Abstract
Chemerin, a chemoattractant ligand for chemokine-like receptor 1 (CMKLR1) is predicted to share similar tertiary structure with antibacterial cathelicidins. Recombinant chemerin has antimicrobial activity. Here we show that endogenous chemerin is abundant in human epidermis, and that inhibition of bacteria growth by exudates from organ cultures of primary human skin keratinocytes is largely chemerin-dependent. Using a panel of overlapping chemerin-derived synthetic peptides, we demonstrate that the antibacterial activity of chemerin is primarily mediated by Val(66)-Pro(85), which causes direct bacterial lysis. Therefore, chemerin is an antimicrobial agent in human skin.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Antimicrobial Cationic Peptides / chemistry
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Antimicrobial Cationic Peptides / genetics
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Antimicrobial Cationic Peptides / immunology*
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Cells, Cultured
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Chemokines / chemistry
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Chemokines / genetics
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Chemokines / immunology*
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Epidermis / immunology*
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Epidermis / microbiology*
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Escherichia coli / immunology
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Escherichia coli / pathogenicity
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Humans
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Intercellular Signaling Peptides and Proteins
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Keratinocytes / immunology
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Keratinocytes / microbiology
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Molecular Sequence Data
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Peptide Fragments / chemistry
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Peptide Fragments / genetics
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Peptide Fragments / immunology
Substances
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Antimicrobial Cationic Peptides
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Chemokines
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Intercellular Signaling Peptides and Proteins
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Peptide Fragments
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RARRES2 protein, human