Results 181 to 190 of about 4,120 (216)

Cardiac high molecular weight calmodulin-binding protein is homologous to calpastatin I and calpastatin II

Biochemical and Biophysical Research Communications, 2008
Calpastatin is an endogenous inhibitor of calpain, which has been implicated in various physiological and pathological processes. In the present study we determined the molecular and inhibitory properties of HMWCaMBP, calpastatin I, and calpastatin II. Western blot analysis with antibodies raised against either full length HMWCaMBP or internal peptides
Nisha Singh, Anuraag Shrivastav, Ashakumary Lakshmikuttyamma   +2 more
exaly   +3 more sources

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
openaire   +2 more sources

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
openaire   +2 more sources

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
openaire   +2 more sources

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
openaire   +2 more sources

The Calpain-Calpastatin System in Hematopoietic Cells

1989
Calpain I requires low Ca2+ for activation and calpain II requires high Ca2+. It was generally accepted that erythrocytes contain calpain I and calpastatin, but no calpain II. We have recently found, however, that nucleated chicken erythrocytes contain both calpains I and II in addition to calpastatin.
T, Murachi, T, Murakami, M, Ueda, I, Fukui, T, Hamakubo, Y, Adachi, M, Hatanaka   +6 more
openaire   +2 more sources

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
openaire   +2 more sources

Erythrocytic calpain-calpastatin system in Alzheimer’s disease

Aging Clinical and Experimental Research, 1996
Calpains, calcium activated neutral proteases (CANP), and calpastatin (CAST), their specific inhibitor, are involved in the proteolysis of amyloid precursor protein (APP), which is thought to be abnormal in Alzheimer's disease (AD). We studied the CANP/CAST system in erythrocytes of 14 clinically probable AD patients, 11 young and 14 old controls. CANP
L. Soldati, M. Alberoni, G. Bianchi, N. Canal, M. Franceschi   +4 more
openaire   +3 more sources

Single nucleotide polymorphisms in caprine calpastatin gene

Russian Journal of Genetics, 2013
The calpains and calpastatin (CAST) make up a major cytosolic proteolytic system, the calpain-calpastatin system, found in mammalian tissues. The relative levels of the components of the calpain-calpastatin system determine the extent of meat tenderization during postmortem storage.
R, Sharma, A, Maitra, A K, Pandey, L V, Singh, B P, Mishra   +4 more
openaire   +2 more sources

Relationships among calpastatin single nucleotide polymorphisms, calpastatin expression and tenderness in pork longissimus.

Animal genetics, 2010
Genome scans in the pig have identified a region on chromosome 2 (SSC2) associated with tenderness. Calpastatin is a likely positional candidate gene in this region because of its inhibitory role in the calpain system that is involved in postmortem tenderization.
A K, Lindholm-Perry, G A, Rohrer, J W, Holl, S D, Shackelford, T L, Wheeler, M, Koohmaraie, D, Nonneman   +6 more
openaire   +1 more source