophoretic mobility shift assays showed that the mutated sequences from -655 to -610 bound Caco-2 cell nuclear protein(s) while the wild type did not. These results indicate that intestinal apoAI gene transcription and protein synthesis are genetically determined and are reduced in the presence of common mutations which induced binding of nuclear protein(s), possibly a transcriptional repressor
— id: 18974, year: 1997, vol: 99, page: 1958, stat: Journal Article,

A common genetic varian upstream of ApoCIII gene coordinately controls intestinal expression of the human apoAI and apoAIV genes
Ginsburg GS; Naganawa S; Ginsberg H; Glickman RM
1996 ;94(8):I.274-I.274, Circulation
— id: 62874, year: 1996, vol: 94, page: I.274, stat: Journal Article,

A common genetic variant in the human apoprotein AI gene intestinal control region reduces transcription and induces high affinity binding of nuclear proteins
Ginsburg GS; Naganawa S; Ginsberg H; Glickman RM
1996 ;94(8):I.396-I.396, Circulation
— id: 62873, year: 1996, vol: 94, page: I.396, stat: Journal Article,

A 35-year-old man with epigastric pain
Glickman R
1995 Aug 9;274(6):495-500, JAMA
— id: 62839, year: 1995, vol: 274, page: 495, stat: Journal Article,

Lipoprotein metabolism
Glickman RM; Sabesin SM
Liver : biology and pathobiology New York : Raven Press, 1994,
— id: 3901, year: 1994, vol: , page: 391, stat: Chapter,

Fostering a new relationship between departments of medicine and teaching hospitals
Glickman RM; Bennett JC; Nolan JP; Stobo JD; Rubenstein A; Terwilliger J
1993 Apr;68(4):276-277, Academic medicine
— id: 18976, year: 1993, vol: 68, page: 276, stat: Journal Article,

United we stand
Glickman RM; Bennett JC; Nolan JP; Stobo JD; Rubenstein AH; Mufson MA; Terwilliger J
1993 Jun 1;118(11):903-904, Annals of internal medicine
— id: 18975, year: 1993, vol: 118, page: 903, stat: Journal Article,

Activism in academic internal medicine
Glickman R; Bennett JC; Nolan J; Stobo J; Rubenstein A; Terwilliger J
1992 Aug 1;117(3):259-260, Annals of internal medicine
— id: 62840, year: 1992, vol: 117, page: 259, stat: Journal Article,

Enterocyte lipid absorption and secretion
Davidson NO; Magun A; Glickman RM
Handbook of physiology Bethesda MD : American Physiological Society, 1991,
— id: 3908, year: 1991, vol: , page: 505, stat: Chapter,

Apolipoprotein synthesis in normal and abetalipoproteinemic intestinal mucosa
Glickman RM; Glickman JN; Magun A; Brin M
1991 Sep;101(3):749-755, Gastroenterology
The genetic disease abetalipoproteinemia is characterized by a total absence of apolipoprotein B-containing lipoproteins from plasma. A presumed synthetic defect in apolipoprotein B synthesis was thought to be responsible for this disorder. The present study quantitates apoprotein B synthesis and apolipoprotein B messenger RNA levels in duodenal mucosa from normal patients and four patients with abetalipoproteinemia. After in vitro [3H]leucine incorporation, small intestinal biopsy specimens from three of four patients with abetalipoproteinemia synthesized immunoprecipitable apolipoprotein B of identical mobility (on sodium dodecyl sulfate gel electrophoresis) to normal apolipoprotein B. In abetalipoproteinemia, the apolipoprotein B content of intestinal mucosa by radioimmunoassay was 15% of normal mucosal values, whereas apolipoprotein B messenger RNA quantitation showed 3-20-fold increased levels compared with normal mucosa. In one patient, smaller-molecular-weight fragments of apolipoprotein B were immunoprecipitated from duodenal biopsy specimens. The synthesis rates and messenger RNA levels of two other chylomicron apoproteins (apolipoprotein A-I and apolipoprotein A-IV) were found to be reduced by 50%. These results show the synthesis of immunologically recognizable apolipoprotein B48 in abetalipoproteinemia. The significance of mucosal apolipoprotein B content in abetalipoproteinemia is discussed in terms of factors controlling apolipoprotein B synthesis in normal mucosa and in abetalipoproteinemia
— id: 18977, year: 1991, vol: 101, page: 749, stat: Journal Article,

Regulation of hepatic apolipoprotein synthesis in the 17 alpha-ethinyl estradiol-treated rat
Seishima M; Bisgaier CL; Davies SL; Glickman RM
1991 Jun;32(6):941-951, Journal of lipid research
Regulatory mechanisms of hepatic apolipoprotein synthesis were studied in groups of male Sprague-Dawley rats made severely hypolipidemic by treatment with pharmacological doses of 17 alpha-ethinyl estradiol. Treatment resulted in a marked reduction of plasma cholesterol and apolipoproteins B, A-I, and A-IV. Hepatic apoA-I mRNA and apoA-I synthesis were increased in the ethinyl estradiol-treated animals. Hepatic apoA-IV protein synthesis rates were unaltered; however, a reduction of the apoA-IV mRNA level was observed. Diet-control studies suggested the effects of 17 alpha-ethinyl estradiol on apoA-I, unlike those on apoA-IV, appeared to be related to the steroid and not to reduced caloric intake. Livers of control and ethinyl estradiol-treated rats synthesized both apoBH and apoBL. Total hepatic apoB (apoBL plus apoBH) synthesis and apoB mRNA levels in the ethinyl estradiol-treated rats were similar to ad libitum fed or diet-controls. In ad libitum fed and diet-control rats, 21% and 32%, respectively, of newly synthesized hepatic apoB was apoBH. In contrast, 47% of the newly synthesized apoB in the ethinyl estradiol-treated animal was apoBH. Nucleotide sequence analysis of hepatic apoB mRNA confirmed a marked decrease in the proportion of the apoBL mRNA in ethinyl estradiol-treated animals. After cessation of 17 alpha-ethinyl estradiol treatment, the hepatic apolipoprotein A-I synthesis rate, apolipoprotein A-I and A-IV mRNA levels, and the apoBH and apoBL synthesis rates, as well as plasma apolipoprotein and cholesterol levels, returned to normal. A major finding of the present study is that pharmacological doses of ethinyl estradiol do not affect total hepatic apoB synthesis, but increase the relative amount of apoBH synthesized
— id: 18978, year: 1991, vol: 32, page: 941, stat: Journal Article,

Management of facial injuries
Capan LM; Miller SM; Glickman R
Trauma : anesthesia and intensive care Philadelphia : Lippincott, 1990,
— id: 3406, year: 1990, vol: , page: 385, stat: Chapter,

Inflammatory bowel disease: ulcerative colitis and Crohn's disease
Glickman RM
Harrison's principles of internal medicine New York : McGraw-Hill, 1990,
— id: 3898, year: 1990, vol: , page: 1403, stat: Chapter,

Abdominal swelling and ascites
Glickman RM; Isselbacher KJ
Harrison's principles of internal medicine New York : McGraw-Hill, 1990,
— id: 3897, year: 1990, vol: , page: 232, stat: Chapter,

Effect of a neutralizing monoclonal antibody to cholesteryl ester transfer protein on the redistribution of apolipoproteins A-IV and E among human lipoproteins
Bisgaier CL; Siebenkas MV; Hesler CB; Swenson TL; Blum CB; Marcel YL; Milne RW; Glickman RM; Tall AR
1989 Jul;30(7):1025-1031, Journal of lipid research
The effect of inhibiting cholesteryl ester transfer protein (CETP) on the in vitro redistribution of apolipoproteins(apo) A-IV and apoE among lipoproteins in whole plasma was studied in seven normal male subjects. Plasmas were incubated in the presence of a purified monoclonal antibody TP2 (Mab TP2) that neutralizes the activity of CETP. Mab TP2 had no effect on lecithin:cholesterol acyltransferase (LCAT) activity. Prior to and following a 6-h incubation at 37 degrees C in the presence of Mab TP2 or a control mouse myeloma immunoglobulin (IgG), plasmas were gel-filtered on Sephacryl S-300 and the distribution of apoA-IV and apoE among lipoproteins was determined by radioimmunoassay. Incubation (i.e., with active LCAT and CETP) increased the amount of apoA-IV associated with lipoproteins by 240%. When CETP activity was inhibited during incubation, the amount of apoA-IV that became lipoprotein-associated was significantly increased (315% of basal). Plasma incubation also caused a redistribution of apoE from high density lipoproteins (HDL) to larger lipoproteins (131% of basal); however, when CETP was inhibited, significantly greater amounts of apoE became associated with the larger particles (155% of basal). These effects were observed in all seven subjects. Increased movement of apoE from HDL to triglyceride-rich particles was not due to displacement by apoA-IV since loss of apoE from HDL was still observed when no movement of apoA-IV onto HDL occurred, such as during LCAT or combined LCAT and CETP inhibition. We speculate that low CETP activity (e.g., in species such as rats) may lead to an increased content of HDL apoA-IV and also to apoE enrichment of triglyceride-rich lipoproteins, augmenting their clearance
— id: 18980, year: 1989, vol: 30, page: 1025, stat: Journal Article,

