Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.24.11 (CD10)
 9,792 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Evidence is presented for the existence of many different systems of proteolytic enzymes in human skeletal muscle. These include the lysosomal system of cathepsins as well as proteinases and peptide hydrolases that are optimally active at neutral and alkaline pH ranges. The majority of proteolytic enzymes examined are found to show increased activity in dystrophic human muscle. Moreover, a high initial rise is observed in cathepsin B1, a thiol-dependent endopeptidase of lysosomes, and in dipeptidyl peptidase IV, a membrane-associated peptidase. In addition, a calcium-activated neutral proteinase is found to be significantly elevated in muscle from patients with Duchenne dystrophy. The possible roles of these proteinases in intracellular protein catabolism and muscle wasting are discussed.
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PMID:Muscular dystrophy and activation of proteinases. 3 47

Matrix metalloprotease (MMP)-9 is an endopeptidase associated with the pathogenesis of Duchenne muscular dystrophy (DMD). The precise function of MMP-9 in DMD has not been elucidated to date. We investigated the effect of genetic ablation of MMP-9 in the mdx mouse model (mdx/Mmp9(-/-)). At the early disease stage, the muscles of mdx/Mmp9(-/-) mice showed reduced necrosis and neutrophil invasion, accompanied by down-regulation of chemokine MIP-2. In addition, muscle regeneration was enhanced, which coincided with increased macrophage infiltration and upregulation of MCP-1, and resulted in increased muscle strength. The mdx/Mmp9(-/-) mice also displayed accelerated upregulation of osteopontin expression in skeletal muscle at the acute onset phase of dystrophy. However, at a later disease stage, the mice exhibited muscle growth impairment through altered expression of myogenic factors, and increased fibroadipose tissue. These results showed that MMP-9 might have multiple functions during disease progression. Therapy targeting MMP-9 may improve muscle pathology and function at the early disease stage, but continuous inhibition of this protein may result in the accumulation of fibroadipose tissues and reduced muscle strength at the late disease stage.
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PMID:Differential roles of MMP-9 in early and late stages of dystrophic muscles in a mouse model of Duchenne muscular dystrophy. 2617 62