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Acta Biochimica et Biophysica Sinica Advance Access published online on November 12, 2009
Acta Biochimica et Biophysica Sinica, doi:10.1093/abbs/gmp091
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© The Author 2009. Published by ABBS Editorial Office in association with Oxford University Press on behalf of the Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences.

Proteolytic regulatory mechanism of chemerin bioactivity

Xiao-Yan Du1,* and Lawrence L.K. Leung1,2

1 Division of Hematology, Stanford University School of Medicine, Stanford, CA 94305, USA
2 VA Palo Alto Health Care System, Palo Alto, CA 94304, USA

* Correspondence address. Tel/Fax: +1-650-736-0974; E-mail: duxiaoyan{at}hotmail.com


  Abstract

Chemerin is a novel chemoattractant recognized by chemokine-like receptor 1 (CMKLR1), a serpentine receptor expressed primarily by plasmacytoid dendritic cells, natural killer cells, and macrophages. Human prochemerin circulates in plasma as an inactive precursor. Its chemotactic activity is expressed upon cleavage of the C-terminal amino acid residues by proteases of the coagulation, fibrinolytic, and inflammatory system. The C-terminal cleavage site of prochemerin is highly conservative, indicating that the proteolytic regulation of chemerin bioactivity is a common mechanism undertaken by different species. In this review, we summarized chemerin–proteases interactions, chemerin receptors, and their importance in normal and pathologic conditions.

Keywords    chemerin; proteolysis; chemotactic; inflammation

Received: August 11, 2009; Accepted: July 7, 2009
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