Reorganizing the AGA: why, how, and when
Glickman RM
1989 Dec;97(6):1361-1367, Gastroenterology
— id: 18979, year: 1989, vol: 97, page: 1361, stat: Journal Article,

House-staff training--the need for careful reform
Glickman RM
1988 Mar 24;318(12):780-782, New England journal of medicine
— id: 18982, year: 1988, vol: 318, page: 780, stat: Journal Article,

Lipoprotein metabolism
Glickman RM; Sabesin SM
Liver : biology and pathobiology New York : Raven Press, 1988,
— id: 3900, year: 1988, vol: , page: 331, stat: Chapter,

Intracellular apoA-I and apoB distribution in rat intestine is altered by lipid feeding
Magun AM; Mish B; Glickman RM
1988 Sep;29(9):1107-1116, Journal of lipid research
Intracellular forms of chylomicrons, very low density lipoprotein (VLDL) and high density lipoprotein (HDL) have previously been isolated from the rat intestine. These intracellular particles are likely to be nascent precursors of secreted lipoproteins. To study the distribution of intracellular apolipoprotein among nascent lipoproteins, a method to isolate intracellular lipoproteins was developed and validated. The method consists of suspending isolated enterocytes in hypotonic buffer containing a lipase inhibitor, rupturing cell membranes by nitrogen cavitation, and isolating lipoproteins by sequential ultracentrifugation. ApoB and apoA-I mass are determined by radioimmunoassay and newly synthesized apolipoprotein characterized following [3H]leucine intraduodenal infusion. Intracellular chylomicron, VLDL, low density lipoprotein (LDL), and HDL fractions were isolated and found to contain apoB, and apoA-IV, and apoA-I. In the fasted animal, less than 10% of total intracellular apoB and apoA-I was bound to lipoproteins and 7% of apoB and 35% of apoA-I was contained in the d 1.21 g/ml infranatant. The remainder of intracellular apolipoprotein was in the pellets of centrifugation. Lipid feeding doubled the percentage of intracellular apoA-I bound to lipoproteins and increased the percentage of intracellular apoB bound to lipoproteins by 65%. Following lipid feeding, the most significant increase was in the chylomicron apoB and HDL apoA-I fractions. These data suggest that in the fasting state, 90% of intracellular apoB and apoA-I is not bound to lipoproteins. Lipid feeding shifts intracellular apolipoprotein onto lipoproteins, but most intracellular apolipoprotein remains non-lipoprotein bound. The constant presence of a large non-lipoprotein-bound pool suggests that apolipoprotein synthesis is not the rate limiting step in lipoprotein assembly or secretion
— id: 18981, year: 1988, vol: 29, page: 1107, stat: Journal Article,

Apolipoprotein A-IV synthesis in rat intestine: regulation by dietary triglyceride
Apfelbaum TF; Davidson NO; Glickman RM
1987 May;252(5 Pt 1):G662-G666, American journal of physiology. Gastrointestinal & liver physiology
Apolipoprotein A-IV (apoA-IV) synthesis rates were measured in vivo in rat enterocytes by immunoprecipitation after administration of [3H]leucine into in situ loops of jejunum and ileum. Basal apoA-IV synthesis rates (percent total protein synthesis) were significantly higher in jejunal enterocytes (2.05 +/- 0.54%) compared with ileal enterocytes (0.48 +/- 0.32%) from the same fasted animals. After an acute triglyceride bolus, significant and sustained elevations of apoA-IV synthesis rates were seen in both jejunal and ileal enterocytes with maximal effects noted at 4-6 h. Animals fed diets containing 30% wt/wt triglyceride as saturated (SF) or polyunsaturated (UF) fats for 6 wk had similarly increased rates of apoA-IV synthesis in jejunal enterocytes with both SF (3.73 +/- 0.83%) and UF (3.33 +/- 0.64%) but no change in ileal enterocytes. By contrast, animals consuming a fat-free diet for 3 wk had jejunal apoA-IV synthesis rates indistinguishable from basal values (2.40 +/- 0.45%). Translatable intestinal mRNA levels for pre-apoA-IV after triglyceride increased in parallel to synthesis rates with a 50% increase in jejunum and a 350% increase in ileum observed at 4-6 h. These results suggest that apoA-IV synthesis by rat small intestine increases in response to acute and chronic dietary triglyceride, is maintained in the absence of dietary triglyceride, and may be under pretranslational control
— id: 18984, year: 1987, vol: 252, page: G662, stat: Journal Article,

A method to screen apolipoprotein polymorphisms in whole plasma: description of apolipoprotein A-IV variants in dyslipidemias and a reassessment of apolipoprotein A-I in Tangier disease
Bisgaier CL; Lee ES; Glickman RM
1987 Apr 24;918(3):242-249, Biochimica & biophysica acta
A sensitive and rapid immunological detection method was used to screen for apolipoprotein A-IV variants. Antibodies to human lymph chylomicron or plasma apolipoprotein A-IV, and plasma apolipoprotein A-I were raised in rabbits. Antibodies to apolipoprotein A-I or apolipoprotein A-IV were shown to be monospecific to their respective antigens by reactivity against human chylomicron apolipoproteins by immunoblot analysis. Plasma samples were obtained from dyslipidemic subjects from the Lipid Research Clinic of Columbia University. The plasma samples were isoelectrically focused (pH 4-6) on slab gels. Plasma proteins were then transferred to nitrocellulose paper for immunoblotting. Apolipoprotein A-IV polymorphism was determined by specific immunological detection of apolipoprotein A-IV. Identical apolipoprotein A-IV isoprotein patterns were observed when either antibodies to lymph or plasma apolipoprotein A-IV were used for immunoblotting. All the dyslipidemic plasma samples screened contained the two major and one or two minor isoproteins of normal plasma. In two instances, new apolipoprotein A-IV variants having an additional isoform were detected. One subject was hypertriglyceridemic (triacylglycerols = 342 mg/dl, cholesterol = 251 mg/dl) and had an additional major acidic apolipoprotein A-IV isoform. Another subject with mild hypocholesterolemia (triacylglycerols = 209 mg/dl, cholesterol = 120 mg/dl) was found to have additional major and minor basic apolipoprotein A-IV isoforms. The specificity of this technique allows detection of polymorphism of apolipoproteins of similar isoelectric points by use of a single dimension isoelectric focusing gel. This technique also demonstrated the presence of altered apolipoprotein A-I isoforms in the plasma of a patient with Tangier disease. These isoforms were previously identified as isoforms 2 and 4 of normal plasma by use of two-dimensional gel electrophoresis. However, by use of this new technique and careful evaluation of previously published two-dimensional gels, we now identify these apolipoprotein A-I isoforms as being more acidic than those of normal plasma
— id: 18985, year: 1987, vol: 918, page: 242, stat: Journal Article,

Effect of lecithin:cholesterol acyltransferase on distribution of apolipoprotein A-IV among lipoproteins of human plasma
Bisgaier CL; Sachdev OP; Lee ES; Williams KJ; Blum CB; Glickman RM
1987 Jun;28(6):693-703, Journal of lipid research
The effect of cholesterol esterification on the distribution of apoA-IV in human plasma was investigated. Human plasma was incubated in the presence or absence of the lecithin:cholesterol acyltransferase (LCAT) inhibitor 5,5-dithiobis(2-nitrobenzoic acid) (DTNB) and immediately fractionated by 6% agarose column chromatography. Fractions were monitored for apoA-IV, apoE, and apoA-I by radioimmunoassay (RIA). Incubation resulted in an elevated plasma concentration of cholesteryl ester and in an altered distribution of apoA-IV. After incubation apoA-IV eluted in the ordinarily apoA-IV-poor fractions of plasma that contain small VLDL particles, LDL, and HDL2. Inclusion of DTNB during the incubation resulted in some enlargement of HDL; however, both cholesterol esterification and lipoprotein binding of apoA-IV were inhibited. Addition of DTNB to plasma after incubation and prior to gel filtration had no effect on the apoA-IV distribution when the lipoproteins were immediately fractionated. Fasting plasma apoE was distributed in two or three peaks; in some plasmas there was a small peak that eluted with the column void volume, and, in all plasmas, there were larger peaks that eluted with the VLDL-LDL region and HDL2. Incubation resulted in displacement of HDL apoE to larger lipoproteins and this effect was observed in the presence or absence of DTNB. ApoA-I was distributed in a single broad peak that eluted in the region of HDL and the gel-filtered distribution was unaffected by incubation either in the presence or absence of DTNB. Incubation of plasma that was previously heated to 56 degrees C to inactivate LCAT resulted in no additional movement of apoA-IV onto lipoproteins, unless purified LCAT was present during incubation. The addition of heat-inactivated LCAT to the incubation, had no effect on movement of apoA-IV. These data suggest that human apoA-IV redistribution from the lipoprotein-free fraction to lipoprotein particles appears to be dependent on LCAT action. The mechanism responsible for the increased binding of apoA-IV to the surface of lipoproteins when LCAT acts may involve the generation of 'gaps' in the lipoprotein surface due to the consumption of substrate from the surface and additional enlargement of the core. ApoA-IV may bind to these 'gaps,' where the packing density of the phospholipid head groups is reduced
— id: 18983, year: 1987, vol: 28, page: 693, stat: Journal Article,

