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Literature DB >> 2478119

Phosphorylation of complement factor C3 in vivo.

Abstract

Complement factor C3, the central protein of the complement system, was found to be phosphorylated both in EDTA- and heparin-anticoagulated whole blood and in coagulating blood. Complement S protein (vitronectin) was also found to be phosphorylated under these conditions. Further, purified C3 was found to be a phosphoprotein in vivo, containing 0.15 mol of alkali-labile phosphate/mol of protein. The ATP concentration in plasma was measured and found to be about 2 microM.

Entities: Chemical Gene

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Year: 1989 PMID： 2478119 PMCID： PMC1138937 DOI： 10.1042/bj2611051

Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857

17 in total

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Authors: S L Chen; K H Kim
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Authors: J Janatova; P E Lorenz; A N Schechter; J W Prahl; B F Tack
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Authors: T M Chiang; A H Kang
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Authors: G V Born; M A Kratzer
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6 in total

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2. Phosphorylation of complement component C3 after synthesis in U937 cells by a putative protein kinase, casein kinase 2, which is regulated by CD11b: evidence that membrane-bound proteases preferentially cleave phosphorylated C3.

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Review 6. The Human Platelet as an Innate Immune Cell: Interactions Between Activated Platelets and the Complement System.

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