Kallikrein-related peptidases are activators of the CC chemokine CCL14

Eur J Immunol. 2018 Sep;48(9):1592-1594. doi: 10.1002/eji.201747452. Epub 2018 Aug 22.

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.

Publication types

  • Letter
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Asthma / pathology
  • Atherosclerosis / pathology
  • Cell Line, Tumor
  • Chemokine CX3CL1 / metabolism
  • Chemokine CXCL12 / metabolism
  • Chemokines / metabolism*
  • Chemokines, CC / metabolism*
  • Crohn Disease / pathology
  • Enzyme Activation
  • Humans
  • Interleukin-8 / metabolism
  • Kallikreins / metabolism*
  • Leukemia / pathology
  • Macrophage Inflammatory Proteins / metabolism
  • Pancreatitis / pathology
  • Reactive Oxygen Species / metabolism

Substances

  • CCL14 protein, human
  • CCL15 protein, human
  • CX3CL1 protein, human
  • CXCL12 protein, human
  • CXCL8 protein, human
  • Chemokine CX3CL1
  • Chemokine CXCL12
  • Chemokines
  • Chemokines, CC
  • Interleukin-8
  • Macrophage Inflammatory Proteins
  • Reactive Oxygen Species
  • KLK5 protein, human
  • KLK8 protein, human
  • Kallikreins