Intestinal apolipoprotein A-I and B-48 metabolism: effects of sustained alterations in dietary triglyceride and mucosal cholesterol flux
Davidson NO; Magun AM; Brasitus TA; Glickman RM
1987 Apr;28(4):388-402, Journal of lipid research
In recent studies (1985. J. Lipid Res. 26:368-379 and 1986. J. Lipid Res. 27:30-39) we characterized aspects of synthesis of rat intestinal apolipoproteins (apo) A-I and B-48 in vivo, and their short term regulation by dietary and biliary lipid flux. We now report studies extending these observations to the effects on intestinal apoA-I and apoB-48 metabolism of sustained (3 or 6 weeks) isocaloric intake of diets containing 0-30% (by weight) triglyceride, the latter as either butter fat (saturated) or corn oil (polyunsaturated). Additional studies were conducted to determine, separately, the effects of perturbations of intestinal mucosal cholesterol flux and hypothyroidism on intestinal apoA-I and apoB-48 metabolism. Intestinal synthesis (% total protein) of apoA-I and apoB-48 was not influenced by either dietary triglyceride quantity or quality (saturated vs. polyunsaturated fat); the values that were obtained were strictly comparable to those of both chow-fed animals and animals maintained for 3 weeks on fat-free chow. Intestinal apoA-I synthesis was not influenced by either acute or chronic perturbations of mucosal cholesterol flux. Hypothyroid rats demonstrated a 50% suppression of jejunal apoA-I synthesis. Intestinal synthesis of apoB-48, by contrast, appeared to undergo regulation by chronic (but not acute) perturbations of mucosal cholesterol flux. Maneuvers that augmented intestinal cholesterol uptake (particularly hypothyroidism) appeared to suppress intestinal apoB-48 synthesis by over 40%, while Surfomer (AOMA) administration reduced cholesterol absorption (control, 54 +/- 7%; AOMA, 26 +/- 8%; P less than 0.0005) and resulted in a 24% increase in apoB-48 synthesis by jejunal enterocytes. Intracellular intestinal lipoproteins demonstrated marked cholesteryl ester enrichment of the triglyceriderich lipoprotein fractions in hypercholesterolemic, hypothyroid rats. When all the groups were compared, cholesterol absorption (used as an index of mucosal cholesterol uptake) was negatively correlated with jejunal apoB-48 synthesis (r = -0.92, P less than 0.05). The data suggest that regulation of rat intestinal apoA-I and apoB-48 metabolism is independent of triglyceride flux. It is further concluded that an important regulatory effect of mucosal cholesterol flux can be demonstrated on enterocyte apoB-48 synthesis. Finally, the data suggest the additional possibility that circulating levels of thyroid hormone may exert an independent effect on the expression of rat intestinal apolipoproteins A-I and B-48
— id: 18986, year: 1987, vol: 28, page: 388, stat: Journal Article,

Inflammatory bowel disease: ulcerative colitis and Crohn's disease
Glickman RM
Harrison's principles of internal medicine New York : McGraw-Hill, 1987,
— id: 3896, year: 1987, vol: , page: 1277, stat: Chapter,

Abdominal swelling and ascites
Glickman RM; Isselbacher KJ
Harrison's principles of internal medicine New York : McGraw-Hill, 1987,
— id: 3895, year: 1987, vol: , page: 188, stat: Chapter,

Apolipoprotein B synthesis in rat small intestine: regulation by dietary triglyceride and biliary lipid
Davidson NO; Kollmer ME; Glickman RM
1986 Jan;27(1):30-39, Journal of lipid research
Apolipoprotein B (apoB) synthesis rates have been determined, in vivo, in rat enterocytes. Following intralumenal administration of a pulse of [3H]leucine, newly synthesized apoB was quantitated by specific immunoprecipitation and compared to [3H]leucine incorporation into total, trichloroacetic acid-insoluble protein. ApoB synthesis rates were determined after acute administration of either 0.1 or 1 g of triglyceride to fasting animals. No differences were found at any time from 90 min to 6 hr after challenge and values were not different from the basal values established in fasted controls. Animals rechallenged with triglyceride after 8 days' intake of fat-free chow also failed to demonstrate a change in intestinal apoB synthesis rate. By contrast, enterocyte content of apoB appeared to fall, temporarily, with the onset of active triglyceride flux. Groups of animals were then subjected to external bile diversion for 48 hr, a maneuver designed to remove all lumenal sources of lipid. Jejunal apoB synthesis rates fell by 43% (from 0.76% +/- 0.14 to 0.43% +/- 0.12, P less than 0.001), a change that was completely prevented by continuous replacement with 10 mM Na taurocholate. The suppression of jejunal apoB synthesis, induced by prolonged bile diversion, was reversed after 14 hr, but not 8 hr, of intralumenal perfusion with 10 mM Na taurocholate. The addition of micellar fatty acid-monoolein to the perfusate for 4 hr produced no further change in apoB synthesis. Ileal apoB synthesis rates fell by 70% (from 0.61% +/- 0.15 to 0.18% +/- 0.10, P less than 0.001) following 48 hr external bile diversion, a change that was only partially prevented by continuous bile salt replacement. These results suggest that jejunal apoB synthesis demonstrates bile salt dependence but not regulation by acute triglyceride flux. The data further suggest that key aspects of the regulation of apoB synthesis by cellular lipid flux may be mediated independently in jejunal and ileal enterocytes
— id: 18988, year: 1986, vol: 27, page: 30, stat: Journal Article,

High-density lipoprotein formation by the intestine
Glickman RM; Magun AM
1986 ;129(1):519-536, Methods in enzymology
— id: 18989, year: 1986, vol: 129, page: 519, stat: Journal Article,

Apolipoprotein B synthesis by human liver and intestine in vitro
Glickman RM; Rogers M; Glickman JN
1986 Jul;83(14):5296-5300, Proceedings of the National Academy of Sciences of the United States of America
The synthesis of apolipoprotein B (apoB) was examined in human fetal and adult intestine and liver. Intestine and liver were minced and then incubated with [3H]leucine, homogenized, and subjected to immunoprecipitation with antiserum that recognized both apoB-100 and apoB-48 (forms of apoB found in low density lipoproteins and in chylomicrons, respectively). Immunoprecipitates of fetal and adult liver contained radioactivity in a single apoB-100 peak when examined by NaDodSO4/polyacrylamide gel electrophoresis. Intestine from fetuses at 11 weeks of gestation incorporated radioactivity mainly into apoB-100, with little incorporation into apoB-48. Sixteen-week fetal intestine showed both apoB-100 and apoB-48, whereas adult intestine incorporated radioactivity only into apoB-48. Pulse-chase experiments with 11- and 16-week fetal intestine showed no evidence for the conversion of apoB-100 to apoB-48. Incubation of intestinal homogenates with fetal liver apoB-100 did not result in the conversion of apoB-100 to smaller forms of apoB. A cDNA probe to hepatic apoB-100 identified a single, 18-kilobase transcript in poly(A)+ RNA from fetal and adult liver and fetal intestine of all ages. These studies define the developmental pattern of apoB synthesis in human fetal and adult liver and intestine. No evidence could be found for the conversion of apoB-100 to apoB-48. The finding of a single mRNA transcript despite the form of apoB synthesized in each tissue is discussed
— id: 18987, year: 1986, vol: 83, page: 5296, stat: Journal Article,

Evaluation of anesthetic agents on human mucous membrane: an illustration of experimental protocol using computers
Greenfield, W; Hittelman, E L; Glickman, R
1986 Oct;52(8):22-28, New York state dental journal
— id: 91146, year: 1986, vol: 52, page: 22, stat: Journal Article,

