PMID: 9191880Jul 1, 1997Paper

The C1q-binding cell membrane proteins cC1q-R and gC1q-R are released from activated cells: subcellular distribution and immunochemical characterization

Clinical Immunology and Immunopathology
K L PetersonB Ghebrehiwet

Abstract

Two types of widely coexpressed cell surface C1q-binding proteins (C1q-R): a 60-kDa calreticulin-homolog which binds to the collagen-like "stalk" of C1q and a 33-kDa protein with affinity for the globular "heads" of the molecule, have been described. In this report, we show that the two molecules are also secreted by Raji cells and peripheral blood lymphocytes and can be isolated in soluble form from serum-free culture supernatant by HPLC purification using a Mono-Q column. The two purified soluble proteins had immunochemical and physical characteristics similar to their membrane counterparts in that both bound to intact C1q and to their respective C1q ligands, cC1q and gC1q. In addition, N-terminal amino acid sequence analyses of the soluble cC1q-R and gC1q-R were found to be identical to the reported sequences of the respective membrane-isolated proteins. Ligand blot analyses using biotinylated membrane or soluble cC1q-R and gC1q-R showed that both bind to the denatured and nondenatured A-chain and moderately to the C-chain of C1q. Moreover, like their membrane counterparts, the soluble proteins were found to inhibit serum C1q hemolytic activity. Although cC1q-R was released when both peripheral blood lymphocytes and Raji cel...Continue Reading

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Citations

Feb 27, 1999·Current Opinion in Immunology·A J Tenner
Feb 27, 1999·Current Opinion in Immunology·A Nicholson-Weller, L B Klickstein
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