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Showing papers on "B-cell activating factor published in 1991"


Journal ArticleDOI
TL;DR: MTNF-R2 showed strong specificity for recombinant murine TNF-alpha, suggesting that the various activities of human tumor necrosis factor alpha reported in mice or in murine cell lines are probably mediated by mT NF-R1.
Abstract: Complementary DNA clones encoding two distinct tumor necrosis factor receptors were isolated from a mouse macrophage cDNA library. The cDNA for murine tumor necrosis factor receptor type 1 (mTNF-R1) predicts a mature polypeptide of 425 amino acids that is 64% identical to its human counterpart, whereas the cDNA of murine tumor necrosis factor receptor type 2 (mTNF-R2) predicts a mature protein of 452 amino acids that is 62% identical to human tumor necrosis factor receptor type 2. The two murine tumor necrosis factor receptors have limited sequence homology (approximately 20% identity) in their extracellular regions but no apparent similarity in their cytoplasmic portions. Northern (RNA) analysis indicates a single 2.6-kilobase (kb) transcript for mTNF-R1; a 3.6-kb and a more predominant 4.5-kb transcript are observed for mTNF-R2. A human cell line transfected with either mTNF-R1 or mTNF-R2 expression vectors specifically bound 125I-labeled recombinant murine tumor necrosis factor alpha (TNF-alpha). Although mTNF-R1 had a similar affinity for both recombinant murine TNF-alpha and human TNF-alpha, mTNF-R2 showed strong specificity for recombinant murine TNF-alpha. This result suggests that the various activities of human tumor necrosis factor alpha reported in mice or in murine cell lines are probably mediated by mTNF-R1.

630 citations


Journal Article
TL;DR: Tumor necrosis factor is a highly potent pleiotropic response modifier in inflammatory and immunologic host defense reactions and can also be toxic to cells and elicit toxic systemic reactions, as evinced by certain pathophysiologic conditions that are initiated or aggravated by an excess of TNF.

97 citations



Journal ArticleDOI
TL;DR: The genes for TNFR1 and TNFR2, a 55-kDa protein, have been mapped to human chromosomes 1 12 and 1pter-p32 by Southern blot analysis of human × Chinese hamster somatic cell hybrid panels.
Abstract: Tumor necrosis factor, TNF, is a 17-kDa protein secreted by macrophages and classified as a cytokine. TNF binds to high-affinity receptors on the cell surface and is involved in a wide variety of biological responses. There are at least two types of receptors, tumor necrosis factor receptors 1 and 2 (TNFR1 and TNFR2). The genes for TNFR1 a 55-kDa protein, and TNFR2, a 70-kDa protein, have been mapped to human chromosomes 1 12 (12pter-cen) and (1pter-p32), respectively, by Southern blot analysis of human x Chinese hamster somatic cell hybrid panels. Recently, the corresponding genes in the mouse have been mapped to chromosomes 4 and 6 in regions that are conserved on human chromosomes 1 and 12.

19 citations


Patent
10 Jul 1991
TL;DR: In this paper, a novel tumor necrosis factor activity inhibitor which inhibits the cytocidal effect of a tumor NCA has been proposed, which has a molecular weight of about 34 kDa and a sequence of 11 amino acids at the N-terminus of Val-Ala-Phe-Thr-Pro-Tyr-ala-pro-AlA.
Abstract: A novel tumor necrosis factor activity inhibitor which inhibits the cytocidal effect of a tumor necrosis factor and has a molecular weight of about 34 kDa and a sequence of 11 amino acids at the N-terminus of Val-Ala-Phe-Thr-Pro-Tyr-Ala-Pro-Ala-Pro-Thr.

18 citations


Journal ArticleDOI
TL;DR: Binding characteristics of cell surface tumor necrosis factor‐α receptor on peripheral blood mononuclear cells in chronic hepatitis B virus carriers were studied and specific binding curves generated were analyzed according to the method of Scatchard to determine cell surface receptor numbers and dissociation constants.

14 citations




Journal Article
TL;DR: A gene coding for human tumor necrosis factor (h alpha TNF) has been assembled by ligating short oligodeoxyribonucleotides and cloning into plasmid vectors using isopropoxyacetyl (IPA) as a protecting group for exoamino- functions of nucleosides.
Abstract: A gene coding for human tumor necrosis factor (h alpha TNF) has been assembled by ligating short oligodeoxyribonucleotides and cloning into plasmid vectors. These oligonucleotides were prepared by the modified phosphoramidite methodology using isopropoxyacetyl (IPA) as a protecting group for exoamino- functions of nucleosides. Gene was expressed in E. coli and the protein product was purified to homogeneity by ion-exchange chromatography.

4 citations



Book ChapterDOI
01 Jan 1991
TL;DR: It is shown that TNF stimulates rat peritoneal macrophages, human polymorphonuclear neutrophils and vascular endothelial cells to synthetize and release PAF, which leads to the enhanced production of biologically active substances.
Abstract: Gram negative sepsis commonly includes several manifestations such as fever, hypotension, intravascular coagulation, and acute oliguric renal failure (1). The sequence of events culminating in renal failure is only partially known. Release of endotoxin, composed of LPS from the outer membrane layer of gram-negative bacterial cell walls into the systemic circulation? leads to the enhanced production of biologically active substances such as angiotensin II, adenosine, interleukin-1, tumor necrosis factor (TNF), arachidonic acid metabolites and platelet- activating factor (PAF). Evidence has accumulated that endotoxin-induced hemodynamic dearrangements and inflammation is primarily mediated by IL-1 and TNF (2,3). We have recently shown that TNF stimulates rat peritoneal macrophages, human polymorphonuclear neutrophils and vascular endothelial cells to synthetize and release PAF ( ).