Characteristics of complement subcomponents C1r and C1s synthesized by Hep G2 cells.
The association and activation states of complement subcomponents C1r and C1s biosynthesized by Hep G2 cells were studied. C1r and C1s are secreted in stoichiometric amounts; in the presence of Ca2+ they are associated in a complex that sediments similarly to plasma C1r2-C1s2. Both compounds are synthesized as monomer proteins of apparent Mr 86 000. C1r is secreted as a dimer. Secreted C1r is not autoactivatable but undergoes proteolysis by exogenous C1r; secreted C1s is also proteolysed by exogenous C1r. In the presence of immune-complex-bound C1q, secreted C1r and C1s are able to reconstitute C1, but normal activation requires extrinsic C1r2-C1s2.
D000818:Animals; D002460:Cell Line; D002499:Centrifugation, Density Gradient; D011232:Chemical Precipitation; D003166:Complement Activating Enzymes / Q000096:biosynthesis* / Q000276:immunology; D015923:Complement C1r; D003173:Complement C1s; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D008114:Liver Neoplasms, Experimental / Q000378:metabolism*; D046911:Macromolecular Substances; D010446:Peptide Fragments / Q000032:analysis
D046911:Macromolecular Substances; D010446:Peptide Fragments; D003166:Complement Activating Enzymes; D015923:Complement C1r; D003173:Complement C1s