Prochemerin cleavage by factor XIa links coagulation and inflammation.

ABSTRACT: Chemerin is a chemoattractant and adipokine that circulates in blood as inactive prochemerin (chem163S). Chem163S is activated by a series of C-terminal proteolytic cleavages resulting in diverse chemerin forms with different levels of activity. We screened a panel of proteases in the coagulation, fibrinolytic, and inflammatory cascades to identify those that process prochemerin in plasma. Factor XIa (FXIa) cleaved chem163S, generating a novel chemerin form, chem162R, as an intermediate product, and chem158K, as the final product. Processing at Arg¹⁶² was not required for cleavage at Lys¹⁵⁸ or regulation of chemerin bioactivity. Contact phase activation of human platelet-poor plasma by kaolin led to cleavage of chem163S, which was undetectable in FXI-depleted plasma a

SUBMITTER: Ge X 

PROVIDER: S-EPMC5774209 | biostudies-literature | 2018 Jan

REPOSITORIES: biostudies-literature