calpain

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Related to Calpains: Cathepsins

calpain

[′kal‚pān]
(cell and molecular biology)
A calcium-dependent cysteine protease in the cytoplasm that is central to most processes in cell biology (plasma membrane-associated signaling events; cell proliferation, differentiation, activation, and communication; and programmed cell death). Its overactivation has been observed in muscular dystrophy, Alzheimer's disease, AIDS, cataract formation, multiple sclerosis, and arthritis.
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Calpain cleavage and inactivation of the sodium calcium exchanger-3 occur downstream of A13 in Alzheimer's disease.
Now, a team from the Perelman School of Medicine, University of Pennsylvania, in collaboration with the University of California at San Francisco and the Department of Biochemistry and Protein Function Discovery at Queen's University, has developed a unique approach to calpain inhibition by mimicking a natural reaction with a synthesized molecule.
Several molecular forms of the calpains exist, but the two major ones are calpain I and calpain II.
Calpains have been identified in the cochlea, and they are active during ischemic injury to cochlear tissues (139) and during noise-induced hearing loss.
Depending on cattle's genetic makeup, different levels of calpastatin exist in the meat and contribute to toughness by inhibiting an enzyme - calpain - in the postmortem aging, or tenderizing process.
We have been focused on calpain inhibition for DMD, and as a result of extensive research we believe that we have developed a unique, proprietary, safe and efficient, targeted calpain inhibitor.
Therefore, after the animal is slaughtered, there is a decrease in pH that activates calcium-dependent proteases, with increased activity of calpains and other proteolytic enzymes, causing a consequent effect on colour, texture, tenderness and water-holding capacity.
Subsequent studies at Mirinz showed that calpains, the major enzymes responsible for tenderness, degrade faster at temperatures above and below 15 C.
His research has been instrumental in proving the role of calcium-dependent proteases, or calpains, in the tenderization process.
9), (10) Calpains break down the protein structures that allow the muscle cell myofribrillar elements to line up correctly.