Degradation of myofibrillar proteins by cathepsins B and D.
Cathepsin B and cathepsin D were purified from rat liver and skeletal muscle. Electrophoretic analyses revealed that the enzymes were highly purified, and isoelectric focusing demonstrated multiple forms of both enzymes. Purified actin and myosin, as well as actin and myosin in myofilaments and myofibrils, were degraded by the purified cathepsins B and D. Degradation of myosin was completely blocked by the cathepsin B and D inhibitors, leupeptin and pepstatin, respectively. Cathepsins B and D were visualized by electron microscopy, using CBZ-Ala- Arg-Arg-4-methoxy-beta-naphthylamine and BZ-Arg-Gly-Phe-Leu-4-methoxy-beta-naphthylamine as substrates.
D000818:Animals; D002403:Cathepsins / Q000378:metabolism*; D006168:Guinea Pigs; D008099:Liver / Q000201:enzymology; D008247:Lysosomes / Q000201:enzymology / Q000648:ultrastructure; D009124:Muscle Proteins / Q000378:metabolism; D009132:Muscles / Q000201:enzymology / Q000648:ultrastructure; D009210:Myofibrils; D051381:Rats; D014811:Vitamin E Deficiency / Q000201:enzymology
D009124:Muscle Proteins; D002403:Cathepsins