Joel D Oppenheim, Ph.D.

Separate domains of the Ran GTPase interact with different factors to regulate nuclear protein import and RNA processing
Ren M; Villamarin A; Shih A; Coutavas E; Moore MS; LoCurcio M; Clarke V; Oppenheim JD; D'Eustachio P; Rush MG
1995 Apr;15(4):2117-2124, Molecular & cellular biology
The small Ras-related GTP binding and hydrolyzing protein Ran has been implicated in a variety of processes, including cell cycle progression, DNA synthesis, RNA processing, and nuclear-cytosolic trafficking of both RNA and proteins. Like other small GTPases, Ran appears to function as a switch: Ran-GTP and Ran-GDP levels are regulated both by guanine nucleotide exchange factors and GTPase activating proteins, and Ran-GTP and Ran-GDP interact differentially with one or more effectors. One such putative effector, Ran-binding protein 1 (RanBP1), interacts selectively with Ran-GTP. Ran proteins contain a diagnostic short, acidic, carboxyl-terminal domain, DEDDDL, which, at least in the case of human Ran, is required for its role in cell cycle regulation. We show here that this domain is required for the interaction between Ran and RanBP1 but not for the interaction between Ran and a Ran guanine nucleotide exchange factor or between Ran and a Ran GTPase activating protein. In addition, Ran lacking this carboxyl-terminal domain functions normally in an in vitro nuclear protein import assay. We also show that RanBP1 interacts with the mammalian homolog of yeast protein RNA1, a protein involved in RNA transport and processing. These results are consistent with the hypothesis that Ran functions directly in at least two pathways, one, dependent on RanBP1, that affects cell cycle progression and RNA export, and another, independent of RanBP1, that affects nuclear protein import
— id: 6723, year: 1995, vol: 15, page: 2117, stat: Journal Article,

THE IGD RECEPTOR (IGD-R) ON HUMAN T-CELLS IS A LECTIN THAT BINDS TO A CARBOHYDRATE SEQUENCE COMMON TO IGD AND IGA1
AMIN, AR; SWENSON, CD; WEI, CF; TAMMA, SML; OPPENHEIM, JD; PATEL, T; COICO, RF; PAREKH, RB; THORBECKE, GJ
1994 MAR 18 ;8(5):A749-A749, FASEB journal
— id: 52519, year: 1994, vol: 8, page: A749, stat: Journal Article,

Explanation for different types of regulation of arginine biosynthesis in Escherichia coli B and Escherichia coli K12 caused by a difference between their arginine repressors
Tian G; Lim D; Oppenheim JD; Maas WK
1994 Jan 7;235(1):221-230, Journal of molecular biology
In Escherichia coli K12, formation of the enzymes of arginine biosynthesis are controlled by arginine, with complete repression during growth with added arginine, severe repression (about 95%) during growth without added arginine and complete derepression during arginine-limited growth. In E. coli B, the degree of repression is not correlated with arginine concentrations. Under all conditions of growth enzyme formation is repressed, with repression being somewhat less in a medium with arginine than in a medium without arginine. These differences in repressibility between the two strains have been shown previously to be due to the presence of different alleles of argR, the gene for the arginine repressor. Here we have compared the binding of the two repressors to the operator sites of argF (ARG boxes). In DNase I footprinting and gel retardation experiments with argF ARG boxes we have shown that the arginine repressor of E. coli K12 bound to arginine (ArgRK-arg) has a greater affinity than the arginine repressor of E. coli B bound to arginine (ArgRB-arg), whereas free ArgRB (ArgRBf) has a much stronger affinity than free ArgRK (ArgRKf). The stronger binding of ArgRBf can explain the repression seen in E. coli B during arginine-limited growth and indicates that ArgRBf, but not ArgRKf, is able to repress enzyme synthesis under physiological conditions. The weaker repression of E. coli B than of E. coli K12 seen in the presence of arginine can be explained by the lower affinity of ArgRB-arg for operator sites as compared to ArgRK-arg. Another contributing cause for the weaker repression is the reduction of ArgRBf concentration due to autoregulation of the gene for the repressor. Thus the combined effects of repression by ArgRBf, but not ArgRKf, with the weaker repression by ArgRB-arg as compared to ArgRK-arg, convert the arginine dependent regulation in E. coli K12 to arginine independent regulation in E. coli B
— id: 6537, year: 1994, vol: 235, page: 221, stat: Journal Article,

TSG-6, an arthritis-associated hyaluronan binding protein, forms a stable complex with the serum protein inter-alpha-inhibitor
Wisniewski HG; Burgess WH; Oppenheim JD; Vilcek J
1994 Jun 14;33(23):7423-7429, Biochemistry
TSG-6 is a secreted 35-kDa glycoprotein, inducible by TNF and IL-1. The N-terminal portion of TSG-6 shows sequence homology to members of the cartilage link protein family of hyaluronan binding proteins. The C-terminal half of TSG-6 contains a so-called CUB domain, characteristic for developmentally regulated proteins. High levels of TSG-6 protein are found in the synovial fluid of patients with rheumatoid arthritis and some other arthritic diseases. Here we show that TSG-6 readily formed a complex with a protein present in human, bovine, rabbit, and mouse serum. This complex was stable during SDS-PAGE under reducing conditions, and in the presence of 8 M urea. The protein that binds TSG-6 was purified from human serum and identified as inter-alpha-inhibitor (I alpha I) by N-terminal microsequencing. Microsequencing of the complex itself revealed the presence of TSG-6 and two of the three polypeptide chains of I alpha I (bikunin and HC2). Experiments with recombinant TSG-6 and I alpha I purified from human serum showed that the TSG-6/I alpha I complex is rapidly formed even in the apparent absence of other proteins at 37 degrees C, but not at 4 degrees C. The TSG-6/I alpha I complex was cleaved by chondroitin sulfate ABC lyase, suggesting that cross-linking by chondroitin sulfate is required for the stability of the complex.(ABSTRACT TRUNCATED AT 250 WORDS)
— id: 6555, year: 1994, vol: 33, page: 7423, stat: Journal Article,