Intraosseous high-grade mucopidermoid carcinoma with four potential microscopic diagnoses
Pierri, L K; Schneider, K L; Super, S; Glickman, R; Salman, L; Yamane, G; Chaudhry, A P
1986 Jan-Mar;41(1):47-50, Journal of oral medicine
— id: 106390, year: 1986, vol: 41, page: 47, stat: Journal Article,

Effect of saturated and unsaturated lipid on the composition of mesenteric triglyceride-rich lipoproteins in the rat
Renner F; Samuelson A; Rogers M; Glickman RM
1986 Jan;27(1):72-81, Journal of lipid research
The effect of saturated and unsaturated lipids on the composition of mesenteric lymph triglyceride-rich lipoproteins was studied in rats. A short-term steady-state infusion model was developed in mesenteric lymph fistula rats. Micellar solutions of linoleate, oleate, or palmitate were infused intraduodenally. Steady-state conditions of lymph flow, triglyceride, and apoA-I and apoB secretion rates were achieved in hours 3-5 after the start of the infusion. During this steady-state period, triglyceride-rich lipoproteins were prepared and characterized. With lipid infusion there were the expected increases in secretion rates of triglyceride, apoB, and apoA-I both in whole lymph and in the d less than 1.006 g/ml lipoproteins. Compositional analysis of d less than 1.006 g/ml lipoproteins revealed no difference in the ratios of phospholipid or apoA-I (surface) to triglyceride (core) constituents between saturated and unsaturated lipids, suggesting a similar particle size. This was directly verified by agarose gel filtration and electron microscopy carried out at 27 degrees C, which showed no difference in particle size between linoleate and palmitate chylomicrons. When these lipoproteins were prepared at 4 degrees C, palmitate lipoproteins exhibited dramatically changed gel filtration elution profiles, suggesting a shift to smaller or at least distorted particles and questioning earlier results suggesting a smaller size for saturated fat d less than 1.006 g/ml lipoproteins. Despite the similarity of size between saturated and unsaturated chylomicrons, the apoB content of unsaturated linoleate chylomicrons was significantly lower than that of palmitate chylomicrons. This difference was present whether chylomicrons were prepared by centrifugation or by gel filtration. The clearance of palmitate chylomicrons from the circulation of recipient rats was slightly more rapid than that of linoleate chylomicrons. The mechanism for this apparently selective increase in the apoB content of saturated fat chylomicrons is unknown but the present studies suggest that these changes may be of physiologic significance, perhaps relating to the potential atherogenicity of saturated lipids
— id: 18990, year: 1986, vol: 27, page: 72, stat: Journal Article,

Differential regulation of jejunal and ileal apoA-IV synthesis by dietary triglyceride
Apfelbaum TF; Davidson NO; Glickman RM
1985 ;5:534A-534A, Arteriosclerosis
— id: 62856, year: 1985, vol: 5, page: 534A, stat: Journal Article,

Distribution of apolipoprotein A-IV in human plasma
Bisgaier CL; Sachdev OP; Megna L; Glickman RM
1985 Jan;26(1):11-25, Journal of lipid research
Human apoA-IV was purified from delipidated urinary chylomicrons. Monospecific antibodies were raised in rabbits and used to develop a double antibody radioimmunoassay (RIA). Displacement of 125I-labeled apoA-IV by plasma or purified chylomicron apoA-IV resulted in parallel displacement curves, indicating that apoA-IV from both sources share common antigenic determinants. The apoA-IV level in plasma from normal healthy fasting male subjects (n = 5) was 37.4 +/- 4.0 mg/dl, while fat-feeding increased the level to 49.1 +/- 7.9 mg/dl (P less than 0.05) at 4 hr. The apoA-IV level in plasma from abetalipoproteinemic fasting subjects was 13.7 +/- 3.1 mg/dl (n = 5). Plasma from a single fasting Tangier subject showed a reduced apoA-IV level of 21.1 mg/dl. The distribution of apoA-IV in fasting and postprandial plasma was determined by 6% agarose gel chromatography. Fifteen to 25% of plasma apoA-IV eluted in the region of plasma high density lipoprotein (HDL), with the remainder eluting in subsequent column fractions. In abetalipoproteinemic plasma this HDL fraction is reduced and lacks apoA-IV, suggesting that at least some of the apoA-IV on these particles is normally derived from triglyceride-rich lipoproteins. Lipemic plasma from a fat-fed subject showed a small rise (3%) in chylomicron-associated apoA-IV. Gel-filtered HDL and subsequent apoA-IV-containing fractions were subjected to 4-30% polyacrylamide gradient gel electrophoresis (4/30 GGE), and apoA-IV was identified by immunolocalization following transfer of proteins to nitrocellulose paper. In normal plasma apoA-IV was localized throughout all HDL fractions. In addition, normal plasma contained apoA-IV localized in a small particle (diameter 7.8-8.0 nm). This particle also contained apoA-I and lipid. A markedly elevated saturated to unsaturated cholesteryl ester ratio was present in gel-filtered plasma fractions containing small HDL, suggesting an intracellular origin of these particles. In abetalipoproteinemic plasma apoA-IV was absent from all HDL fractions except for the small HDL particles, suggesting that they are not derived from the surface of triglyceride-rich particles. All plasmas contained free apoA-IV. In contrast to gel-filtered plasma, lipoprotein subfractions of fasted normal plasma prepared in the ultracentrifuge primarily contained apoA-IV in the d greater than 1.26 g/ml fraction, suggesting an artifactual redistribution of the apolipoprotein during centrifugation. Overall, these data suggest that apoA-IV secretion into plasma is increased with fat feeding, and that apoA-IV normally exists as both a free apolipoprotein and in association with HDL particles
— id: 18994, year: 1985, vol: 26, page: 11, stat: Journal Article,

Apolipoprotein A-I synthesis in rat small intestine: regulation by dietary triglyceride and biliary lipid
Davidson NO; Glickman RM
1985 Mar;26(3):368-379, Journal of lipid research
Techniques were developed to provide direct quantitation of apolipoprotein A-I (apoA-I) synthesis rates in rat small intestine. Following intralumenal administration of a pulse of [3H]leucine, newly synthesized enterocyte apoA-I was quantitated by specific immunoprecipitation and compared to [3H]leucine incorporation into total trichloroacetic acid-precipitable protein. ApoA-I synthesis rates (% total protein) were found to be significantly higher in jejunal enterocytes (1.84 +/- 0.20) compared to ileal enterocytes (0.91 +/- 0.25) from the same, fasting, animals, P less than 0.01. It was found that rats consuming regular (4.5% w/w fat) rodent chow had apoA-I synthesis rates, 30 to 240 min after receiving an intraduodenal bolus of 100 mg of triglyceride, that were indistinguishable from control animals receiving either saline or an isocaloric, but fat-free, enteral preparation. By contrast, animals consuming a fat-free chow for 8 days prior to study had a small but significant response to acute reintroduction of dietary triglyceride. Four hours after 100 mg of triglyceride was administered, jejunal apoA-I synthesis (% total protein) was 1.84 +/- 0.1 compared to 1.37 +/- 0.04 for animals exposed to an isocaloric, fat-free enteral preparation, P less than 0.01. External bile diversion for 48 hr, which effectively removed all lumenal sources of lipid, reduced apoA-I synthesis in jejunal enterocytes but produced no more depression than that found in sham-operated controls infused for 48 hr with dextrosesaline or control animals fasted for 30 hr. By contrast, apoA-I synthesis in ileal enterocytes was reduced significantly by external bile diversion (0.59 +/- 0.20) in comparison to sham-operated controls (1.19 +/- 0.32) P less than 0.01. Continuous infusion of 10 mM Na taurocholate for 48 hr or 10 mM Na taurocholate for 44 hr and 80 mg of micellar lipid for 4 hr produced results similar to those obtained by bile diversion alone (0.56 +/- 0.2 and 0.61 +/- 0.25, respectively) suggesting that bile salt deficiency alone was not responsible for the observed depression in ileal apoA-I synthesis. These results suggest that, under conditions of physiological dietary triglyceride intake, apoA-I synthesis in jejunal enterocytes is not actuely regulated by changes in triglyceride flux. After prolonged dietary triglyceride withdrawal, the reintroduction of fat produces a small, but significant, increase in jejunal apoA-I synthesis. The data further suggest that apoA-I synthesis in jejunal enterocytes is regulated in part by the availability of lumenal lipid, but that the presence of bile does not exert an additional level of control.(ABSTRACT TRUNCATED AT 400 WORDS)
— id: 18992, year: 1985, vol: 26, page: 368, stat: Journal Article,

