cDNA cloning and primary structure analysis of C1qR(p), the human C1q/MBL/SPA receptor that mediates enhanced phagocytosis in vitro

205Citations
Citations of this article
32Readers
Mendeley users who have this article in their library.

Abstract

The complement protein C1q, mannose-binding lectin (MBL), and pulmonary surfactant protein A (SPA) are structurally similar molecules that enhance phagocytic function in vitro. Monoclonal antibodies R3 and R139, which inhibit the enhancement triggered by these three ligands, were used to purify a 126,000 M(r) cell surface protein designated C1qR(p). Amino acid sequence was obtained and the corresponding cDNA was cloned. C1qR(p) is a novel type I membrane protein with the following putative structural elements: a C-type carbohydrate recognition domain, five EGF-like domains, a transmembrane domain, and a short cytoplasmic tail. All peptides identified by amino acid sequencing are encoded by the cDNA. Additionally, an anti-peptide antiserum was generated, which is reactive with C1qR(p). The data indicate that the cloned cDNA encodes the receptor that plays a role in C1q/MBL/SPA-mediated removal or destruction of pathogens and immune complexes by phagocytosis.

Cite

CITATION STYLE

APA

Nepomuceno, R. R., Henschen-Edman, A. H., Burgess, W. H., & Tenner, A. J. (1997). cDNA cloning and primary structure analysis of C1qR(p), the human C1q/MBL/SPA receptor that mediates enhanced phagocytosis in vitro. Immunity, 6(2), 119–129. https://doi.org/10.1016/S1074-7613(00)80419-7

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free