Overexpression of hsa-miR-148a promotes cartilage production and inhibits cartilage degradation by osteoarthritic chondrocytes

Osteoarthritis Cartilage. 2014 Jan;22(1):145-53. doi: 10.1016/j.joca.2013.11.006. Epub 2013 Nov 21.

Abstract

Objective: Hsa-miR-148a expression is decreased in Osteoarthritis (OA) cartilage, but its functional role in cartilage has never been studied. Therefore, our aim was to investigate the effects of overexpressing hsa-miR-148a on cartilage metabolism of OA chondrocytes.

Design: OA chondrocytes were transfected with a miRNA precursor for hsa-miR-148a or a miRNA precursor negative control. After 3, 7, 14 and 21 days, real-time PCR was performed to examine gene expression levels of aggrecan (ACAN), type I, II, and X collagen (COL1A1, COL2A1, COl10A1), matrix metallopeptidase 13 (MMP13), a disintegrin and metalloproteinase with thrombospondin motifs 5 (ADAMTS5) and the serpin peptidase inhibitor, clade H (heat shock protein 47), member 1 (SERPINH1). After 3 weeks, DNA content and proteoglycan and collagen content and release were determined. Type II collagen was analyzed at the protein level by Western blot.

Results: Overexpression of hsa-miR-148a had no effect on ACAN, COL1A1 and SERPINH1 gene expression, but increased COL2A1 and decreased COL10A1, MMP13 and ADAMTS5 gene expression. Luciferase reporter assay confirmed direct interaction of miR-148a and COL10A1, MMP13 and ADAMTS5. The matrix deposited by the miR-148a overexpressing cells contained more proteoglycans and collagen, in particular type II collagen. Proteoglycan and collagen release into the culture medium was inhibited, but total collagen production was increased.

Conclusion: Overexpression of hsa-miR-148a inhibits hypertrophic differentiation and increases the production and deposition of type II collagen by OA chondrocytes, which is accompanied by an increased retention of proteoglycans. Hsa-miR-148a might be a potential disease-modifying compound in OA, as it promotes hyaline cartilage production.

Keywords: Cartilage; Chondrocytes; MicroRNA; Osteoarthritis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • ADAM Proteins / biosynthesis
  • ADAM Proteins / genetics
  • ADAMTS5 Protein
  • Aged
  • Aged, 80 and over
  • Cartilage, Articular / metabolism
  • Cartilage, Articular / pathology*
  • Cells, Cultured
  • Chondrocytes / metabolism*
  • Chondrocytes / pathology
  • Collagen Type II / biosynthesis
  • Collagen Type II / genetics
  • Collagen Type X / biosynthesis
  • Collagen Type X / genetics
  • Female
  • Gene Expression Regulation
  • Humans
  • Male
  • Matrix Metalloproteinase 13 / biosynthesis
  • Matrix Metalloproteinase 13 / genetics
  • MicroRNAs / biosynthesis
  • MicroRNAs / physiology*
  • Middle Aged
  • Osteoarthritis, Knee / genetics
  • Osteoarthritis, Knee / metabolism*
  • Osteoarthritis, Knee / pathology
  • Proteoglycans / metabolism
  • RNA, Messenger / genetics

Substances

  • Collagen Type II
  • Collagen Type X
  • MIRN148 microRNA, human
  • MicroRNAs
  • Proteoglycans
  • RNA, Messenger
  • ADAM Proteins
  • ADAMTS5 Protein
  • ADAMTS5 protein, human
  • MMP13 protein, human
  • Matrix Metalloproteinase 13