Characterization of Clq, Cls and Cl̄ Inh synthesized by stimulated human monocytes in vitro
1985
Abstract Clq, Cls and Cl Inh synthesized and secreted by human monocytes were characterized by SDS-PAGE. Clq is formed of three chains A ( M r ~35000), B ( M r ~33000) and C ( M r ~25000) which are associated in two subunits A-B and C-C. It appears identical to C1q purified from plasma. Cls is secreted as a non-activated, monocatenar protein of M r ~87000 identical to proenzymic Cls from plasma. Secreted Cl Inh ( M r ~100000) has a slightly higher M r than purified plasmatic Cl Inh. Monensin treatment of the cells favours the intracytoplasmic accumulation of products at various glycosylation stages.
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