Regulation of extracellular matrix compounds involved in angiogenic processes in short- and long-track elite runners

Scand J Med Sci Sports. 2010 Jun;20(3):441-8. doi: 10.1111/j.1600-0838.2009.00960.x. Epub 2009 Jun 23.

Abstract

Exercise induces alterations of the extracellular matrix (ECM), e.g. by an increased release of endostatin or by regulation of matrix metalloproteases (MMP)-2/-9, and cathepsin L. To investigate the influence of training status on exercise-induced ECM-processing of angiogenic molecules, alterations of endostatin-, MMP-2, and MMP-9 plasma concentrations during incremental running step tests in male elite short-track (n=6) and male elite long-track runners (n=7) were studied. Three blood samples (pre-exercise, 0, and 1 h post-exercise) were taken from each subject at each running test. In both groups, the basal endostatin plasma concentration was significantly decreased at the second running test, i.e. after the training season. Exercise-related acute alterations of the parameters were also observed only during the second test. In the long-track group, there was a significant increase in endostatin at 0 h and of MMP-2 at 1 h post-exercise. In the short-track group, only MMP-9 was significantly increased at 0 h post-exercise. Cathepsin L was increased at 0 h post-exercise. In conclusion, regular exercise performance decreases the basal endostatin plasma concentration, facilitates ECM-processing of angiogenic molecules by regular performance, and seems to be dependent on the kind of training.

MeSH terms

  • Adult
  • Athletes*
  • Cathepsin L / blood*
  • Cathepsin L / metabolism
  • Endostatins / blood*
  • Endostatins / metabolism
  • Extracellular Matrix / metabolism*
  • Humans
  • Male
  • Matrix Metalloproteinase 2 / blood*
  • Matrix Metalloproteinase 2 / metabolism
  • Matrix Metalloproteinase 9 / blood*
  • Matrix Metalloproteinase 9 / metabolism
  • Running / physiology*
  • Young Adult

Substances

  • Endostatins
  • Cathepsin L
  • Matrix Metalloproteinase 2
  • Matrix Metalloproteinase 9