Muscular dystrophy and activation of proteinases
Autor: | Carl M. Pearson, Nirmal C. Kar |
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Rok vydání: | 1978 |
Předmět: |
Dipeptidases
Physiology Muscle Proteins Biology Aminopeptidases Muscular Dystrophies Dipeptidyl peptidase Substrate Specificity Cellular and Molecular Neuroscience Enzyme activator Physiology (medical) medicine Humans Muscular dystrophy Cathepsin Catabolism Muscles Proteolytic enzymes Skeletal muscle Hydrogen-Ion Concentration medicine.disease Cathepsins Endopeptidase Enzyme Activation medicine.anatomical_structure Biochemistry Calcium Neurology (clinical) Lysosomes Peptide Hydrolases |
Zdroj: | Muscle AND Nerve. 1:308-313 |
ISSN: | 1097-4598 0148-639X |
DOI: | 10.1002/mus.880010407 |
Popis: | 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. |
Databáze: | OpenAIRE |
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