Phosphorylation of plasma proteins with emphasis on complement component C3.
Phosphorylation of complement component C3 by different protein kinases in vitro has been demonstrated to alter the functional properties of the protein. Extracellular phosphorylation mediated by activated platelets is a newly described mechanism by which the function of plasma proteins can be regulated. Upon activation of platelets a casein kinase is released concomitant with large amounts of ATP and Ca2+. These components are sufficient to phosphorylate proteins e.g., C3 extracellularly. In vivo, in patients with SLE, the phosphate content in plasma proteins, including C3 has been demonstrated to increase during exacerbation. The changes were linked to platelet activation by a covariation with the levels of beta-thromboglobulin. The purpose of this review is to summarise the findings in this field.
The Department of Clinical Immunology and Transfusion Medicine, University Hospital, Uppsala, Sweden.
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K
Nilsson Ekdahl
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B
Nilsson
D000818:Animals; D001798:Blood Proteins / Q000378:metabolism*; D003176:Complement C3 / Q000378:metabolism*; D006801:Humans; D010766:Phosphorylation
D001798:Blood Proteins; D003176:Complement C3