Malabsorption : pathophysiology and diagnosis
Glickman RM
Cecil textbook of medicine Philadelphia : Saunders, 1985,
— id: 3903, year: 1985, vol: , page: 719, stat: Chapter,

The future of the physician scientist. Presidential address delivered before the 76th annual meeting of the American Society for Clinical Investigation, Washington, DC, 4 May 1985
Glickman RM
1985 Oct;76(4):1293-1296, Journal of clinical investigation
— id: 18991, year: 1985, vol: 76, page: 1293, stat: Journal Article,

Isolation of high density lipoproteins from rat intestinal epithelial cells
Magun AM; Brasitus TA; Glickman RM
1985 Jan;75(1):209-218, Journal of clinical investigation
Previous studies have defined forms of high density lipoproteins (HDL) in rat mesenteric lymph, suggesting that they have a secretory origin. This study describes the isolation and characterization of intestinal intracellular HDL. Two preparations were made as follows: (a) Rat enterocytes were isolated and a Golgi organelle fraction was prepared. (b) Cell homogenates were subjected to nitrogen cavitation and a cytoplasmic fraction was prepared. Lipoproteins were isolated from both preparations by sequential ultracentrifugation. When the HDL fraction (1.07-1.21 g/ml) was subjected to isopyknic density gradient ultracentrifugation, a peak of apoproteins A-I and B (apoA-I and apoB, respectively) was found at a density of 1.11-1.14 g/ml. Electron microscopy of the fraction showed spherical particles ranging in size from 6 to 13 nm. Immunoelectrophoresis revealed a precipitin arc in the alpha region against apoA-I which extended into the pre-beta region where a precipitin arc against apoB was also seen. ApoB antisera depleted the pre-beta particles whereas the alpha migrating particles remained. Lipid analysis of the whole HDL fraction revealed phospholipid, cholesteryl ester, and triglyceride as the major lipids. [3H]leucine was then administered into the duodenum and a radiolabeled intracellular HDL fraction was isolated. The newly synthesized apoproteins of the HDL fraction, as determined by gel electrophoresis, were apoB, apoA-I, and apolipoprotein A-IV (ApoA-IV). Immunoprecipitation of the apoB particles revealed apoA-I and apoA-IV in the supernatant. These data demonstrate that there are at least two intracellular intestinal forms of HDL particles, one of which contains apoB. The other particle contains apoA-I and apoA-IV, has alpha mobility, is spherical, and resembles a particle found in the lymph
— id: 18993, year: 1985, vol: 75, page: 209, stat: Journal Article,

Intracellular intestinal apoprotein distribution is altered by lipid feeding
Magun AM; Russel DA; Davidson NO; Glickman RM
1985 ;5:533A-533A, Arteriosclerosis
— id: 62857, year: 1985, vol: 5, page: 533A, stat: Journal Article,

Intestinal synthesis (SYN) of apoA-I (A-I) and B-48 is independently regulated by triglyceride (TG) and bile salt flux
Davidson NO; Glickman RM; Kollmer ME
1984 ;70:II.120-II.120, Circulation
— id: 62872, year: 1984, vol: 70, page: II.120, stat: Journal Article,

Apoprotein A-I (apoA-I) synthesis in rat small intestine: effects of prolonged exposure to high saturated (SF) or polyunsaturated (UF) fat diets
Davidson NO; Kollmer ME; Brasitus TA; Glickman RM
1984 ;86:II.1058-II.1058, Gastroenterology
— id: 62854, year: 1984, vol: 86, page: II.1058, stat: Journal Article,

Fat absorption and malabsorption
Glickman RM
The role of the gastrointestinal tract in nutrient delivery Orlando : Academic Press, 1984,
— id: 3907, year: 1984, vol: , page: 145, stat: Chapter,

Review of five textbooks of internal medicine
Glickman RM
1984 ;311:1324-1326, New England journal of medicine
— id: 62846, year: 1984, vol: 311, page: 1324, stat: Journal Article,

Absorption and malabsorption of nutrients
Glickman RM; Brasitus TA
1984 ;1:144-157, Gastroenterology annual
— id: 62844, year: 1984, vol: 1, page: 144, stat: Journal Article,

Biosynthesis of human preapolipoprotein A-IV
Gordon JI; Bisgaier CL; Sims HF; Sachdev OP; Glickman RM; Strauss AW
1984 Jan 10;259(1):468-474, Journal of biological chemistry
The primary translation product of human intestinal apolipoprotein A-IV mRNA was purified from ascites and wheat germ cell-free systems. Comparison of its NH2-terminal sequence with mature, chylomicron-associated apo-A-IV revealed that apo-A-IV was initially synthesized with a 20-amino acid long NH2-terminal extension: Met-X-Leu-X-Ala-Val-Val-Leu-X-Leu-Ala-Leu-Val-Ala-Val-Ala-Leu-X-X-Ala. Co-translational cleavage of the cell-free product as well as Edman degradation of the stable intracellular form of the protein recovered from Hep G2 cells indicated that this entire 20-amino acid sequence behaved as a signal peptide. There is at least 55% sequence homology between the rat and human apo-A-IV signal peptides and 33% homology between the human A-I and A-IV presegments. Agarose gel chromatography of Hep G2 culture media indicated that neither apo-A-IV nor -A-I is associated with particles that have physical properties resembling any of the plasma lipoprotein density classes. Incubation of plasma with Hep G2 media resulted in transfer of A-I but not A-IV to lipoproteins. Since the NH2 termini of co-translationally cleaved and chylomicron-associated apo-A-IV are identical, it is apparent that 1) this polypeptide does not undergo NH2-terminal post-translational proteolysis like proapo-A-II or proapo-A-I, and 2) regulation of A-IV-lipoprotein interaction is not dependent on any NH2-terminal proteolytic processing event
— id: 18995, year: 1984, vol: 259, page: 468, stat: Journal Article,

Plasma distribution of apoliprotein A-IV in acquire LCAT deficiency
Sachdev OP; Bisgaier CL; Glickman RM
1984 ;4:546A-547A, Arteriosclerosis
— id: 62855, year: 1984, vol: 4, page: 546A, stat: Journal Article,

Intestinal synthesis, secretion, and transport of lipoproteins
Bisgaier CL; Glickman RM
1983 ;45(2):625-636, Annual review of physiology
— id: 18998, year: 1983, vol: 45, page: 625, stat: Journal Article,

Apoprotein A-IV distribution in human plasma
Bisgaier CL; Sachdev OP; Megna L; Glickman RM
1983 ;68(Suppl III):215A-215A, Circulation
— id: 62870, year: 1983, vol: 68, page: 215A, stat: Journal Article,

Lipid absorption in man
Davidson NO; Glickman RM
1983 ;4:57-75, Progress in gastroenterology
— id: 62842, year: 1983, vol: 4, page: 57, stat: Journal Article,

Regulation of apoprotein A-I (apoA-I) synthesis in rat small intestine (S.I.)
Davidson NO; Glickman RM
1983 ;68(Suppl. III):213-213, Circulation
— id: 62871, year: 1983, vol: 68, page: 213, stat: Journal Article,

Rat intestine secretes spherical high density lipoproteins
Forester GP; Tall AR; Bisgaier CL; Glickman RM
1983 May 10;258(9):5938-5943, Journal of biological chemistry
— id: 18996, year: 1983, vol: 258, page: 5938, stat: Journal Article,

Small spherical high density lipoproteins from rat intestinal cells
Forester GP; Tall AR; Glickman RM
1983 May;84:1157-1157, Gastroenterology
— id: 62853, year: 1983, vol: 84, page: 1157, stat: Journal Article,

Fat absorption and malabsorption
Glickman RM
1983 May;12(2):323-334, Clinics in gastroenterology
— id: 18997, year: 1983, vol: 12, page: 323, stat: Journal Article,

Inflammatory bowel disease: ulcerative colitis, Crohn's disease
Glickman RM
Harrison's principles of internal medicine New York : McGraw-Hill, 1983,
— id: 3894, year: 1983, vol: , page: 1738, stat: Chapter,

Absorption and malabsorption of nutrients
Glickman RM; Brasitus TA
1983 ;1:127-147, Gastroenterology annual
— id: 62843, year: 1983, vol: 1, page: 127, stat: Journal Article,

Abdominal swelling and ascites
Glickman RM; Isselbacher KJ
Harrison's principles of internal medicine New York : McGraw-Hill, 1983,
— id: 3893, year: 1983, vol: , page: 209, stat: Chapter,

Isolation of high density lipoproteins from rat intestinal cells
Magun AM; Brasitus TA; Glickman RM
1983 ;31:503A-503A, Clinical research
— id: 62863, year: 1983, vol: 31, page: 503A, stat: Journal Article,

