BIOMAT Database Logo BIOMAT Database Logo

Serine protease in mice with hereditary muscular dystrophy. 1978

Y Sanada, and N Yasogawa, and N Katunuma

The activities of serine protease, cathepsin B1, ornithine aminotransferase, and aldolase in skeletal muscles of mice with hereditary muscular dystrophy and their normal litter mates were studied. In dystrophic muscle, the specific and total activities of serine protease were much higher than in normal muscle, and the specific activities, but not the total activities, of cathepsin B1 and ornithine aminotransferase were twice those in normal muscle, and several new fragments, which are normally formed by limited proteolysis, were found in dystrophic muscle. When myofibrillar proteins of normal and dystrophic muscles were incubated with highly purified serine protease, their myosin, alpha-actinin and tropomyosin disappeared completely.

UI MeSH Term Description Entries
D009124 Muscle Proteins The protein constituents of muscle, the major ones being ACTINS and MYOSINS. More than a dozen accessory proteins exist including TROPONIN; TROPOMYOSIN; and DYSTROPHIN. Muscle Protein,Protein, Muscle,Proteins, Muscle
D009137 Muscular Dystrophy, Animal MUSCULAR DYSTROPHY that occurs in VERTEBRATE animals. Animal Muscular Dystrophies,Animal Muscular Dystrophy,Dystrophies, Animal Muscular,Dystrophy, Animal Muscular,Muscular Dystrophies, Animal
D009210 Myofibrils The long cylindrical contractile organelles of STRIATED MUSCLE cells composed of ACTIN FILAMENTS; MYOSIN filaments; and other proteins organized in arrays of repeating units called SARCOMERES . Myofilaments,Myofibril,Myofilament
D009953 Ornithine-Oxo-Acid Transaminase A pyridoxal phosphate enzyme that catalyzes the formation of glutamate gamma-semialdehyde and an L-amino acid from L-ornithine and a 2-keto-acid. EC 2.6.1.13. Ornithine Aminotransferase,Ornithine Transaminase,L-Ornithine-2-Oxo-Acid Aminotransferase,L-Ornithine-2-Oxoglutarate Aminotransferase,Ornithine Ketoacid Aminotransferase,Ornithine-2-Ketoglutarate Aminotransferase,Ornithine-Keto-Acid-Transaminase,Ornithine-Ketoacid-Transaminase,Pyrroline-5-Carboxylate Synthase,Aminotransferase, L-Ornithine-2-Oxo-Acid,Aminotransferase, L-Ornithine-2-Oxoglutarate,Aminotransferase, Ornithine,Aminotransferase, Ornithine Ketoacid,Aminotransferase, Ornithine-2-Ketoglutarate,Ketoacid Aminotransferase, Ornithine,L Ornithine 2 Oxo Acid Aminotransferase,L Ornithine 2 Oxoglutarate Aminotransferase,Ornithine 2 Ketoglutarate Aminotransferase,Ornithine Keto Acid Transaminase,Ornithine Ketoacid Transaminase,Ornithine Oxo Acid Transaminase,Pyrroline 5 Carboxylate Synthase,Synthase, Pyrroline-5-Carboxylate,Transaminase, Ornithine,Transaminase, Ornithine-Oxo-Acid
D010450 Endopeptidases A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS. Endopeptidase,Peptide Peptidohydrolases
D002403 Cathepsins A group of lysosomal proteinases or endopeptidases found in aqueous extracts of a variety of animal tissues. They function optimally within an acidic pH range. The cathepsins occur as a variety of enzyme subtypes including SERINE PROTEASES; ASPARTIC PROTEINASES; and CYSTEINE PROTEASES. Cathepsin
D005634 Fructose-Bisphosphate Aldolase An enzyme of the lyase class that catalyzes the cleavage of fructose 1,6-biphosphate to form dihydroxyacetone phosphate and glyceraldehyde 3-phosphate. The enzyme also acts on (3S,4R)-ketose 1-phosphates. The yeast and bacterial enzymes are zinc proteins. (Enzyme Nomenclature, 1992) E.C. 4.1.2.13. Aldolase,Fructosediphosphate Aldolase,Aldolase A,Aldolase B,Aldolase C,Fructose 1,6-Bisphosphate Aldolase,Fructose 1,6-Bisphosphate Aldolase, Class II,Fructose 1-Phosphate Aldolase,Fructose Biphosphate Aldolase,Fructosemonophosphate Aldolase,1,6-Bisphosphate Aldolase, Fructose,Aldolase, Fructose 1,6-Bisphosphate,Aldolase, Fructose 1-Phosphate,Aldolase, Fructose Biphosphate,Aldolase, Fructose-Bisphosphate,Aldolase, Fructosediphosphate,Aldolase, Fructosemonophosphate,Fructose 1 Phosphate Aldolase,Fructose 1,6 Bisphosphate Aldolase,Fructose Bisphosphate Aldolase
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia

Related Publications

Y Sanada, and N Yasogawa, and N Katunuma
[Muscular dystrophy and serine protease].
November 1977, Nihon rinsho. Japanese journal of clinical medicine,
Y Sanada, and N Yasogawa, and N Katunuma
MYOSIN FROM MICE WITH HEREDITARY MUSCULAR DYSTROPHY.
January 1964, Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine (New York, N.Y.),
Y Sanada, and N Yasogawa, and N Katunuma
Phosphatase activities in mice with hereditary muscular dystrophy.
December 1966, Wakayama medical reports,
Y Sanada, and N Yasogawa, and N Katunuma
Enzyme studies in muscular dystrophy. III. In hereditary muscular dystrophy in mice.
October 1958, Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine (New York, N.Y.),
Y Sanada, and N Yasogawa, and N Katunuma
Nucleic acid metabolism in mice with hereditary muscular dystrophy.
August 1962, Archives of biochemistry and biophysics,
Y Sanada, and N Yasogawa, and N Katunuma
Evidence for a defective thiol protease inhibitor in skeletal muscle of mice with hereditary muscular dystrophy.
October 1986, Biochemistry and cell biology = Biochimie et biologie cellulaire,
Y Sanada, and N Yasogawa, and N Katunuma
Phosphoglucomutase activity in hereditary muscular dystrophy in mice.
January 1959, Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine (New York, N.Y.),
Y Sanada, and N Yasogawa, and N Katunuma
In vivo effects of protease inhibitors on chickens with hereditary muscular dystrophy.
April 1981, The Journal of clinical investigation,
Y Sanada, and N Yasogawa, and N Katunuma
PLASMA CREATINE KINASE ACTIVITY IN MICE WITH HEREDITARY MUSCULAR DYSTROPHY.
January 1962, Enzymologia biologica et clinica,
Y Sanada, and N Yasogawa, and N Katunuma
Histamine in the skin of mice with hereditary muscular dystrophy.
January 1965, Texas reports on biology and medicine,
Copied contents to your clipboard!