Results 171 to 180 of about 4,652 (211)

Calpain and calpastatin

Trends in Biochemical Sciences, 1983
Calpain is a Ca2(+)-dependent cysteine endopeptidase and calpastatin is a calpain-specific endogenous inhibitor protein. Both calpain and calpastatin are very widely distributed in various animal tissues and cells. Low (microM) Ca2(+)-requiring calpain I and high (mM) Ca2(+)-requiring calpain II are known to exist. Calpain consists of one heavy (80 kDa)
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Modulation of the Calpain Autoproteolysis by Calpastatin and Phospholipids

Biochemical and Biophysical Research Communications, 1996
The Ca-induced autoproteolysis calpain proceeds through the sequential formation of two forms of active enzyme with molecular masses of 78 kD and 75 kD, respectively. The autolysed calpains are produced by the cleavage of the peptide bond between Ser15-Ala16 and then between Gly27-Leu28.
MELLONI, EDON, MICHETTI, MAURO, SALAMINO, FRANCA, MINAFRA, ROBERTO, PONTREMOLI, SANDRO   +4 more
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cDNA Cloning of Human Calpastatin: Sequence Homology Among Human, Pig, and Rabbit Calpastatins

Journal of Enzyme Inhibition, 1989
cDNA of human calpastatin, an inhibitor protein specific for calpain (EC 3.4.22.17; Ca2(+)-dependent cysteine proteinase) was isolated by screening of a library prepared from human liver mRNA with pig calpastatin cDNA fragment as a probe. The primary structure of human calpastatin was deduced from the nucleotide sequence of the cDNA and compared with ...
K, Asada, Y, Ishino, M, Shimada, T, Shimojo, M, Endo, F, Kimizuka, I, Kato, M, Maki, M, Hatanaka, T, Murachi   +9 more
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Calpain and calpastatin in rabbit corneal epithelium

Current Eye Research, 1990
The purpose of this study was to provide a direct assay for calpain and its endogenous inhibitor calpastatin in normal rabbit epithelium. Corneal epithelial extracts were fractionated by DEAE (1) chromatography on HPLC. Fractions were analyzed for calpain by ELISA, immunoblotting, and caseinolytic enzyme activity with FITC-labeled casein.
T R, Shearer, M, Azuma, L L, David, Y, Yamagata, T, Murachi   +4 more
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Microinjection of Calpastatin Inhibits Fusion in Myoblasts

Experimental Cell Research, 1999
Rat satellite cells (RSC) were microinjected with purified calpastatin or m-calpain, and myoblasts from a C2C12 mouse line were microinjected with purified calpastatin. Microinjection with calpastatin completely prevented fusion of myoblasts from both sources, whereas microinjection with m-calpain significantly increased the rate of fusion of cultured ...
C J, Temm-Grove, D, Wert, V F, Thompson, R E, Allen, D E, Goll   +4 more
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Calpain and calpastatin activity in the optic pathway

Neuroscience Letters, 1990
The levels of the neutral proteolytic enzymes calpains and their endogenous inhibitor calpastatin were determined in the retina and in the retrobulbar optic pathway in the albino rabbit. The highest level of calpains was observed in the optic nerve with decreasing levels in the optic tract and superior colliculus. The level of calpastatin in the retina
K, Blomgren, J O, Karlsson
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Molecular diversity of calpastatin in mammalian organs

Biochemical and Biophysical Research Communications, 1984
The crude homogenates of various human and porcine organs were subjected to immunoelectrophoretic blot analysis using affinity-purified anti-calpastatin antibody which specifically reacts with human erythrocyte 70 kDa calpastatin. Multiple immuno-reactive bands were revealed which ranged from 100 to 50 kDa.
E, Takano, N, Yumoto, R, Kannagi, T, Murachi   +3 more
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Calpain and calpastatin regulate neutrophil apoptosis

Journal of Cellular Physiology, 1999
The average polymorphonuclear neutrophil (PMN) lives only a day and then dies by apoptosis. We previously found that the calcium-dependent protease calpain is required for apoptosis in several mouse models of cell death. Here we identify calpain, and its endogenous inhibitor calpastatin, as regulators of human neutrophil apoptosis. Cell death triggered
M K, Squier, A J, Sehnert, K S, Sellins, A M, Malkinson, E, Takano, J J, Cohen   +5 more
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Characterization of a functional domain of human calpastatin

Biochemical and Biophysical Research Communications, 1990
Expression plasmids were constructed from the cDNA of human calpastatin to examine the contribution to the inhibition of calpain of highly conserved sequences in each of four repetitive domains. A series of deletion derivatives of domain 1 proteins, truncated at either the amino or carboxy terminus, were produced in E. coli.
Takashi Uemori, Tomoko Shimojo, Kiyozo Asada, Tadao Asano, Fusao Kimizuka, Ikunoshin Kato, Masatoshi Maki, Masakazu Hatanaka, Takashi Murachi, Hiroyuki Hanzawa, Yoji Arata   +10 more
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Effects of genetic variants for the calpastatin gene on calpastatin activity and meat tenderness in Hanwoo (Korean cattle)

Meat Science, 2012
This study was designed to investigate the effects of calpastatin genotypes determined by PCR-SSCP (polymerase chain reaction-single strand conformation polymorphism) on calpastatin activity (CAC) and Warner-Bratzler Shear Force (WBS). Longissimus muscles were prepared from 379 Hanwoo bulls aged approximately 20months.
Hoyoung, Chung, Michael, Davis
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