Omentin-1 prevents cartilage matrix destruction by regulating matrix metalloproteinases

Biomed Pharmacother. 2017 Aug:92:265-269. doi: 10.1016/j.biopha.2017.05.059. Epub 2017 May 24.

Abstract

Matrix metalloproteinases (MMPs) play a crucial role in the degradation of the extracellular matrix and pathological progression of osteoarthritis (OA). Omentin-1 is a newly identified anti-inflammatory adipokine. Little information regarding the protective effects of omentin-1 in OA has been reported before. In the current study, our results indicated that omentin-1 suppressed expression of MMP-1, MMP-3, and MMP-13 induced by the proinflammatory cytokine interleukin-1β (IL-1β) at both the mRNA and protein levels in human chondrocytes. Importantly, administration of omentin-1 abolished IL-1β-induced degradation of type II collagen (Col II) and aggrecan, the two major extracellular matrix components in articular cartilage, in a dose-dependent manner. Mechanistically, omentin-1 ameliorated the expression of interferon regulatory factor 1 (IRF-1) by blocking the JAK-2/STAT3 pathway. Our results indicate that omentin-1 may have a potential chondroprotective therapeutic capacity.

Keywords: Matrix metalloproteinases; Omentin-1; Osteoarthritis; Type II collagen.

MeSH terms

  • Cartilage, Articular / drug effects
  • Cartilage, Articular / metabolism*
  • Cytokines / metabolism*
  • Cytokines / pharmacology
  • GPI-Linked Proteins / metabolism
  • GPI-Linked Proteins / pharmacology
  • Humans
  • Interleukin-1beta / metabolism
  • Interleukin-1beta / pharmacology
  • Lectins / metabolism*
  • Lectins / pharmacology
  • Matrix Metalloproteinase 1 / physiology*
  • Matrix Metalloproteinase 13 / physiology*
  • Matrix Metalloproteinase 3 / physiology*

Substances

  • Cytokines
  • GPI-Linked Proteins
  • ITLN1 protein, human
  • Interleukin-1beta
  • Lectins
  • Matrix Metalloproteinase 13
  • Matrix Metalloproteinase 3
  • Matrix Metalloproteinase 1