| Literature DB >> 3006672 |
A Reboul, J C Bensa, M G Colomb.
Abstract
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.Entities:
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Year: 1986 PMID: 3006672 PMCID: PMC1153062 DOI: 10.1042/bj2330559
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857