TSG-6, AN ARTHRITIS-ASSOCIATED HYALURONAN-BINDING PROTEIN, FORMS A STABLE COMPLEX WITH INTER-ALPHA-INHIBITOR VIA A GLYCOSAMINOGLYCAN CROSS-LINK
WISNIEWSKI, HG; BURGESS, WH; OPPENHEIM, JD; VILCEK, J
1994 JAN 4 ;269(6):338-338, Journal of cellular biochemistry
— id: 52588, year: 1994, vol: 269, page: 338, stat: Journal Article,

The immunoaugmenting properties of murine IgD reside in its C delta 1 and C delta 3 regions: potential role for IgD-associated glycans
Amin AR; Tamma SM; Swenson CD; Kieda CC; Oppenheim JD; Finkelman FD; Coico RF
1993 Jun;5(6):607-614, International immunology
IgD receptor (IgD-R) bearing CD4+ T cells with immunoaugmenting properties in vivo are induced in mice within 24 h after a single injection of dimeric or aggregated IgD. In the present study, we sought to identify the region(s) of IgD responsible for upregulation of IgD-R and for the immunoaugmenting effect of IgD. IgD-R can be upregulated on CD4+ T cells in vitro and in vivo by glutaraldehyde-aggregated mutant IgD or by fragments of enzymatically digested IgD molecules possessing either the C delta 1 domain (Fd delta) or the C delta 3 domain (Fc delta). Neoglycoproteins (D-galactose--BSA and N-acetyl-D-glucosamine--BSA), can competitively block upregulation of IgD-R by IgD in vitro. Furthermore, when injected 1 day before antigen, the aggregated IgD derived molecules, KWD1 (which lacks C delta 1), KWD6 (which lacks C delta 1 plus C delta-hinge), and Fab delta can all cause augmentation of antigen-specific primary and secondary antibody responses comparable to that achieved with intact aggregated IgD. Moreover, the immunoaugmenting effect of intact oligomeric IgD molecules in primary antibody responses is competitively blocked by simultaneous injection of monomeric forms of KWD6 and Fab delta. These results suggest that the binding of IgD to IgD-R, previously shown to be dependent on N-glycans present on Fd delta and Fc delta regions, also contributes to the upregulation of IgD-R and immunoagumentation
— id: 13148, year: 1993, vol: 5, page: 607, stat: Journal Article,

Characterization of proteins that interact with the cell-cycle regulatory protein Ran/TC4
Coutavas E; Ren M; Oppenheim JD; D'Eustachio P; Rush MG
1993 Dec 9;366(6455):585-587, Nature
The human Ras-related nuclear protein Ran/TC4 (refs 1-4) is the prototype of a well conserved family of GTPases that can regulate both cell-cycle progression and messenger RNA transport. Ran has been proposed to undergo tightly controlled cycles of GTP binding and hydrolysis, to operate as a GTPase switch whose GTP- and GDP-bound forms interact differentially with regulators and effectors. One known regulator, the protein RCC1 (refs 12, 13), interacts with Ran to catalyse guanine nucleotide exchange, and both RCC1 and Ran are components of an intrinsic checkpoint control that prevents the premature initiation of mitosis. To test and extend the GTPase-switch model, we searched for a Ran-specific GTPase-activating protein (GAP), and for putative effectors (proteins that interact specifically with Ran/TC4-GTP). We report here the identification of a Ran GAP and its use to characterize the GTP-hydrolysing properties of mutant Ran proteins, and the identification and cloning of a binding protein specific for Ran/TC4-GTP
— id: 6344, year: 1993, vol: 366, page: 585, stat: Journal Article,

WHILE OLIGOMERIC IGD AUGMENTS, MONOMERIC IGD INHIBITS THE GENERATION OF IGG MEMORY IN THE ANTIBODY-RESPONSE IN PARALLEL WITH IGD RECEPTOR EXPRESSION ON T-CELLS
SWENSON, CD; AMIN, AR; RIZINASHVILI, E; OPPENHEIM, JD; THORBECKE, GJ
1993 APR 15 ;150(8):A276-A276, Journal of immunology
— id: 54232, year: 1993, vol: 150, page: A276, stat: Journal Article,

Mammalian mitochondrial chaperonin 60 functions as a single toroidal ring
Viitanen PV; Lorimer GH; Seetharam R; Gupta RS; Oppenheim J; Thomas JO; Cowan NJ
1992 Jan 15;267(2):695-698, Journal of biological chemistry
Chaperonins are thought to participate in the process of protein folding in bacteria and in eukaryotic mitochondria and chloroplasts. While some chaperonins are relatively well characterized, the structures of the mammalian chaperonins are unknown. We have expressed a mammalian mitochondrial chaperonin 60 in Escherichia coli and purified the recombinant protein to homogeneity. Structural and biochemical analyses of this protein establish a single toroidal structure of seven subunits, in contrast to the homologous bacterial, fungal, and plant chaperonin 60s, which have double toroidal structures comprising two layers of seven identical subjects each. The recombinant mammalian chaperonin 60, together with the mammalian chaperonin 10 (but not with bacterial chaperonin 10), facilitates the formation of catalytically active ribulose-bisphosphate carboxylase from an unfolded state in the presence of K+ and MgATP. Analysis of the partial reactions involved in this in vitro reconstitution reveals that the single toroid of chaperonin 60 can form stable complexes with both unfolded or partially folded [35S]ribulose-bisphosphate carboxylase and mitochondrial (but not bacterial) chaperonin 10 in the presence of MgATP. We conclude that the minimal functional unit of chaperonin 60 is a single hepatmeric toroid
— id: 8274, year: 1992, vol: 267, page: 695, stat: Journal Article,

