Characterization of C1q, C1s and C-1 Inh synthesized by stimulated human monocytes in vitro.
C1q, C1s and C1 Inh synthesized and secreted by human monocytes were characterized by SDS-PAGE. C1q is formed of three chains A (Mr approximately 35 000), B (Mr approximately 33 000) and C (Mr approximately 25 000) which are associated in two subunits A-B and C-C. It appears identical to C1q purified from plasma. C1s is secreted as a non-activated, monocatenar protein of Mr approximately 87 000 identical to proenzymic C1s from plasma. Secreted C1 Inh (Mr approximately 100 000) has a slightly higher Mr than purified plasmatic C1 Inh. Monensin treatment of the cells favours the intracytoplasmic accumulation of products at various glycosylation stages.
D002478:Cells, Cultured; D011232:Chemical Precipitation; D003166:Complement Activating Enzymes / Q000096:biosynthesis*; D003174:Complement C1 Inactivator Proteins / Q000096:biosynthesis*; D015922:Complement C1q; D003173:Complement C1s; D003593:Cytoplasm / Q000276:immunology; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007120:Immunochemistry; D008985:Monensin / Q000494:pharmacology; D009000:Monocytes / Q000276:immunology*
D003174:Complement C1 Inactivator Proteins; D015922:Complement C1q; D008985:Monensin; D003166:Complement Activating Enzymes; D003173:Complement C1s