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

M Freeman, J Ashkenas, DJ Rees… - Proceedings of the …, 1990 - National Acad Sciences
M Freeman, J Ashkenas, DJ Rees, DM Kingsley, NG Copeland, NA Jenkins, M Krieger
Proceedings of the National Academy of Sciences, 1990National Acad Sciences
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 …
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 chromosomes 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).
National Acad Sciences