Specificity of the murine IgD receptor on T cells is for N-linked glycans on IgD molecules
Amin AR; Tamma SM; Oppenheim JD; Finkelman FD; Kieda C; Coico RF; Thorbecke GJ
1991 Oct 15;88(20):9238-9242, Proceedings of the National Academy of Sciences of the United States of America
IgD receptors on murine T cells have been reported in this issue [Tamma, S. M. L., Amin, A. R., Finkelman, F. D., Chen, Y.-W., Thorbecke, G. J. & Coico, R. F. (1991) Proc. Natl. Acad. Sci. USA 88, 9233-9237] to bind either the first or third constant region of the heavy-chain of IgD molecules--findings that could not be satisfactorily explained by IgD amino acid sequences. We now find that boiled IgD molecules or low-Mr fragments from protease-digested IgD still inhibit binding of IgD-coated erythrocytes to IgD receptors. This inhibitory activity can be absorbed with the murine IgD-binding lectin from Griffonia simplicifolia 1 (GS-1) immobilized on Sepharose. N-linked glycans, obtained from N-glycanase-treated IgD and purified by binding to GS-1-Sepharose, also inhibit rosette formation of T-helper cells bearing receptors for IgD with IgD- or mutant IgD-coated erythrocytes. Deglycosylated IgD, produced by treatment with N-glycanase, no longer binds to the lectin and fails to inhibit IgD rosetting. Binding of intact IgD to T cells is also competitively inhibited by N-acetylgalactosamine, galactose, N-acetylglucosamine, and neoglycoproteins containing these sugars. These results clearly show that N-linked glycans, present in both the first and third constant regions of the delta heavy-chain domains, are prerequisites for binding of IgD to IgD receptors
— id: 57447, year: 1991, vol: 88, page: 9238, stat: Journal Article,

The Bacillus subtilis sin gene, a regulator of alternate developmental processes, codes for a DNA-binding protein
Gaur, N K; Oppenheim, J; Smith, I
1991 Jan;173(2):678-686, Journal of bacteriology
The sin gene of Bacillus subtilis encodes a dual-function regulatory protein, Sin, which is a negative as well as a positive regulator of alternate developmental processes that are induced at the end of vegetative growth in response to nutrient depletion. Sin has been purified to homogeneity by using a simple two-step procedure. It was found to bind to the developmentally regulated aprE (alkaline protease) gene at two sites in vitro. The stronger Sin-binding site (SBS-1) is located more than 200 bp upstream from the transcription start site. It is required for Sin repression of aprE expression in vivo, as strains bearing SBS-1 deletions were not affected by the sin gene. The second, weaker Sin-binding site lies on a DNA fragment that contains the aprE promoter. Results of DNase I, exonuclease III, and dimethyl sulfate footprinting analysis of SBS-1 suggested that Sin binding involves two adjacent binding sites which appear to contain two different partial dyad symmetries. An analysis of the predicted amino acid sequence of Sin revealed a potential leucine zipper protein dimerization motif which is flanked by two helix-turn-helix motifs that could be involved in recognizing two different dyad symmetries
— id: 138918, year: 1991, vol: 173, page: 678, stat: Journal Article,

Isolation and properties of the RepA1 protein of the IncFII replicon, RepFIC [published erratum appears in Mol Microbiol 1991 Dec;5(12):3089]
Maas R; Oppenheim J; Saadi S; Fuchs T; Maas WK
1991 Apr;5(4):927-932, Molecular microbiology
The initiator protein RepA1 of the IncFII replicon RepFIC derived from the enterotoxin plasmid EntP307 has been cloned under the control of the lambda PL promoter. This has enabled us to overproduce this protein and study its properties. Here we show that RepA1 is a soluble basic protein with an experimentally determined molecular weight of 40,000. Deletion analysis indicates that the overproduced protein originates from the open reading frame which we previously designated as coding for RepA1. We have also shown that the replication function of the replicon RepFIC depends on the intact RepA1 coding frame
— id: 14084, year: 1991, vol: 5, page: 927, stat: Journal Article,

Seasonally occurring lectins from the bryozoan Bugula neritina
Colon-Urban, R; Oppenheim, J D
1990 May;254(2):138-143, Journal of experimental zoology
Two different lectins (termed BnA-I and BnA-II) with distinct carbohydrate specificities were identified and subsequently isolated from the marine bryozoan Bugula neritina. BnA-I hemagglutinating activity was inhibited by N-acetylated hexosamines, their polymers, and glycoproteins rich in these moieties. BnA-II-induced hemagglutination was not blocked by any simple sugars but could be inhibited by several complex glycoproteins (e.g., thyroglobulin and orosomucoid). Both lectins required the presence of Ca(+)+ for reactivity and were purified by affinity chromatographic procedures. Purified BnA-I was determined to have a native molecular weight of 240 Kd and appeared to be a hexameric homopolymer while BnA-II was shown to be a 65-70 Kd monomer. Both lectins showed seasonality in expression, BnA-I appearing in animal extracts prepared in the spring and fall while BnA-II was expressed only during the summer and winter
— id: 141122, year: 1990, vol: 254, page: 138, stat: Journal Article,

