An ancient, highly conserved family of cysteine-rich protein domains revealed by cloning type I and type II murine macrophage scavenger receptors

Mason Freeman, John Ashkenas, D. J G Rees, David M. Kingsley, Neal G. Copeland, Nancy A. Jenkins, Monty Krieger

Research output: Contribution to journalArticle

252 Scopus citations

Abstract

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).

Original languageEnglish (US)
Pages (from-to)8810-8814
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume87
Issue number22
DOIs
StatePublished - Nov 1990

Keywords

  • Atherosclerosis
  • CD5
  • Complement factor I
  • Evolution
  • Speract receptor

ASJC Scopus subject areas

  • Genetics
  • General

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