Regulation of proteolytic enzyme activities in muscles practice and hypothesis.
Two weeks of immobilization in shortened state caused 50% decrease in muscle mass and an increase in lysosomal proteinase activities. In this study causes of elevated protease activities in muscle are studied. Many factors could play a role in these elevated proteinase activities. We have found that redox state, ATP content, fuel supply and glucocorticoid receptor number were important in this period. Testosterone, insulin or proteinase inhibitors were not proved to play role in elevated proteinase activities. These practical results are explained by the results achieved in other types of cells. We conclude that changes in redox potential and/or oxygen free radical content of muscle elements can cause a post-translational covalent modification of cysteine proteinases and -SH dependent metalloproteinases, leading thereby to their activation. Lysosomal cysteine proteinases can activate procathepsin D that can damage lysosomal cysteine proteinase inhibitors and in another path it activates procathepsin B, L and H reversely. This feed-back regulation and the activation of cysteine proteinases by metalloproteinases might accelerate the proteinase activities in skeletal muscles.
Sohár
I
I
Department of Biochemistry, Szent-Györgyi A. Medical University, Szeged, Hungary.
D000818:Animals; D010450:Endopeptidases / Q000378:metabolism*; D004789:Enzyme Activation; D005609:Free Radicals; D008247:Lysosomes / Q000201:enzymology; D009132:Muscles / Q000201:enzymology*; D010084:Oxidation-Reduction
D005609:Free Radicals; D010450:Endopeptidases