Biochemical characterization of Plasmodium falciparum hemozoin
Goldie P; Roth EF Jr; Oppenheim J; Vanderberg JP
1990 Dec;43(6):584-596, American journal of tropical medicine & hygiene
Hemozoin, the pigment granule which develops within the blood stage food vacuole of the malaria parasite Plasmodium falciparum, was biochemically characterized. Hemozoin was found to be composed of 65% protein, 16% ferriprotoporphyrin-IX (hematin), 6% carbohydrate, and trace amounts of lipid and nucleic acids. The overwhelming majority of the protein component is a mixture of native and denatured human globin non-covalently associated with the metalloporphyrin. Immunoelectron microscopy, employing anti-human hemoglobin as a probe, identified in situ association of hemoglobin with hemozoin. Hemozoin produced within diabetic blood had a higher proportion of carbohydrate, suggesting that the carbohydrate component comes from non-enzymatic glycosylation of hemoglobin
— id: 14250, year: 1990, vol: 43, page: 584, stat: Journal Article,

Expression of the cloned gene for enterotoxin STb of Escherichia coli
Lawrence, R M; Huang, P T; Glick, J; Oppenheim, J D; Maas, W K
1990 Apr;58(4):970-977, Infection & immunity
This study involved the construction of hybrid plasmids to produce heat-stable enterotoxin type II of Escherichia coli (STb). The translation of the open reading frame for the STb gene estA was demonstrated in several ways. Studies using in vivo labeling with [35S]cysteine demonstrated a radiolabeled protein band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the expected molecular weight of 5,000 for toxin STb. Insertion of translational or transcriptional termination signals into the BglII site of the estA gene blocked the expression of estA. The estA gene was cloned into high-expression vector pKC30 downstream from the strong pL promoter. Northern (RNA) blotting assays revealed a 10- to 20-fold increase in mRNA produced by strain C600F(pKC30STb) over other STb-producing strains, compared with little or no increase in enterotoxin activity demonstrated by bioassay. The estA gene, with its own promoter and Shine-Delgarno region and a portion of the sequence for the signal peptide deleted, was also inserted under the control of the tac promoter. Even after induction of the tac promoter by addition of isopropyl-beta-D-thiogalactopyranoside, no biologic enterotoxin activity could be identified. Neutralizing antibodies to STb were produced in rabbits by using either a purified OmpF-STb-beta-galactosidase fusion protein or a 19-amino-acid synthetic STb peptide coupled to keyhole limpet hemocyanin
— id: 67823, year: 1990, vol: 58, page: 970, stat: Journal Article,

A rapid one step purification procedure for murine IgD based on the specific affinity of Bandeiraea (Griffonia) simplicifolia-1 for N-linked carbohydrates on IgD
Oppenheim JD; Amin AR; Thorbecke GJ
1990 Jul 3;130(2):243-250, Journal of immunological methods
The alpha-D-galactopyranosyl binding lectin from the seeds of Bandeiraea simplicifolia (a.k.a. Griffonia simplicifolia) termed BS-I, strongly reacts with murine IgD and with no other protein in ascites including all other classes of immunoglobulins as determined by immunoprecipitation, hemagglutination inhibition and affinity binding. Based on this finding, murine IgD could be rapidly purified directly from whole ascitic fluid by passage over affinity beads of BS-I linked to Sepharose 4B and subsequent elution by a buffer containing 0.1 M D-galactose. The sugar eluted product is 95-99% pure as determined by SDS-PAGE and represents 90-95% of the total IgD in the initial ascites by ELISA assay. Both monomeric and dimeric murine IgD may be purified by this procedure. Human IgD is unreactive with this lectin. Treatment of purified IgD with endoglycosidases that remove either O- or N-linked glycosides indicates that BS-I binds to IgD only via N-linked carbohydrate chains
— id: 8754, year: 1990, vol: 130, page: 243, stat: Journal Article,

Immunocytochemical localization of the [3H]estradiol-binding protein in rat pancreatic acinar cells
Grossman A; Oppenheim J; Grondin G; St. Jean P; Beaudoin AR
1989 Jun;124(6):2857-2866, Endocrinology
Significant amounts of an estradiol-binding protein (EBP) are present in pancreatic acinar cells. This protein differs from the one found in female reproductive tissues and secondary sex organs (which is commonly referred to as estrogen receptor). EBP has now been purified from rat pancreas and was used as an antigen to induce polyclonal antibodies in rabbits. The antiserum obtained was purified initially by ammonium sulfate fractionation and then still further by interaction with a protein fraction from pancreas that was devoid of estradiol-binding activity. The latter procedure was used to precipitate nonspecific immunoglobulin Gs. Western blot analysis demonstrated that the anti-EBP antibody reacted specifically with a doublet of protein bands having mol wt of 64K and 66K. When this purified antibody was used as an immunocytochemical probe in conjunction with protein-A-gold, acinar cells were labeled on the surface of the endoplasmic reticulum, on the plasma membrane, and in mitochondria. This specific labeling pattern was not observed when preimmune serum was used. No labeling was observed over the nucleus, Golgi apparatus, or zymogen granules with purified anti-EBP antibodies. The unexpected distribution of EBP in both the endoplasmic reticulum and mitochondria is discussed
— id: 10614, year: 1989, vol: 124, page: 2857, stat: Journal Article,

Isolation of a hemolysin from a spore-crystal mixture of Bacillus thuringiensis israelensis (serotype H-14)
Weinstein SA; Bernheimer AW; Oppenheim JD
1988 ;26(8):733-746, Toxicon
A hemolytic toxin from Bacillus thuringiensis israelensis was obtained by alkaline extraction and fast protein liquid chromatography (chromatofocusing followed by gel filtration). The toxin displayed a pI of 4.6-4.8 and an Mr of 26,000. Amino acid analysis demonstrated large amounts of serine, glycine and glutamic acid. The toxin was strongly lytic for rabbit, human and non-human primate erythrocytes, and was weakly lytic toward equine, feline, canine, bovine, amphibian and reptilian erythrocytes. It was weakly entomocidal as indicated by a lethal potency (LC50) of 25 micrograms/ml for second instar larvae of Anopheles stephansi. Direct micro-ELISA indicated that the toxin lacked antigenic identity with numerous eukaryotic and prokaryotic toxins and venoms
— id: 11252, year: 1988, vol: 26, page: 733, stat: Journal Article,

