AN ANCIENT, HIGHLY CONSERVED FAMILY OF CYSTEINE-RICH PROTEIN DOMAINS REVEALED BY CLONING TYPE-I AND TYPE-II MURINE MACROPHAGE SCAVENGER RECEPTORS
AN ANCIENT, HIGHLY CONSERVED FAMILY OF CYSTEINE-RICH PROTEIN DOMAINS REVEALED BY CLONING TYPE-I AND TYPE-II MURINE MACROPHAGE SCAVENGER RECEPTORS
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DOI:
10.1073/pnas.87.22.8810
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发表时间:
1990-11-01
影响因子:
11.1
通讯作者:
KRIEGER, M
中科院分区:
文献类型:
--
作者:
FREEMAN, M;ASHKENAS, J;KRIEGER, M
Scavenger receptors have been implicated in the development of atherosclerosis and other macrophage-associated functions. The bovine type I and type II scavenger receptors are multidomain transmembrane proteins that differ only by the presence in the type I receptor of an additional, extracellular cysteine-rich C-terminal domain. The isolation of type I and type II receptor cDNAs from a murine macrophage cell line, p388D1, establishes the presence of mRNAs encoding both receptor types in a single cell. Their sequences are highly similar to the bovine cDNAs. Receptor type-specific cDNA probes map to a common locus on murine chromosome 8, suggesting that a single gene encodes both mRNAs. The type I-specific scavenger receptor cysteine-rich (SRCR) domain helps define a previously unrecognized family of remarkably well-conserved domains. Highly homologous SRCR domains (one, three, or four per polypeptide chain) are found in diverse secreted and cell-surface proteins from humans (e.g., CD5, complement factor I), mice (Ly-1), and sea urchins (speract receptor).