Results 171 to 180 of about 4,120 (216)
Some of the next articles are maybe not open access.
Immunoaffinity purification of calpastatin and calpastatin constructs
BBA - Proteins and Proteomics, 2002It has been difficult to purify calpastatin without using a step involving heating to 90-100 degrees C. Preparations of calpastatin obtained after heating often contain several polypeptides that have been ascribed to proteolytic degradation. Because calpastatin is highly susceptible to proteolytic degradation and several different calpastatin isoforms ...
Valery F Thompson, Darrel E Goll
exaly +3 more sources
Correlation between a novel calpastatin biosensor and traditional calpastatin assay techniques
Biosensors and Bioelectronics, 2008An optical fiber biosensor to detect calpastatin has been investigated as a preliminary step in developing tenderness detection instrumentation. Longissimus dorsi samples were taken from beef carcasses (n=21) at 0, 24, 36 and 48h postmortem. Muscle homogenates were assayed for calpastatin activity using traditional methods and an optical fiber ...
Sheila A Grant, C L Lorenzen
exaly +3 more sources
Calpain–calpastatin system and cancer progression
Biological Reviews, 2021ABSTRACTThe calpain system is required by many important physiological processes, including the cell cycle, cytoskeleton remodelling, cellular proliferation, migration, cancer cell invasion, metastasis, survival, autophagy, apoptosis and signalling, as well as the pathogenesis of a wide range of disorders, in which it may function to promote ...
Hong Nian, Binyun Ma
openaire +2 more sources
Interaction of calpastatin with calpain: a review
Biological Chemistry, 2004Calpastatin is a multiheaded inhibitor capable of inhibiting more than one calpain molecule. Each inhibitory domain of calpastatin has three subdomains, A, B, and C; A binds to domain IV and C binds to domain VI of the calpains. Crystallographic evidence shows that binding of C to domain VI involves hydrophobic interactions at a site near the first EF ...
Amanda, Wendt +2 more
openaire +2 more sources
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)
openaire +2 more sources
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)
openaire +2 more sources
American Journal of Physiology - Renal Physiology, 2000 The interaction between the cysteine proteases calpain and caspases during renal ischemia-reperfusion (I/R) was investigated. An increase in the activity of calpain, as determined by 1) the appearance of calpain-mediated spectrin breakdown products and 2)
Charles L Edelstein
exaly +2 more sources
Modulation of the Calpain Autoproteolysis by Calpastatin and Phospholipids
Biochemical and Biophysical Research Communications, 1996The 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 +4 more
openaire +3 more sources
cDNA Cloning of Human Calpastatin: Sequence Homology Among Human, Pig, and Rabbit Calpastatins
Journal of Enzyme Inhibition, 1989cDNA 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 +9 more
openaire +2 more sources
Calpain and calpastatin activity in the optic pathway
Neuroscience Letters, 1990The 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
openaire +2 more sources
Calpain and calpastatin in rabbit corneal epithelium
Current Eye Research, 1990The 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 +4 more
openaire +2 more sources