Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.24.23 (MMP)
 4,246 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The activity of different cathepsins and neutral proteinases was measured in normal and vitamin E-deficient rabbit muscles using specific substrates. Among the changes of enzyme activities in dystrophy caused by vitamin E-deficiency the increase in the activity of cathepsin B is the most striking. The activity of cathepsin H, both in the fast and slow muscles and that of MMP-ase in the slow muscle remains practically unchanged. Activities of other proteases significantly increase. The change in the activity of proteolytic enzymes in striated muscle of vitamin E-deficient rabbits seems to be selective. As a rule the increase in the activity is higher in fast than in slow muscles.
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PMID:Effect of vitamin E-deficiency on the activity of some lysosomal and non-lysosomal proteases in rabbit muscles. 181 30

Lysosomal cysteine proteinase (cathepsin B, H, and L) and MMP-7ase muscle metalloproteinase activities were measured in serum from Duchenne muscular dystrophic male patients and their mothers as gene-carriers. The activity of cathepsin H significantly increased in the Duchenne muscular dystrophic (DMD)-hemizygotes group and in the group of DMD heterozygotes. Significant positive correlation was found between the activity of serum creatine kinase (which previously has been proven to be a marker of muscular dystrophy) and of cathepsin L in the DMD-hemizygotes group. Furthermore, correlations were found between the activity of creatine kinase and MMP-7ase or between activity of creatine kinase and cathepsin H in the DMD heterozygotes. The changes in activity of proteolytic enzymes in serum of dystrophic patients can be explained by the elevated proteolytic enzyme activity in dystrophic muscle observed previously.
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PMID:Cysteine and metalloproteinase activities in serum of Duchenne muscular dystrophic genotypes. 320 67