Effect of biliary diversion on rat mesenteric lymph apolipoprotein-I and high density lipoprotein
Bearnot HR; Glickman RM; Weinberg L; Green PH; Tall AR
1982 Jan;69(1):210-217, Journal of clinical investigation
— id: 19000, year: 1982, vol: 69, page: 210, stat: Journal Article,

Radioimmunoassay of rat apoprotein A-I with monoclonal antibodies
Bisgaier CL; Davidson N; Chess L; Irigoyen O; Glickman RM
1982 ;41:598-598, Federation Proceedings (Federation of American Societies for Experimental Biology)
— id: 62864, year: 1982, vol: 41, page: 598, stat: Journal Article,

Intestinal HDL: composition and origin of a small spherical particle
Forester GP; Tall AR; Bisgaier CL; Glickman RM
1982 ;82:1059-1059, Gastroenterology
— id: 62852, year: 1982, vol: 82, page: 1059, stat: Journal Article,

Malabsorption
Glickman RM
Cecil textbook of medicine Philadelphia : Saunders, 1982,
— id: 3902, year: 1982, vol: , page: 678, stat: Chapter,

Lipoprotein metabolism
Glickman RM; Sabesin SM
Liver : biology and pathobiology New York : Raven Press, 1982,
— id: 3899, year: 1982, vol: , page: 123, stat: Chapter,

Apolipoprotein localization and quantitation in the human intestine
Green PH; Lefkowitch JH; Glickman RM; Riley JW; Quinet E; Blum CB
1982 Dec;83(6):1223-1230, Gastroenterology
Apolipoproteins B, A-I, and A-IV were localized in human intestinal epithelium using immunoperoxidase techniques. Staining was most obvious in villus tip cells. Lipid absorption resulted in an increase in intraepithelial staining for each apoprotein. The pattern for apo-B in the biopsy specimens taken after lipid absorption revealed a marked redistribution of staining to the intercellular spaces and an increase in the supranuclear staining of apo-A-I and apo-A-IV. After lipid absorption, staining appeared to extend further down the villus than in the fasting biopsy specimens. Quantitation of apo-A-I and apo-A-IV in isolated epithelial cells confirmed that the mass of these apoproteins increases in response to lipid absorption. Apolipoprotein B and apo-A-I were absent in the epithelium of 3 patients with abetalipoproteinemia while apo-A-IV was present in 2 patients. These studies demonstrate differences in the localization and quantitation of apoproteins in the villus-crypt unit as well as differences in the localization pattern of the different apoproteins
— id: 18999, year: 1982, vol: 83, page: 1223, stat: Journal Article,

Intestinal lipoprotein metabolism
Green PH; Glickman RM
1981 Nov;22(8):1153-1173, Journal of lipid research
— id: 19001, year: 1981, vol: 22, page: 1153, stat: Journal Article,

Effect of bile diversion on intestinal apoA-I production
Bernot HR; Green PHR; Glickman RM; Tall AR; Riley JW
1980 ;78:1138-1138, Gastroenterology
— id: 62851, year: 1980, vol: 78, page: 1138, stat: Journal Article,

Intestinal fat absorption
Glickman RM
1980 ;9(4):29-41, Current concepts in nutrition
— id: 19006, year: 1980, vol: 9, page: 29, stat: Journal Article,

Intestinal lipoprotein formation
Glickman RM
1980 ;24 Suppl 1(4):3-11, Nutrition & metabolism
The average western diet contains approximately 40% of total calories as dietary fat or approximately 100 g of fat. The efficiency of the entire process of fat absorption can be judged by the fact that under normal conditions less than 5% of ingested fat is recovered in the stool. In the past several years, new concepts have greatly added to our understanding of the process by which dietary fat is digested, absorbed and processed in the intestinal epithelial cell for delivery to the body via the intestinal lymph and the portal venous system. These newer concepts include an understanding of the physical chemistry of lipids, the physiology of bile salts and the formation and metabolisms of lipoprotein all directly influencing the process of fat absorption. The present discussion will emphasize the formation of lipoproteins within the intestinal mucosa. New information suggests that the small intestinal mucosa is a quantitatively important source of lipoprotein constituents for systemic lipoproteins. This is hardly surprising when one considers the large quantities of lipid transversing the intestinal mucosa each day which must exit in the form of lipoproteins
— id: 19005, year: 1980, vol: 24 Suppl 1, page: 3, stat: Journal Article,

Apoprotein secretion from the human intestine
Glickman RM; Green PHR
Atheroscleoris V New York : Springer Verlag, 1980,
— id: 3906, year: 1980, vol: , page: 160, stat: Chapter,

Abdominal swelling and ascites
Glickman RM; Isselbacher KJ
Harrison's principles of internal medicine New York : McGraw-Hill, 1980,
— id: 3892, year: 1980, vol: , page: 210, stat: Chapter,

Diseases of the small intestine
Glickman RM; Isselbacher KJ
Harrison's principles of internal medicine New York : McGraw-Hill, 1980,
— id: 3891, year: 1980, vol: , page: 1410, stat: Chapter,

Human apolipoprotein A-IV. Intestinal origin and distribution in plasma
Green PH; Glickman RM; Riley JW; Quinet E
1980 Apr;65(4):911-919, Journal of clinical investigation
— id: 19004, year: 1980, vol: 65, page: 911, stat: Journal Article,

The effect of chronic cholesterol feeding on intestinal lipoproteins in the rat
Riley JW; Glickman RM; Green PH; Tall AR
1980 Sep;21(7):942-952, Journal of lipid research
— id: 19002, year: 1980, vol: 21, page: 942, stat: Journal Article,

Products of delipidation of intestinal chylomicrons with diethyl ether
Tall AR; Abreu E; Glickman RM; Green PH; Riley JW
1980 Jun;36(2):223-239, Atherosclerosis
— id: 19003, year: 1980, vol: 36, page: 223, stat: Journal Article,

In memoriam. Daniel Victor Kimberg, 1933--1978
Field M; Glickman RM
1979 Nov;77(5):973-978, Gastroenterology
— id: 19008, year: 1979, vol: 77, page: 973, stat: Journal Article,

Immunofluorescence studies of apolipoprotein B in intestinal mucosa. Absence in abetalipoproteinemia
Glickman RM; Green PH; Lees RS; Lux SE; Kilgore A
1979 Feb;76(2):288-292, Gastroenterology
During fat absorption, active synthesis of cholesterol, phospholipids, and specific apolipoproteins are required for chylomicron formation and secretion. In the inherited disease abetalipoproteinema, chylomicrons cannot be made in response to fat feeding, and they as well as low and very low density lipoproteins are completely absent from plasma. The genetic defect in the disease is presumed to be an inability to synthesize apolipoprotein B, the apoprotein common to all the above lipoprotein classes, but such a defect has not been directly demonstrated. With peroral intestinal biopsies and immunofluorescence and intracellular localization of apolipoprotein B within jejunal epithelial cells of five normal subjects and have shown that its content increases markedly after fat feeding. In two patients with abetalipoproteinemia no apolipoprotein B was seen by immunofluorescence techniques in the jejunal mucosa in the fasting state or after a fatty meal. Intestinal synthesis of apolipoprotein B appears not to occur in abetalipoproteinemia
— id: 19011, year: 1979, vol: 76, page: 288, stat: Journal Article,

Human intestinal lipoproteins. Studies in chyluric subjects
Green PH; Glickman RM; Saudek CD; Blum CB; Tall AR
1979 Jul;64(1):233-242, Journal of clinical investigation
— id: 19010, year: 1979, vol: 64, page: 233, stat: Journal Article,

Human apoA-IV -- intestinal origin and distribution in plasma
Green PHR; Glickman RM; Riley JW
1979 ;59:II.119-II.119, Circulation
— id: 62868, year: 1979, vol: 59, page: II.119, stat: Journal Article,

Human apoprotein A-IV-intestinal origin
Green PHR; Glickman RM; Riley JW; Quinet E
1979 ;76:1143-1143, Gastroenterology
— id: 62849, year: 1979, vol: 76, page: 1143, stat: Journal Article,

Fat malabsorption--advances in our understanding
Riley JW; Glickman RM
1979 Dec;67(6):980-988, American journal of medicine
The intestinal absorption of triglyceride constitutes a multistep process with active involvement of the pancreatobiliary system, the intestine and lymphatics. It is only through the integrated function of these organs that dietary triglyceride can be efficiently absorbed and delivered to the peripheral blood for subsequent metabolism. In this review we discuss each aspect of triglyceride absorption and chylomicron formation and illustrate how various diseases may interfere with the process resulting in fat malabsorption. In addition, the role of the intestine as a major synthetic source of lipoprotein constituents for circulating lipoproteins is discussed
— id: 19007, year: 1979, vol: 67, page: 980, stat: Journal Article,

