Increased mRNA expression of tissue inhibitors of metalloproteinase-1 and -2 in Duchenne muscular dystrophy

Acta Neuropathol. 2005 Mar;109(3):285-93. doi: 10.1007/s00401-004-0941-0. Epub 2004 Dec 23.

Abstract

In dystrophinopathies, disease severity is generally related to the extent of muscle fibrosis. To determine whether a decrease in matrix degradation contributes to the severe fibrosis seen in Duchenne muscular dystrophy (DMD), we quantified RNA transcript numbers for the fibrolytic matrix metalloproteinases (MMP)-1 and -2 and their natural tissue inhibitors (TIMP)-1 and -2 in DMD muscle as well as in pathological and normal controls. In addition, we investigated gelatinase (MMP-2) enzyme activity by zymography. We found an up-regulation of TIMP-1, TIMP-2 and MMP-2 RNA in DMD muscle. Zymography revealed an increase in MMP-2 activity in DMD muscle homogenates, which was absent in pathological and normal controls. Therefore, besides enhanced fibrogenesis, a disturbance of matrix degradation may play a significant role in muscle fibrosis in DMD. TIMP-1 should be investigated further as a promising target for pharmacological intervention to prevent muscle fibrosis in DMD.

Publication types

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

MeSH terms

  • Adolescent
  • Child
  • Child, Preschool
  • DNA Mutational Analysis
  • Electrophoresis / methods
  • Humans
  • Immunohistochemistry / methods
  • Male
  • Muscles / drug effects
  • Muscles / enzymology
  • Muscular Dystrophy, Duchenne / enzymology*
  • Muscular Dystrophy, Duchenne / genetics
  • Platelet Endothelial Cell Adhesion Molecule-1 / metabolism
  • RNA, Antisense / pharmacology
  • RNA, Messenger / metabolism
  • Reverse Transcriptase Polymerase Chain Reaction / methods
  • Statistics, Nonparametric
  • Tissue Inhibitor of Metalloproteinase-1 / genetics
  • Tissue Inhibitor of Metalloproteinase-1 / metabolism*
  • Tissue Inhibitor of Metalloproteinase-2 / genetics
  • Tissue Inhibitor of Metalloproteinase-2 / metabolism*
  • Up-Regulation / physiology
  • Vimentin / metabolism

Substances

  • Platelet Endothelial Cell Adhesion Molecule-1
  • RNA, Antisense
  • RNA, Messenger
  • Tissue Inhibitor of Metalloproteinase-1
  • Vimentin
  • Tissue Inhibitor of Metalloproteinase-2