Effect of leupeptin on protein turnover in normal and dystrophic chicken skeletal muscle cells in culture.
Explore this paper's citation graph
Summary
The muscle proteases that are specifically inhibited by leupeptin seem to have no major role in initiating myofibrillar protein turnover, as measured by the response of normal and dystrophic muscle cells to leipeptin treatment.
- Type
- article
- Published
- 1980-06-01
- Cited by
- 21
- References
- 29
- OpenAlex
- https://openalex.org/W2036845363
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:40444279
Keywords
Leupeptin, Myofibril, Myosin, Protein turnover, Biology
References
- The origin of urinary creatine in progressive muscular dystrophy.
- Degradation of myofibrillar proteins by cathepsins B and D.
- Removal of Z-lines and alpha-actinin from isolated myofibrils by a calcium-activated neutral protease.
- Possible significance of myofibrillar protease in muscle catabolism. Enzyme activity in dystrophic, tumor-bearing, and glucocorticoid-treated animals.
- Protein measurement with the Folin phenol reagent.
- Serine protease in mice with hereditary muscular dystrophy.
- Purification and some physico-chemical and enzymic properties of a calcium ion-activated neutral proteinase from rabbit skeletal muscle.
- Lipid changes in Duchenne muscular dystrophy
- Aseptic autolysis in rabbit and bovine muscle during storage at 37
- Fatty acid oxidation by skeletal muscle mitochondria in Duchenne muscular dystrophy.
- Delayed degeneration of dystrophic and normal muscle cell cultures treated with pepstatin, leupeptin, and antipain.
- Muscular dystrophy: inhibition of degeneration in vivo with protease inhibitors.
- Leupeptin, a protease inhibitor, decreases protein degradation in normal and diseased muscles.
- Normal and dystrophic chicken muscle at successive stages in tissue culture.
- Myogenic defect in muscular dystrophy of the chicken.
- Serum enzyme alterations in neuromuscular disorders.
- Myogenic defect in acetylcholinesterase regulation in muscular dystrophy of the chicken.
- MAJOR PHYSIOLOGIC AND HISTOCHEMICAL CHARACTERISTICS OF INHERITED DYSTROPHY OF THE CHICKEN *
- Cathepsins A, B, C, D and autolysis during development of breast muscle of normal and dystrophic chickens.
- The Activity of Partially Purified Bovine Catheptic Enzymes on Various Natural and Synthetic Substratesa
Cited by
- Ca2-activated proteinases, protein degradation and muscular dystrophy.
- Use of stable isotope labelling to study protein degradation in chick embryonic skeletal muscle cell cultures
- Standardization of collection requirements for fasting samples: for the Working Group on Preanalytical Phase (WG-PA) of the European Federation of Clinical Chemistry and Laboratory Medicine (EFLM).
- Tissue and subcellular distribution of enzymes inactivating leupeptin
- Protein degradation in cultured skeletal muscle from duchenne muscular dystrophy patients
- Urinary trace element concentrations in environmental settings: is there a value for systematic creatinine adjustment or do we introduce a bias?
- Analysis of peptides with unusual structural features by fast atom bombardment mass spectrometry: Protease inhibitors
- Normal and dystrophic embryonic chicken pectoralis muscle cultures: I. Cell differentiation, protein synthesis, and enzyme levels
- Action of a serine proteinase from fish skeletal muscle on myofibrils.
- Turnover of myofibrillar proteins in cultured muscle cells from normal and dystrophic chick embryos.
- Drug evaluation in muscular dystrophy of the chicken
- Intracellular protein degradation in cultures of dystrophic muscle cells and fibroblasts.
- Is it feasible for patients to estimate their own 24 hour urine volume?
- Content and synthesis of glycolytic enzymes and creatine kinase in skeletal muscles and normal and dystrophic chickens.
- Disparate responses of cultured skeletal muscle cells and growing chicks to tripeptide aldehyde protease inhibitors and an in vivo interaction with ethanol
- Tissue culture studies of muscle disorders: Part 2. Biochemical studies, nerve‐muscle culture, metabolic myopathies, and animal models
- Fish muscle cytoskeletal network: its spatial organization and its degradation by an endogenous serine proteinase.
- Similarities in protein synthesis and degradation in normal and dystrophic muscle cultures.
- Elevated ammonia release from dystrophic chicken muscle cell and fibroblast cultures
- Errors in the Extra-Analytical Phases of Clinical Chemistry Laboratory Testing
Related papers
- Stabilizing effect of Ca2+ on myosin and myofibrils of squid mantle muscle as affected by heating conditions
- Biochemical susceptibility of myosin in chicken myofibrils subjected to hydroxyl radical oxidizing systems.
- Myofibrillar protein turnover. Synthesis rates of myofibrillar and sarcoplasmic protein fractions in different muscles and the changes observed during postnatal development and in response to feeding and starvation.
- Myofibrillar protein turnover: the proteasome and the calpains.
- Regulation of Ca2+-dependent protein turnover in skeletal muscle by thyroxine.
- Some paradoxical effects of inhibitors of protein synthesis on protein turnover in cultured human cells
- Effects of thyroxine on protein turnover in rat skeletal muscle.
- Characteristics of skeletal muscle growth and protein turnover in a fast-growing rat strain
- Turnover of liver ribosomes in fed and in fasted rats.