Kinetics of hemolysis induced by a toxin from Bacillus thuringiensis israelensis
Weinstein SA; Bernheimer AW; Oppenheim JD
1988 ;26(12):1177-1185, Toxicon
The kinetics of hemolysis resulting from the action on rabbit erythrocytes of a highly purified cytolytic toxin (26,000 mol. wt) isolated from a spore-crystal mixture of Bacillus thuringiensis israelensis was studied. Course of hemolysis, as determined by release of hemoglobin, yielded sigmoid curves whose maximum slopes were taken as a measure of the rate of lysis. Hemolysis occurred without an induction period, and the rate of lysis was a linear function of toxin concentration. Rate of hemolysis as a function of temperature yielded an Arrhenius constant of 9300 calories per mole. The toxin was active between pH 4.5 and 8.0. Lysis was strongly inhibited by Cu2+, Fe2+ and Zn2+ in concentrations as low as 0.025 M. Phosphatidylserine, phosphatidylinositol, phosphatidylcholine and sphingomyelin inhibited lysis, whereas phosphatidylethanolamine, cerebroside, cholesterol and major integral erythrocyte membrane proteins caused little or no inhibition. Inhibition of lysis by sucrose indicates that hemolysis is of the colloid-osmotic type
— id: 11240, year: 1988, vol: 26, page: 1177, stat: Journal Article,

Some properties of flammutoxin from the edible mushroom Flammulina velutipes
Bernheimer AW; Oppenheim JD
1987 ;25(11):1145-1152, Toxicon
A cytolytic toxin from the basidiocarps of the edible mushroom Flammulina velutipes was purified to homogeneity. The lysin, flammutoxin, is a single polypeptide chain of Mr 32,000 and pK about 5.4. It contains unusually large amounts of tryptophan, serine and glycine, and few or none of the sulfur-containing amino acids. Erythrocytes of rat, rabbit, guinea pig, man, mouse, cat and dog were sensitive to lysis, in that order, whereas erythrocytes of sheep, ox, goat, swine and horse were largely or completely resistant to lysis. The toxin appears not to be a phospholipase and it was not inhibitable by any of a variety of lipids. Hemolysis probably involves alteration of the erythrocyte membrane, with formation of submicroscopic ion channels, and it appears to be of the osmotic type. In some respects flammutoxin resembles phallolysin, a cytolytic toxin obtained from the mushroom Amanita phalloides
— id: 11414, year: 1987, vol: 25, page: 1145, stat: Journal Article,

LECTIN-LIKE BINDING-PROTEINS FROM THE BRYOZOAN BUGULA-NERITINA
COLONURBAN, R; OPPENHEIM, J
1987 FEB ;27(4):A37-A37, American zoologist
— id: 41831, year: 1987, vol: 27, page: A37, stat: Journal Article,

Nucleotide sequence of the argR gene of Escherichia coli K-12 and isolation of its product, the arginine repressor
Lim DB; Oppenheim JD; Eckhardt T; Maas WK
1987 Oct;84(19):6697-6701, Proceedings of the National Academy of Sciences of the United States of America
In Escherichia coli, the arginine repressor, the product of the argR gene, in conjunction with L-arginine controls the synthesis of the enzymes of arginine biosynthesis. We describe the nucleotide sequence of the argR gene, including its control region, and show that formation of the repressor is autoregulated. The argR control region contains two promoters, one of which overlaps the operator site and, as with other arg genes, consists of two adjacent palindromic sequences ('ARG boxes'). The arginine repressor protein and an arginine repressor-beta-galactosidase fusion protein were purified, and the amino acid sequence of the N-terminal end of the repressor protein portion of the fusion protein was determined. Antibodies prepared against the fusion protein react with the repressor. The repressor is precipitable by L-arginine, which facilitates its purification. The native repressor is a hexamer with a molecular weight of 98,000; its monomeric subunit has a molecular weight of 16,500. To verify its properties postulated from genetic studies, we show that in the presence of L-arginine, repressor inhibits transcription of argF and binds to the ARG boxes of argF and argR
— id: 11360, year: 1987, vol: 84, page: 6697, stat: Journal Article,

RAPID PURIFICATION OF ANTI-I AND ANTI-I COLD ANTIBODIES BY AFFINITY-CHROMATOGRAPHY
GLICK, J; OPPENHEIM, JD
1985 ;49(1):49-57, Vox sanguinis
— id: 41220, year: 1985, vol: 49, page: 49, stat: Journal Article,

Lack of inhibitory effects of alpha 1-acid glycoprotein (orosomucoid) on Plasmodium falciparum invasion of human erythrocytes
Gupta SK; Oppenheim JD; Glick J; Schulman S; Vanderberg JP
1985 Sep;34(5):441-446, American journal of tropical medicine & hygiene
There has been controversy whether the plasma protein, alpha 1-acid glycoprotein (AGP), is able to inhibit invasion of erythrocytes by P. falciparum merozoites. Because AGP resembles a typical cell membrane sialoglycoprotein, it has been proposed that it can inhibit the parasite from interacting with its sialoglycoprotein receptor on the erythrocyte surface. We therefore isolated and tested samples of AGP obtained from a series of separate individuals. For comparative purposes, we also tested AGP prepared from the plasma of patients with elevated levels of AGP, as well as AGP obtained from two commercial sources. The authenticity and purity of the AGP samples was established by SDS-PAGE, radial immunodiffusion, and crossed immunoelectrophoresis. Our results indicated that none of the nine samples tested had any significant inhibitory effects in our P. falciparum invasion assay system
— id: 29364, year: 1985, vol: 34, page: 441, stat: Journal Article,

