Calpastatin
Mostrando 1-12 de 21 artigos, teses e dissertações.
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1. Perfil proteômico muscular de bovinos inteiros da raça Nelore / Muscle proteomic profile of Nellore bulls
The present work aimed to study beef quality (Longissimus dorsi) from Nellore bull through two-dimensional proteomic analysis. For this purpose, two specific objectives were proposed: (i) to study the proteolysis of meat at different aging times, if 24 hours, seven and 14 days, and (ii) to study the protein profile of meat from Nellore bull with contrasting
IBICT - Instituto Brasileiro de Informação em Ciência e Tecnologia. Publicado em: 16/07/2012
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2. The inhibitory role of sympathetic nervous system in the Ca2+-dependent proteolysis of skeletal muscle
Mammalian cells contain several proteolytic systems to carry out the degradative processes and complex regulatory mechanisms to prevent excessive protein breakdown. Among these systems, the Ca2+-activated proteolytic system involves the cysteine proteases denoted calpains, and their inhibitor, calpastatin. Despite the rapid progress in molecular research on
Brazilian Journal of Medical and Biological Research. Publicado em: 2009-01
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3. Protein metabolism, body chemical composition, carcass traits and meat quality of Nellore steers (Bos indicus) as a function of their residual feed intake / Metabolismo protéico, composição corporal, características de carcaça e qualidade de carne de novilhos Nelore (Bos indicus) em função de seu consumo alimentar residual
Residual feed intake (RFI) is a feed efficiency trait that is independent of growth rate and mature weight. Genetic improvement in RFI may reduce the costs of feeding cattle, however a better understanding of biological processes underlying variation in RFI is necessary. Moreover, associations between RFI and carcass quality have been poorly investigated in
Publicado em: 2009
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4. Caracterização da freqüência de polimorfismos em genes ligados à maciez da carne em bovinos da raça Nelore / Polymorphism frequencies characterization in candidate genes linkage with meat tenderness in Nellore beef cattle
O objetivo deste trabalho foi avaliar o potencial de utilização de marcadores moleculares em genes candidatos da calpaína (CAPN) e calpastatina (CAST) como ferramenta auxiliar para programas de melhoramento de características relacionadas ao crescimento e maciez da carne. Foram avaliados 605 bovinos da raça Nelore, pertencentes à Agropecuária CFM Ltda
Publicado em: 2008
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5. Association of CAPN1 and CAST gene polymorphisms with meat tenderness in Bos taurus beef cattle from Argentina
The activity of the calpains/calpastatin proteolytic system is closely related to the postmortem tenderization of meat. We investigated the association between beef tenderness and single nucleotide polymorphism (SNP) markers on the CAPN1 gene (SNP316, alleles C/G; SNP530 alleles A/G) and the CAST gene 3' untranslated region (SNP2870, alleles A/G). We sampled
Genetics and Molecular Biology. Publicado em: 2007
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6. Autoantibodies to calpastatin (an endogenous inhibitor for calcium-dependent neutral protease, calpain) in systemic rheumatic diseases.
We identified an autoantibody that reacts with calpastatin [an inhibitor protein of the calcium-dependent neutral protease calpain (EC 3.4.22.17)]. In early immunoblot studies, sera from patients with rheumatoid arthritis (RA) recognized unidentified 60-, 45-, and 75-kDa proteins in HeLa cell extracts. To identify these autoantigens, we used patient sera to
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7. v-Src-Induced Modulation of the Calpain-Calpastatin Proteolytic System Regulates Transformation
v-Src-induced oncogenic transformation is characterized by alterations in cell morphology, adhesion, motility, survival, and proliferation. To further elucidate some of the signaling pathways downstream of v-Src that are responsible for the transformed cell phenotype, we have investigated the role that the calpain-calpastatin proteolytic system plays during
American Society for Microbiology.
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8. Detection and expression of a cDNA clone that encodes a polypeptide containing two inhibitory domains of human calpastatin and its recognition by rheumatoid arthritis sera.
RA is the most frequent and most destructive inflammatory arthropathy. Rheumatoid factors, in spite of their lack of disease specificity, are important serological markers for RA and appear important in its immunopathogenesis as well. In search of more disease-specific autoimmune systems, we have screened a human placenta lambda gt11 cDNA expression library
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9. Role of calpain in adipocyte differentiation
Evidence is presented that the calcium-activated protease, calpain, is required for differentiation of 3T3-L1 preadipocytes into adipocytes induced by methylisobutylxanthine (a cAMP phosphodiesterase inhibitor), dexamethasone, and insulin. Calpain is expressed by preadipocytes and its level falls during differentiation. Exposure of preadipocytes to the
The National Academy of Sciences.
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10. Endogenous inhibitor for calcium-dependent cysteine protease contains four internal repeats that could be responsible for its multiple reactive sites.
A cDNA encoding an endogenous inhibitor, termed calpastatin, for calcium-dependent cysteine protease (calpain, EC 3.4.22.17) was cloned by screening rabbit cDNA libraries with a synthetic oligodeoxynucleotide probe based on the partial amino acid sequence of the purified protein. The deduced amino acid sequence contains 718 amino acid residues (Mr, 76,964),
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11. Role of calpain in skeletal-muscle protein degradation
Although protein degradation is enhanced in muscle-wasting conditions and limits the rate of muscle growth in domestic animals, the proteolytic system responsible for degrading myofibrillar proteins in skeletal muscle is not well defined. The goals of this study were to evaluate the roles of the calpains (calcium-activated cysteine proteases) in mediating mu
The National Academy of Sciences.
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12. Proteolysis by calpains: a possible contribution to degradation of p53.
p53 is a short-lived transcription factor that is frequently mutated in tumor cells. Work by several laboratories has already shown that the ubiquitin-proteasome pathway can largely account for p53 destruction, at least under specific experimental conditions. We report here that, in vitro, wild-type p53 is a sensitive substrate for milli- and microcalpain, w