Biological and structural characterization of the tumor necrosis factor receptor on multiple cell types: relationship to function
The authors compared the biochemical characteristics and molecular structure of the receptor to human recombinant tumor necrosis factor (HurTNF) on cells of different tissue origin that differ in their response to one of the known activities of TNF. They studied: (1) tumor cell lines that respond to the cytotoxic action of TNF and resistant variants that bind TNF, (2) normal cell lines that are stimulated to proliferate by TNF and those that are not affected by TNF, and (3) peripheral blood granulocytes whose activation is also augmented by TNF. Using /sup 125/I-HurTNF, they found that all the cell types bind TNF in a saturable, time-, temperature-, and dose-dependent manner. In addition, they describe that the /sup 125/I-HurTNF bound mainly to four cellular polypeptides, three of which were found in every cell type examined and one was observed only in a human breast carcinoma cell line that is highly responsive to the cytotoxic action of TNF. The 138-kDa polypeptide was not found in resistant variants of MCF-7 that bind TNF. In contrast to the other polypeptides, the 138-kDa protein was detected 30 min after incubation at 4/sup 0/C, as compared to 5 min. Scatchard analysis and cross-linking data suggest a model for the TNF receptor structure whereby the receptor is composed of noncovalently linked membrane-bound polypeptides that bind TNF with high affinity (Kd of .056 - .8 nM) with the 138-kDa protein being the least abundant and/or even absent in most cells.
- Research Organization:
- Cetus Corp., Emeryville, CA
- OSTI ID:
- 6279001
- Report Number(s):
- CONF-870644-
- Journal Information:
- Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States), Vol. 46:6; Conference: 78. annual meeting of the American Society of Biological Chemists conference, Philadelphia, PA, USA, 7 Jun 1987
- Country of Publication:
- United States
- Language:
- English
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