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

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 12...

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Bibliographic Details
Published in:Immunity (Cambridge, Mass.) Mass.), 1997-02, Vol.6 (2), p.119-129
Main Authors: Nepomuceno, R R, Henschen-Edman, A H, Burgess, W H, Tenner, A J
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Base Sequence
Carrier Proteins - metabolism
Cloning, Molecular
Collectins
Complement Activating Enzymes - analysis
Complement Activating Enzymes - metabolism
Complement Activating Enzymes - physiology
DNA, Complementary - analysis
Humans
Hyaluronan Receptors
Lymphoma, Large B-Cell, Diffuse
Macrophage Activation - physiology
Membrane Glycoproteins
Mitochondrial Proteins
Molecular Sequence Data
Phagocytosis - physiology
Pulmonary Surfactants - metabolism
Receptors, Complement - analysis
Receptors, Complement - metabolism
Receptors, Complement - physiology
Receptors, Immunologic - analysis
Receptors, Immunologic - metabolism
Tumor Cells, Cultured
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Summary: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.
ISSN:1074-7613
DOI:10.1016/S1074-7613(00)80419-7