Results 161 to 170 of about 26,568 (204)

μ-Calpain and calpain-3 are not autolyzed with exhaustive exercise in humans

American Journal of Physiology-Cell Physiology, 2006
μ-calpain and calpain-3 are Ca2+-dependent proteases found in skeletal muscle. Autolysis of calpains is observed using Western blot analysis as the cleaving of the full-length proteins to shorter products. Biochemical assays suggest that μ-calpain becomes proteolytically active in the presence of 2–200 μM Ca2+. Although calpain-3 is poorly understood,
Murphy, Robyn., Snow, Rodney., Lamb, Graham.   +2 more
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MEF2A regulates Calpain 3 expression in L6 myoblasts

Gene, 2018
Calpain 3 (Capn3), a skeletal muscle-specific member of the calpain family, executes some non-proteolytic functions besides its role as a Ca2+-regulated proteolytic enzyme. Previously, we found that changes in Capn3 expression were linearly correlated with the degree of muscular atrophy following reversible sciatic nerve injury and that knockdown of ...
Ronghua Wu, Jun Wang, Jian Yao, Zhangji Dong, Yan Liu, Mei Liu   +5 more
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Calpain 3 deficiency presenting as fibre type disproportion

Neuropathology and Applied Neurobiology, 2009
No abstract ...
VATTEMI, Gaetano Nicola, TONIN, PAOLA, Neri M., MARINI, Matteo, Gualandi F., GUGLIELMI, Valeria, Ferlini A., TOMELLERI, Giuliano   +7 more
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ADULTS WITH EOSINOPHILIC MYOSITIS AND CALPAIN-3 MUTATIONS

Neurology, 2008
A recent report found that six patients who presented with eosinophilic myositis in childhood actually had a calpainopathy (LGMD 2A).1 I have encountered two patients previously diagnosed with adult-onset eosinophilic polymyositis who had mutations in the calpain-3 gene ( CAPN3 ). ### Case reports. #### Case 1. A 22-year-old woman presented with a 1-
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Calpain 3 is expressed in astrocytes of rat and Microcebus brain

Journal of Chemical Neuroanatomy, 2003
The calcium-dependent protease calpain is involved in numerous functions, including the control of cell survival, plasticity and motility. Whereas the isoforms calpain 1 and 2 have been described as ubiquitously expressed enzymes, calpain 3 has been called "muscle-specific", although trace amounts of calpain 3 mRNA have been detected by Northern blot ...
König, Norbert, Raynaud, Fabrice, Feane, Helen, Durand, Micheline, Mestre-Francés, Nadine, Rossel, Mireille, Ouali, Ahmed, Benyamin, Yves   +7 more
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Ca²⁺ Dependency of Calpain 3 (p94) Activation

Biochemistry, 2006
Calpain 3, commonly called p94 in the literature, is the abundant skeletal muscle-specific calpain that is genetically linked to limb girdle muscular dystrophy type 2A. Recently, we showed that p94's insertion sequence 1 (IS1) is a propeptide that must be autoproteolytically cleaved to provide access of substrates and inhibitors to the enzyme's active ...
Beatriz E, García Díaz, Sherry, Gauthier, Peter L, Davies   +2 more
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Calpain 3/p94 is not involved in postmortem proteolysis.

Journal of animal science, 2005
Studies on the correlation between expression and/or autolysis of calpain and postmortem proteolysis in muscle have provided conflicting evidence regarding the possible role of calpain 3 in postmortem tenderization of meat. Thus, the objective of this research was to test the effect of postmortem storage on proteolysis and structural changes in muscle ...
Geesink, M., Taylor, Richard, Koohmaraie, M.   +2 more
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Calpain-3 is activated following eccentric exercise

Journal of Applied Physiology, 2009
to the editor: In a recent article by Lehti et al. ([3][1]) the effect of fatiguing exercise on the mRNA expression of a number of skeletal muscle proteins was examined. In the discussion it was stated that in a study conducted by our laboratory, calpain-3 mRNA was increased 24 h after a bout ...
Lamb, Graham., Murphy, Robyn Maree.
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Calpain-3 Deficiency Causes a Mild Muscular Dystrophy in Childhood

Neuropediatrics, 1997
Among our 20 families with LGMD2, 10 were documented to have muscle-specific calcium-activated neutral protease 3 (calpain-3) deficiency. Consanguinity was present in all. The current ages of the index cases were between 12 and 23 years, and there were additional nine members affected.
H, Topaloğlu, P, Dinçer, I, Richard, Z, Akçören, D, Alehan, S, Ozme, M, Cağlar, A, Karaduman, J A, Urtizberea, J S, Beckmann   +9 more
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Immunohistochemical analysis of calpain 3: Advantages and limitations in diagnosing LGMD2A

Neuromuscular Disorders, 2009
Immunoblot is currently the preferred laboratory test to assist the diagnosis of limb-girdle muscular dystrophy (LGMD) 2A (calpainopathy). To assess whether immunohistochemistry may offer a reliable alternative screening we used two antibodies, Calp3-2C4 (exon 1) and Calp3-12A2 (exon 8), to label blots and sections of skeletal muscle from controls and ...
Charlton R, Henderson M, Richards J, Hudson J, Straub V, Bushby K, Barresi R   +6 more
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