Characterization of human tumor necrosis factor produced by peripheral blood monocytes and its separation from lymphotoxin
Kelker HC; Oppenheim JD; Stone-Wolff D; Henriksen-DeStefano D; Aggarwal BB; Stevenson HC; Vilcek J
1985 Jul 15;36(1):69-73, International journal of cancer
Cultures of human peripheral blood leukocytes (PBL) induced with phytohemagglutinin (PHA) and the phorbol ester 12-0-tetradecanoylphorbol 13-acetate (TPA) produced two types of cytotoxic proteins, indistinguishable in the in vitro assay employing murine L 929 cells as targets. One of these proteins had the antigenic and physicochemical properties of lymphotoxin (LT). We have identified the other cytotoxin as tumor necrosis factor (TNF), mainly on the basis of antigenic cross-reactivity demonstrated with antiserum to TNF, and also by its characteristic physicochemical properties and cell source. Unlike LT, PBL-derived TNF did not bind to Concanavalin A-Sepharose or to several other agglutinin-Sepharose columns specific for carbohydrate moieties common in glycoproteins. The molecular weight of native TNF determined by gel filtration was approximately 40,000 while SDS-PAGE revealed a single sharp peak of 16,500 +/- 500. When cultures of monocytes and lymphocytes separated by elutriation were stimulated with PHA and/or TPA, monocytes were the major source of TNF. In contrast, only lymphocytes produced LT. A mixture of antisera to TNF and LF neutralized all cytotoxicity of crude human lymphokine preparations for L 929 cells, suggesting that TNF and LT are either the only, or the major, cytotoxic proteins present in such crude lymphokine preparations demonstrable in this assay
— id: 15035, year: 1985, vol: 36, page: 69, stat: Journal Article,

Role of the carbohydrate domains of glycophorins as erythrocyte receptors for invasion by Plasmodium falciparum merozoites
Vanderberg JP; Gupta SK; Schulman S; Oppenheim JD; Furthmayr H
1985 Jan;47(1):201-210, Infection & immunity
Solubilized preparations of purified glycophorins and specific domains of these molecules were assessed for their effects as inhibitors of Plasmodium falciparum invasion of human erythrocytes in vitro. The ability of newly invaded merozoites to continue developing and incorporating [3H]hypoxanthine during a 24-h period after their invasion was used as an assay for merozoite invasion. Glycophorins A, B, and C were found to be equally effective as inhibitors. Previous studies had shown N-acetylglucosamine, a sugar component of glycophorins A and C but not B, to be an effective inhibitor. Accordingly, molecular domains common to all of the glycophorins were further assessed. Sialic acid was shown to act almost as effectively as N-acetylglucosamine, presumably because of the structural similarities between these sugars. The inhibitory ability of sialic acid is considerably enhanced when presented to the parasite in a clustered form, as in an oligosaccharide. The acetyl group of these sugars does not appear to play an essential role in this inhibition. How the P. falciparum merozoite recognizes and interacts with the sugar domains of the glycophorin molecule remains to be determined
— id: 29367, year: 1985, vol: 47, page: 201, stat: Journal Article,

THE DISTRIBUTION OF AND THE BIOCHEMICAL AND SEROLOGICAL RELATIONSHIPS BETWEEN THE I/I AND ABH BLOOD-GROUP ANTIGENS OF THE HUMAN-ERYTHROCYTE MEMBRANE AS DETERMINED BY IMMUNOELECTROPHORETIC TECHNIQUES
Oppenheim, JD; Nachbar, MS; Blank, M
1983 ;4(1):53-62, Electrophoresis
— id: 30672, year: 1983, vol: 4, page: 53, stat: Journal Article,

Assay of erythrocyte components as inhibitors of Plasmodium falciparum merozoite invasion of erythrocytes
Schulman S; Oppenheim JD; Vanderberg JP
1983 Jul;32(4):666-670, American journal of tropical medicine & hygiene
Three red blood cell membrane fractions (Band 3, macromolecules exhibiting I antigenic determinants, and a delipidated glycoprotein fraction) were separated from red blood cell membranes and tested for their ability to inhibit penetration of red blood cells by Plasmodium falciparum merozoites in an in vitro inhibition assay. The delipidated glycoprotein fraction (containing the major sialoglycoproteins and devoid of Band 3) was the only fraction that inhibited merozoite invasion. This fraction showed 73% and 70% inhibition at 1 mg/ml and 500 micrograms/ml, respectively, and slight inhibition below these levels
— id: 29370, year: 1983, vol: 32, page: 666, stat: Journal Article,

Tomato (Lycopersicon esculentum) lectin
Nachbar MS; Oppenheim JD
1982 ;83(9):363-368, Methods in enzymology
— id: 18944, year: 1982, vol: 83, page: 363, stat: Journal Article,

MITOGENIC AND ADJUVANT PROPERTIES OF THE LPS-LIKE COMPONENT OF LISTERIA-MONOCYTOGENES
Oppenheim, JD; Nachbar, MS; Bhardwaj, N; Wexler, H
1981 ;10(1):25-28, FEMS microbiology letters
— id: 30224, year: 1981, vol: 10, page: 25, stat: Journal Article,