Effect of chronic cholesterol feeding on intestinal lipoproteins in the rat
Riley JW; Glickman RM; Green PHR; Tall AR
1979 ;76:1226-1226, Gastroenterology
— id: 62850, year: 1979, vol: 76, page: 1226, stat: Journal Article,

Abnormal lipoproteins in rate mesenteric lymph in response to chronic cholesterol feeding
Riley JW; Glickman RM; Tall AR; Green PHR
1979 ;59:II.32-II.32, Circulation
— id: 62869, year: 1979, vol: 59, page: II.32, stat: Journal Article,

Metabolic fate of chylomicron phospholipids and apoproteins in the rat
Tall AR; Green PH; Glickman RM; Riley JW
1979 Oct;64(4):977-989, Journal of clinical investigation
— id: 19009, year: 1979, vol: 64, page: 977, stat: Journal Article,

Apoprotein A-I synthesis in normal intestinal mucosa and in Tangier disease
Glickman RM; Green PH; Lees RS; Tall A
1978 Dec 28;299(26):1424-1427, New England journal of medicine
To determine whether human small intestine synthesizes apoA-I, the major apoprotein of plasma high-density lipoproteins, we used immunofluorescence technics and monospecific antiserums to visualize apoA-I within intestinal epithelial cells from four normal subjects and one patient with Tangier disease. Biopsies from all subjects during fasting showed limited fluorescence. After lipid feeding intracellular apoA-I markedly increased in both normal subjects and the patient. During alimentary lipemia, mean plasma apoA-I levels (milligrams per deciliter) increased in four normal subjects from 161 +/- 12 (+/- S.E.M.) to 180 +/- 15 (P less than 0.05) and in the patient from 1.9 to 6.8. Normal plasma chylomicrons contained apoB, apoE and the C peptides but not apoA-I. The patient's chylomicrons contained ap0A-I. Normal and Tangier-disease intestinal-mucosa cells increase their content of apoA-I during chylomicron formation and subsequently contribute to plasma apoA-I levels. The low levels of apoA-I in Tangier disease are not due to a failure of intestinal synthesis but might be due to abnormal metabolism of chylomicron apoproteins
— id: 19012, year: 1978, vol: 299, page: 1424, stat: Journal Article,

Intestinal synthesis of apoprotein A-I: normals and Tangier disease
Glickman RM; Green PHR; Lees RS
1978 ;26:497A-497A, Clinical research
— id: 62862, year: 1978, vol: 26, page: 497A, stat: Journal Article,

Studies of apoB in normal and abetalipoproteinemic intestinal epithelial cells
Glickman RM; Green PHR; Lees RS; Lux S
1978 ;74(5):1038-1038, Gastroenterology
— id: 62848, year: 1978, vol: 74, page: 1038, stat: Journal Article,

Chylomicron apoprotein localization within rat intestinal epithelium: studies of normal and impaired lipid absorption
Glickman RM; Kilgore A; Khorana J
1978 Feb;19(2):260-268, Journal of lipid research
— id: 19013, year: 1978, vol: 19, page: 260, stat: Journal Article,

Rat intestine secretes discoid high density lipoprotein
Green PH; Tall AR; Glickman RM
1978 Feb;61(2):528-534, Journal of clinical investigation
— id: 19014, year: 1978, vol: 61, page: 528, stat: Journal Article,

Intestinal lipoprotein secretion chyluiric man
Green PHR; Glickman RM; Saudek CD; Blum C; Tall AR
1978 ;5?:?-?, Circulation
— id: 62866, year: 1978, vol: 5?, page: ?, stat: Journal Article,

High density lipoproteins from chylomicrons
Tall AR; Green PHR; Glickman RM; Abreu E
1978 ;5?:?-?, Circulation
— id: 62867, year: 1978, vol: 5?, page: ?, stat: Journal Article,

Rat intestinal glycolipids. III. Fatty acids and long chain bases of glycolipids from villus and crypt cells
Bouhours JF; Glickman RM
1977 Apr 26;487(1):51-60, Biochimica & biophysica acta
Previous studies from this laboratory have demonstrated a striking difference in rat intestinal glycolipids between differentiated villus cells and immature crypt cells. Villus cells contained proportionally greater amounts of glucosylceramide and hematoside while crypt cells were deficient in hematoside, but contained proportionally greater amounts of trihexosylceramide. In order to further elucidate possible differences between villus and crypt cell glycolipids, a study of the sphingosine and fatty acids of rat intestinal glycolipids was conducted. Villus and crypt cells were separated from rat intestine and the glycolipids purified. Fatty acids and long chain bases of the three major glycolipids (glucosylceramide, trihexosylceramide, hematoside) extracted from these cells were characterized. Phytosphingosine accounted for 63-73% of the total long chain bases in all glycolipids whether from villus or crypt cells. Hydroxy fatty acids represented 70% of total fatty acids in the glucosylceramide and in the hematoside but accounted for only 30% in the trihexosylceramide. In addition, trihexosylceramide contained a larger percentage of fatty acids with 20-carbon atoms than glucosylceramide and hematoside isolated from villus cells. These fatty acids were more concentrated in crypt cells than in villus cells glycolipids. These results suggest that hematoside and trihexosylceramide, respectively abundant in villus and in crypt cells, may be derived from a different lactosylceramide precursor and further underscore differences in villus and crypt cell glycolipid synthesis
— id: 19016, year: 1977, vol: 487, page: 51, stat: Journal Article,

The intestine as a source of apolipoprotein A1
Glickman RM; Green PH
1977 Jun;74(6):2569-2573, Proceedings of the National Academy of Sciences of the United States of America
The major apoprotein of rat mesenteric lymph chylomicrons has been isolated and characterized and shown to be identical to apoprotein A1 (apo A1) isolated from serum high density lipoprotein (HDL). During intestinal lipid absorption, active synthesis of apo A1 was demonstrated by radioactive amino acid incorporation into lymph chylomicron A1 as well as lymph HDL. Immunofluorescence studies of intestinal epithelium demonstrated a marked increase in apo A1 fluorescence, confirming an active synthesis of this apoprotein during lipid absorption. Quantitative immunoelectrophoretic methods were used to measure apo A1 in lymph and peripheral blood during various conditions designed to estimate the quantitative importance of intestinal apo A1 to the levels of circulating lipoproteins. During lipid feeding there was an increase in lymph apo A1 that was associated with lymph lipoproteins (50%) of density less than 1.006 g/ml whereas in basal lymph most apo A1 (85%) was in the lipoproteins of density greater than 1.006 g/ml. Lipid feeding in animals without lymph fistulas resulted in a significant increase in serum apo A1 levels; biliary diversion, designed to eliminate intestinal lipoproteins of density less than 1.006 g/ml, resulted in a significant decrease in serum apo A1 levels. These studies demonstrate that the intestine actively synthesizes apo A1 and is a significant source of this apoprotein for circulating lipoproteins
— id: 19015, year: 1977, vol: 74, page: 2569, stat: Journal Article,

Abdominal swelling and ascites
Glickman RM; Isselbacher KJ
Harrison's principles of internal medicine New York : McGraw-Hill, 1977,
— id: 3890, year: 1977, vol: , page: 223, stat: Chapter,

Diseases of the small intestine
Glickman RM; Isselbacher KJ
Harrison's principles of internal medicine New York : McGraw-Hill, 1977,
— id: 3889, year: 1977, vol: , page: 1537, stat: Chapter,

The intestine as a source of apoprotein A-I
Green PHR; Glickman RM
1977 ;25:392A-392A, Clinical research
— id: 62861, year: 1977, vol: 25, page: 392A, stat: Journal Article,

Rat intestine secretes discoidal nascent HDL
Green PHR; Tall A; Glickman RM
1977 ;56:210-210, Circulation
— id: 62865, year: 1977, vol: 56, page: 210, stat: Journal Article,

