Abstract
Chemokine CCL14 is inactive in its proform. Here, we show that inflammation- and cancer-associated kallikrein-related peptidases KLK5 and KLK8 remove the N-terminal eight amino acids from the proform thereby converting CCL14 to its active state. Activity of the chemokine is demonstrated by migration of myeloid cells expressing relevant receptors.
Keywords:
CCL14; THP-1; chemokines; myeloid cells.
© 2018 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
Publication types
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Letter
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Research Support, Non-U.S. Gov't
MeSH terms
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Asthma / pathology
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Atherosclerosis / pathology
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Cell Line, Tumor
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Chemokine CX3CL1 / metabolism
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Chemokine CXCL12 / metabolism
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Chemokines / metabolism*
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Chemokines, CC / metabolism*
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Crohn Disease / pathology
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Enzyme Activation
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Humans
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Interleukin-8 / metabolism
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Kallikreins / metabolism*
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Leukemia / pathology
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Macrophage Inflammatory Proteins / metabolism
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Pancreatitis / pathology
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Reactive Oxygen Species / metabolism
Substances
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CCL14 protein, human
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CCL15 protein, human
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CX3CL1 protein, human
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CXCL12 protein, human
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CXCL8 protein, human
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Chemokine CX3CL1
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Chemokine CXCL12
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Chemokines
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Chemokines, CC
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Interleukin-8
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Macrophage Inflammatory Proteins
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Reactive Oxygen Species
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KLK5 protein, human
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KLK8 protein, human
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Kallikreins