نتایج جستجو برای: calpastatin

تعداد نتایج: 596  

Journal: :American journal of physiology. Gastrointestinal and liver physiology 2004
Heike Weber Ludwig Jonas Saskia Hühns Peter Schuff-Werner

Calpain, a calcium-dependent cytosolic cysteine protease, is implicated in a multitude of cellular functions but also plays a role in cell death. Recently, we have shown that two ubiquitous isoforms, termed micro-calpain and m-calpain, are expressed in rat pancreatic acinar cells and that calcium ionophore-induced calpain activation leads to acinar cell injury. On the basis of these observation...

2012
M. AHANI AZARI E. DEHNAVI S. YOUSEFI L. SHAHMOHAMADI

Calpains play a major role in post mortem tenderization and calpastatin is the endogenous inhibitor of calpain proteases and regulates the rate and extent of post mortem tenderization. Myostatin is an inhibitor of skeletal muscle growth and a mutation in the gene coding region leads to increased muscling. Therefore, they are considered as candidate genes for meat and growth traits. Blood sample...

Journal: :American journal of physiology. Regulatory, integrative and comparative physiology 2005
Wei Wei Moin U Fareed Amy Evenson Michael J Menconi Hongmei Yang Victoria Petkova Per-Olof Hasselgren

We examined the influence of sepsis on the expression and activity of the calpain and caspase systems in skeletal muscle. Sepsis was induced in rats by cecal ligation and puncture (CLP). Control rats were sham operated. Calpain activity was determined by measuring the calcium-dependent hydrolysis of casein and by casein zymography. The activity of the endogenous calpain inhibitor calpastatin wa...

Journal: :Journal of animal science 2001
E F Delgado G H Geesink J A Marchello D E Goll M Koohmaraie

Activities of mu- and m-calpain and of calpastatin were measured at four different times during postmortem storage (0, 1, 3, and 10 d) in three muscles from either callipyge or noncallipyge (normal) sheep. The weights of two muscles, the biceps femoris and the longissimus, are greater in the callipyge phenotype, whereas the weight of the infraspinatus is not affected. The activity of m-calpain ...

Journal: :Meat science 2001
E Veiseth M Koohmaraie

The effect of extraction buffer on extractable calpain and calpastatin activity in postmortem muscles was examined. Muscles were removed from ovine carcasses 24 h after slaughter and extracted with three volumes of two extraction buffers containing 20 (pH 7.5) and 100 (pH 8.3) mM Tris. There was a significant difference in pH of the muscle homogenates, having a pH of 5.84 and 7.58 for 20 and 10...

Journal: :Cardiovascular research 2013
Yanpeng Wang Dong Zheng Meng Wei Jian Ma Yong Yu Ruizhen Chen James C Lacefield Huaxi Xu Tianqing Peng

AIMS Doxorubicin causes damage to the heart, which may present as cardiomyopathy. However, the mechanisms by which doxorubicin induces cardiotoxicity remain not fully understood and no effective prevention for doxorubicin cardiomyopathy is available. Calpains, a family of calcium-dependent thiol-proteases, have been implicated in cardiovascular diseases. Their activities are tightly controlled ...

Journal: :Journal of animal science 1993
T L Kendall M Koohmaraie J R Arbona S E Williams L L Young

The effects of bovine skeletal muscle m-calpain and calpastatin on the degradation of casein and isolated bovine myofibrils were characterized under various pH values (7.0, 6.2, 5.7) and ionic strengths (32 to 400 mM KCl) at 25 degrees C. Caseinolytic assays indicated that m-calpain activity increased with increasing pH (P < .01) but decreased with increasing ionic strength (P < .01). Regardles...

Journal: :The Journal of Cell Biology 1998
David A. Potter Jennifer S. Tirnauer Richard Janssen Dorothy E. Croall Christina N. Hughes Kerry A. Fiacco James W. Mier Masatoshi Maki Ira M. Herman

Previous studies suggest that the Ca2+-dependent proteases, calpains, participate in remodeling of the actin cytoskeleton during wound healing and are active during cell migration. To directly test the role that calpains play in cell spreading, several NIH-3T3- derived clonal cell lines were isolated that overexpress the biological inhibitor of calpains, calpastatin. These cells stably overexpr...

2012
M Niapour C Farr M Minden S A Berger

Calpains are intracellular cysteine proteases that have crucial roles in many physiological and pathological processes. Elevated calpain activity has been associated with many pathological states. Calpain inhibition can be protective or lethal depending on the context. Previous work has shown that c-myc transformation regulates calpain activity by suppressing calpastatin, the endogenous negativ...

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