Rat intestinal glycolipids. II. Distribution and biosynthesis of glycolipids and ceramide in villus and crypt cells
Bouhours JF; Glickman RM
1976 Jul 20;441(1):123-133, Biochimica & biophysica acta
Intestinal epithelial cells were isolated from rat intestine and grouped into villus and crypt cell fractions. Glycolipids were purified from each cell fraction and quantitated by fluorimetric determination of glycolipid sphingosine. Significant quantities of ceramide were found in all cell fractions and accounted for approximately 15% of total glycolipid sphingosine. While villus and crypt cell fractions quantitatively contained differing amounts of sphingosine, all cell fractions contained proportionally similar quantities of sphingosine when compared to cellular cholesterol or phospholipid. Individual glycolipids, however, showed significant differences in distribution between villus and crypt cells. Hematoside and glucosylceramide were proportionally increased in villus cells, while crypt cells showed an increase in trihexosylceramide and ceramide content. The rate of UDPglucose : hydroxy fatty acid ceramide glucosyltransferase was higher in villus cells while the rate of UDPgalactose : lactosylceramide galactosyltransferase was 3--4 times increased in crypt cells. These studies demonstrate that significant differences in both the distribution and biosynthesis of individual glycolipids occur in crypt and villus cells of rat intestine and are of possible importance in the process of intestinal cell differentiation
— id: 19018, year: 1976, vol: 441, page: 123, stat: Journal Article,

Chylomicron formation by the intestine
Glickman RM
Lipid absorption : biochemical and clinical aspects Baltimore : University Park Press, 1976,
— id: 3905, year: 1976, vol: , page: 99, stat: Chapter,

Characterization, distribution and biosynthesis of the major ganglioside of rat intestinal mucosa
Glickman RM; Bouhours JF
1976 Jan 22;424(1):17-25, Biochimica & biophysica acta
The major sialic acid containing glycolipid has been isolated from rat intestinal mucosa. Characterization of this ganglioside by thin layer and gas chromatographic analysis indicates that it is an hematoside (GM3) with the major portion of the sialic acid in the N-glycolyl form. The distribution of this ganglioside was determined in villus and crypt cells isolated from rat intestine. The hematoside content of crypt cells was found to be significantly decreased when compared to villus cells. CMP-sialic acid:lactosylceramide sialyltransferase, responsible for the sialylation of lactosylceramide, was measured in differentiated villus and undifferentiated crypt cells and found to be greatly reduced in the crypt cell fraction. The present study demonstrates that marked differences in ganglioside content and biosynthesis occur in contiguous populations of cells in varying states of differentiation when isolated from normal rat intestine
— id: 19020, year: 1976, vol: 424, page: 17, stat: Journal Article,

Localization of apolipoprotein B in intestinal epithelial cells
Glickman RM; Khorana J; Kilgore A
1976 Sep 24;193(4259):1254-1255, Science
Indirect immunofluorescence techniques were employed to determine the distribution within intestinal epithelial cells of apolipoprotein B, a protein essential for the normal transport of fat. Isolated intestinal cells were prepared from rats either during active lipid absorption or after biliary diversion. Specific immunofluorescence from an antiserum to apolipoprotein B was detected in the apical portion of epithelial cells from bile-diverted animals, demonstrating that a pool of apolipoprotein B is present in the nonabsorptive epithelial cell and may be a component of intestinal cell membranes. During lipid absorption in normal rats, an early and sustained increase in immunofluorescence was demonstrated, consistent with an increase synthesis of apolipoprotein B during lipid absorption. This study demonstrates the presence of apolipoprotein B within intestinal epithelium and provides evidence for the participation of this apoprotein in intestinal lipid transport
— id: 19017, year: 1976, vol: 193, page: 1254, stat: Journal Article,

Immunofluorescent localization of apoprotein B in intestinal epithelial cells
Glickman RM; Kilgore A; Khorana J
1976 ;24:285-285, Clinical research
— id: 62860, year: 1976, vol: 24, page: 285, stat: Journal Article,

Intestinal lipoprotein formation: effect of cholchicine
Glickman RM; Perrotto JL; Kirsch K
1976 Mar;70(3):347-352, Gastroenterology
The possibility that microtubules might be involved in intestinal lipoprotein formation or secretion was studied by determining the effect of colchicine, a known microtubule inhibitor, on intestinal lipid absorption. The effect of colchicine (0.5 mg per 100 g) in the lymphatic absorption of [14C]oleic acid was studied in rats with indwelling mesenteric lymph cannulas. Colchicine-treated animals showed a marked delay as well as a decrease in the lympatic absorption of [14C]oleic acid. Chylomicrons from colchicine-treated animals showed no difference in apoprotein content when examined on sodium dodecyl sulfate polyacrylamide gels. Micellar lipid absorption was next studied from in situ jejunal loops in animals pretreated with colchicine. Colchicine administration was associated with a 3-fold increase in residual mucosal lipid when compared with controls. Thin layer chromatography of residual lipid demonstrated that residual lipid was largely present as triglyceride, suggesting that the impairment in lipid transport induced by colchicine was at a site distal to triglyceride resynthesis. Electron microscopic examination of intestine from colchicine-treated animals revealed that most residual lipid was present within the endoplasmic reticulum and Golgi in numerous particles the size of chylomicrons (0.2 to 0.4 mu). These results suggest that the impairment in lipid transport induced by colchicine is distal and, in part, may represent an 'exit block'. These results suggest a possible role for microtubules in intestinal lipid transport. However, further studies are required to demonstrate directly the participation of microtubules in chylomicron secretion
— id: 19019, year: 1976, vol: 70, page: 347, stat: Journal Article,

The effect of colchicine on intestinal lipoprotein secretion
Glickman RM; Perrotto JL; Kirsch K
1975 ;23:249-249, Clinical research
— id: 62859, year: 1975, vol: 23, page: 249, stat: Journal Article,

"Review of gastroenterology" (Abraham Bogoch; McGraw-Hill, 1973)
Glickman RM
1974 ;290:59-60, New England journal of medicine
— id: 62845, year: 1974, vol: 290, page: 59, stat: Journal Article,

Abdominal swelling and ascites
Glickman RM; Isselbacher KJ
Harrison's principles of internal medicine New York : McGraw-Hill, 1974,
— id: 3888, year: 1974, vol: , page: 228, stat: Chapter,

The apoproteins of various size classes of human chylous fluid lipoproteins
Glickman RM; Kirsch K
1974 Nov 5;371(1):255-266, Biochimica & biophysica acta
— id: 19021, year: 1974, vol: 371, page: 255, stat: Journal Article,

Lymph chylomicron formation during the inhibition of protein synthesis. Studies of chylomicron apoproteins
Glickman RM; Kirsch K
1973 Nov;52(11):2910-2920, Journal of clinical investigation
— id: 19022, year: 1973, vol: 52, page: 2910, stat: Journal Article,

The apoproteins of human mesenteric lymph lipoproteins: a comparison of chylomicrons and VLDL
Glickman RM; Kirsch K
1973 ;21:513-513, Clinical research
— id: 62858, year: 1973, vol: 21, page: 513, stat: Journal Article,

Fat absorption during inhibition of protein synthesis: studies of lymph chylomicrons
Glickman RM; Kirsch K; Isselbacher KJ
1972 Feb;51(2):356-363, Journal of clinical investigation
— id: 19023, year: 1972, vol: 51, page: 356, stat: Journal Article,

On the role of protein sythesis in the intestinal absorption of fat
Iseelbacher KJ; Glickman RM
Transport across the intestine Edinburgh : Churchill Livingstone, 1972,
— id: 3904, year: 1972, vol: , page: 245, stat: Chapter,

Fat absorption during inhibition of protein synthesis: studies of chylomicron size
Glickman RM; Kirsch K; Isselbacher KJ
1971 ;60:775-775, Gastroenterology
— id: 62847, year: 1971, vol: 60, page: 775, stat: Journal Article,

Method for determination of specific activity of proteins in polyacrylamide gels
Alpers DH; Glickman R
1970 Jun;35(2):314-320, Analytical biochemistry
— id: 62838, year: 1970, vol: 35, page: 314, stat: Journal Article,

Increased lymph alkaline phosphatase after fat feeding: effects of medium chain triglycerides and inhibition of protein synthesis
Glickman RM; Alpers DH; Drummey GD; Isselbacher KJ
1970 Feb 24;201(2):226-235, Biochimica & biophysica acta
— id: 19024, year: 1970, vol: 201, page: 226, stat: Journal Article,

Abdominal swelling and ascites
Isselbacher KJ; Glickman RM
Harrison's principles of internal medicine New York : McGraw-Hill, 1970,
— id: 3887, year: 1970, vol: , page: 261, stat: Chapter,

The pathogenesis and control of the hemorrhagic defect in open heart surgery
Kevy SV; Glickman RM; Bernhard WF; Diamond LK; Gross RE
1966 Aug;123(2):313-318, Surgery, gynecology & obstetrics
— id: 19025, year: 1966, vol: 123, page: 313, stat: Journal Article,

Studies on the effects of irradiation on cellular particulates. IV. The time sequence of phosphorylation changes in vivo
Yost Jr. HT; Glickman RM; Beck LH
1964 ;127:173-173, Biological bulletin
— id: 62841, year: 1964, vol: 127, page: 173, stat: Journal Article,