TWO HUMAN TNF RECEPTORS HAVE SIMILAR EXTRACELLULAR BUT DISTINCT INTRACELLULAR DOMAIN SEQUENCES
TWO HUMAN TNF RECEPTORS HAVE SIMILAR EXTRACELLULAR BUT DISTINCT INTRACELLULAR DOMAIN SEQUENCES
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DOI:
10.1016/1043-4666(90)90022-l
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发表时间:
1990-01-01
期刊:
影响因子:
3.8
通讯作者:
LESSLAUER W
中科院分区:
文献类型:
--
作者:
DEMBIC Z;LOETSCHER H;LESSLAUER W
Tumor necrosis factor (TNF) is a cytokine with a wide range of biological activities in inflammatory and immunologic responses. These activities are mediated by specific cell surface receptors of 55 kDa and 75 kDa apparent molecular masses. A 75-kDa TNF receptor cDNA was isolated using partial amino acid sequence information and the polymerase chain reaction (PCR). When expressed in COS-1 cells, the cDNA transfer specific TNF-binding properties comparable to those of the native receptor. The predicted extracellular region contains four domains with characteristic cysteine residues higly similar to those of the 55-kDa TNF receptor, the nerve growth factor (NGF) receptor, and the CDw40 and OX40 antigens. The consensus sequence of the TNF receptor extracellular domains also has similarity to the cysteine-rich sequence motif LIM. In marked contrast to the extracellular regions, the intracellular domains of the two TNF receptors are entirely unrelated, suggesting different modes of signaling and function.