Plasmodium falciparum: assay in vitro for inhibitors of merozoite penetration of erythrocytes
Weiss MM; Oppenheim JD; Vanderberg JP
1981 Jun;51(3):400-407, Experimental parasitology
— id: 29375, year: 1981, vol: 51, page: 400, stat: Journal Article,

Stimulation of human gamma interferon production by diterpene esters
Yip YK; Pang RH; Oppenheim JD; Nachbar MS; Henriksen D; Zerebeckyj-Eckhardt I; Vilcek J
1981 Oct;34(1):131-139, Infection & immunity
The diterpene ester 12-O-tetradecanoylphorbol-13-acetate (TPA) and several structurally related compounds were tested for their ability to stimulate interferon (IFN) production in primary cultures of human leukocytes. In cultures of Ficoll-Hypaque-purified mononuclear cells, TPA treatment alone induced only low levels of IFN, but TPA pretreatment of cells caused significant enhancement of IFN yields produced with phytohemagglutinin or several other T cell mitogens. In cultures of unprocessed cells derived from plateletpheresis residues or buffy coats, TPA treatment alone induced high levels of IFN and costimulation with TPA and phytohemagglutinin produced some further enhancement of IFN production. Phorbol 12,13-dibutyrate was comparable to TPA in its ability to enhance phytohemagglutinin-induced IFN production. Several other phorbol ester analogs were also active, but maximal stimulation occurred only at higher drug concentrations. Mezerein, a structurally related diterpene ester, was at least as active as TPA in stimulating IFN production in either Ficoll-Hypaque-purified or unprocessed cells. IFN produced after stimulation with TPA or mezerein, singly or in combination with phytohemagglutinin, had several properties characteristic of IFN-gamma, e.g., it was largely inactivated by dialysis at pH 2, or after exposure to sodium dodecyl sulfate, whereas it was not neutralized by antibody to IFN-alpha and IFN-beta. The stimulatory effect of diterpene esters has proved helpful in producing IFN-gamma for physicochemical analysis and other studies
— id: 15601, year: 1981, vol: 34, page: 131, stat: Journal Article,

Lectins in the United States diet: a survey of lectins in commonly consumed foods and a review of the literature
Nachbar MS; Oppenheim JD
1980 Nov;33(11):2338-2345, American journal of clinical nutrition
Plant lectins or phytohemagglutinins possess potent in vivo biological activities. Some, primarily of the family Leguminosae, have been shown to have deleterious nutritional effects. Little information exists, however, regarding the prevalence of lectins or the specific foods that contain lectins in the United States diet. In the present study the edible parts of 29 of 88 foods tested, including common salad ingredients, fresh fruits, roasted nuts, and processed cereals were found to possess significant lectin-like activity as assessed by hemagglutination and bacterial agglutination assays. Based on this survey and a review of the literature we conclude that dietary exposure to plant lectins is widespread. The spectrum of nutritional consequences of such exposure remains to be determined
— id: 18945, year: 1980, vol: 33, page: 2338, stat: Journal Article,

Lectins in the U.S. Diet. Isolation and characterization of a lectin from the tomato (Lycopersicon esculentum)
Nachbar MS; Oppenheim JD; Thomas JO
1980 Mar 10;255(5):2056-2061, Journal of biological chemistry
— id: 18946, year: 1980, vol: 255, page: 2056, stat: Journal Article,

Plasmodium berghei and Plasmodium knowlesi: serum binding to sporozoites
Schulman S; Oppenheim JD; Vanderberg JP
1980 Jun;49(3):420-429, Experimental parasitology
— id: 29377, year: 1980, vol: 49, page: 420, stat: Journal Article,

ISOLATION, CHARACTERIZATION, AND BIOLOGICAL PROPERTIES OF AN ENDOTOXIN-LIKE MATERIAL FROM THE GRAM-POSITIVE ORGANISM LISTERIA-MONOCYTOGENES
Wexler, H; Oppenheim, JD
1979 ;23(3):845-857, Infection & immunity
— id: 29989, year: 1979, vol: 23, page: 845, stat: Journal Article,

Chloride self exchange in Ehrlich ascites cells. Inhibition by furosemide and 4-acetamido-4'-isothiocyanostilbene-2,2'-disulfonic acid
Aull F; Nachbar MS; Oppenheim JD
1977 Dec 15;471(3):341-347, Biochimica & biophysica acta
The effects of furosemide and 4-acetamido-4'-isothiocyanostilbene-2,2'-disulfonic acid (SITS) on steady-state Cl- flux were studied in Ehrlich mouse ascites cells. At 10 mM, furosemide inhibited isotopically-determined Cl- flux by 86% without changing cell Cl- content, indicating that influx and efflux were depressed by the same amount. These results suggest that at least 86% of the steady-state Cl- flux may occur as a one for one exchange. Half of the inhibitory effect was not reversed by vigorous washing with albumin-Ringer. A smaller portion of steady-state Cl- flux was inhibited by SITS. The maximum effect of SITS was reached near 0.6 mM; at this concentration Cl- flux was reduced by 37% without an alteration in cell Cl- content. Possible competition of environment Cl- and SITS was investigated by replacing environment Cl- with acetate or NO3. These anions reduced the efficacy of SITS because they depressed cell Cl- turnover themselves, apparently acting on the same exchange process
— id: 18947, year: 1977, vol: 471, page: 341, stat: Journal Article,

