Proteolytic regulatory mechanism of chemerin bioactivity - PubMed (original) (raw)

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Proteolytic regulatory mechanism of chemerin bioactivity

Xiao-Yan Du et al. Acta Biochim Biophys Sin (Shanghai). 2009 Dec.

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.

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Figures

Figure 1

Figure 1

Alignment of amino acid sequences of chemerins from various species Domains of signal peptide, chemotaxis, and anti-inflammation were indicated.

Figure 2

Figure 2

Human chemerin precursor and its variants

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