Nature of lectin-induced alteration of potassium transfer in Ehrlich ascites tumor cells
Aull F; Nachbar MS; Oppenheim JD
1977 Jan;90(1):9-14, Journal of cellular physiology
The way in which the lectins concanavalin A (Con A) and Ricinus communis agglutinin (Ricin) alter the K+ content of Ehrlich ascites tumor cells was investigated. Unidrectional and net fluxes were determined in unwashed cells during a time course following lectin addition. Total influx, ouabain sensitive influx, Mg++- and Na+-K+-ATPase activity were all unaffected. Cell ATP content was normal for at least 19 minutes after exposure to Con A. Early after contact with Ricin or Con A efflux was stimulated 2-3-fold, resulting in net K+ loss, but after 20 minutes efflux had returned to normal. Ricin and Con A acted similarly although Ricin was present at only 1/50 the concentration of Con A. When the findings are evaluated together with previous work it is suggested that a particular membrane glycoprotein may be concerned in the efflux alteration observed
— id: 18951, year: 1977, vol: 90, page: 9, stat: Journal Article,

CHLORIDE EXCHANGE AND EFFECT OF SITS IN EHRLICH ASCITES TUMOR- CELLS
Aull, F; Nachbar, MS; Oppenheim, JD
1977 ;297(2):163-163, Journal of supramolecular structure
— id: 29576, year: 1977, vol: 297, page: 163, stat: Journal Article,

The use of lectins in the quantitation and analysis of macromolecules by affinoelectrophoresis
Owen P; Oppenheim JD; Nachbar MS; Kessler RE
1977 Jun;80(2):446-457, Analytical biochemistry
— id: 18949, year: 1977, vol: 80, page: 446, stat: Journal Article,

MECHANISM OF LECTIN INDUCED CHANGES IN POTASSIUM-TRANSPORT OF EHRLICH ASCITES TUMOR-CELLS
Aull, F; Nachbar, MS; Oppenheim, JD
1976 ;35(3):605-605, Federation Proceedings (Federation of American Societies for Experimental Biology)
— id: 29495, year: 1976, vol: 35, page: 605, stat: Journal Article,

Interactions of lectins with plasma membrane glycoproteins of the Ehrlich ascites carcinoma cell
Nachbar MS; Oppenheim JD; Aull F
1976 Feb 6;419(3):512-529, Biochimica & biophysica acta
Several aspects of the interaction of various lectins with the surface of Ehrlich ascites carcinoma cells are described. The order of agglutinating activity for various lectins is Ricinus communis greater than wheat germ greater than or equal to concanavalin A greater than or equal to soybean greater than Limulus polyphemus. No agglutination was noted for Ulex europaeus. Using 125I-labeled lectins it was determined that there are 1.6 and 7 times as many Ricinus communis lectin binding sites for concanavalin A and soybean lectins. Sodium deoxycholate-solubilized plasma membrane material was subjected to lectin affinity chromatography and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The lectin receptors of the plasma membrane appeared to be heterogeneous and some qualitative differences could be discerned among the electrophoretically analyzed material, which bound to and was specifically eluted from the various lectin affinity columns. The characteristics of elution of bound material from individual lectin columns indicated secondary hydrophobic interactions between concanavalin A or wheat germ agglutinin and their respective lectin receptor molecules
— id: 18952, year: 1976, vol: 419, page: 512, stat: Journal Article,

Multiple specificities of mammalian blood group substances comparatively studied with human isoagglutinins and fractionated anti-H lectins
Chuba JV; Kuhns WJ; Oppenheim JD; Nachbar MS; Nigrelli RF
1975 Jul;29(1):17-30, Immunology
Purified blood group-active substances derived from different pig, horse, baboon, Rhesus monkey and human tissues were quantitatively studied for their haemagglutination inhibiting potency with: (1) human IgM anti-A and anti-B; (2) human anti-Lea and anti-Leb; (3) Ulex europaeus extracts separated into lectin fractions with respective L-fucose-inhibitable ('anti-HF') and chitobiose-cellobiose-inhibitable ('anti-HC') combining sites. Irrespective of species origin, A and B blood group activity per milligram of purified material tended to be strikingly higher in substances low in, or devoid of, Lewis blood group activity. Most of the blood group substances displayed variable but about equally balanced amounts of Ulex anti-HF and anti-HC inhibiting activity. In contrast, pig submaxillary gland mucins displayed strikingly high levels of Ulex anti-HC inihibiting activity, even in the complete absence of Ulex anti-HF inhibiting activity. These serological findings are consistent with current biochemical concepts regarding the heterosaccharide microheterogeneity of blood group-active glycoproteins
— id: 18953, year: 1975, vol: 29, page: 17, stat: Journal Article,

Cell surface contributions to the malignant process
Nachbar MS; Oppenheim JD; Aull F
1974 Sep;268(3):122-138, American journal of the medical sciences
— id: 18954, year: 1974, vol: 268, page: 122, stat: Journal Article,

Purification of a hemagglutinin from Limulus polyphemus by affinity chromatography
Oppenheim JD; Nachbar MS; Salton MR; Aull F
1974 Jun 18;58(4):1127-1134, Biochemical & biophysical research communications
— id: 18955, year: 1974, vol: 58, page: 1127, stat: Journal Article,

Labile inhibitor of lymphocyte transformation in plasma from a patient and subacute sclerosing panencephalitis
Allen J; Oppenheim J; Brody JA; Miller J
1973 Jul;8(1):80-82, Infection & immunity
— id: 57743, year: 1973, vol: 8, page: 80, stat: Journal Article,

The production and purification of specific anti-soybean agglutinin antibody by affinity chromatography
Nachbar MS; Oppenheim JD
1973 Sep 14;320(2):494-502, Biochimica & biophysica acta
— id: 18957, year: 1973, vol: 320, page: 494, stat: Journal Article,

Localization and distribution of Micrococcus lysodeikticus membrane ATPase determined by ferritin labeling
Oppenheim, J D; Salton, M R
1973 Mar 16;298(2):297-322, Biochimica & biophysica acta
— id: 76897, year: 1973, vol: 298, page: 297, stat: Journal Article,