Consulta: subjectFacets:"Calpain"
Registros recuperados: 6
Data/hora: 13/06/2024 06:52:32

Meat tenderness genetic polymorphisms occurrence and distribution in five Zebu breeds in Mexico
Provedor de dados: 69
Autores: Parra-Bracamonte,Gaspar Manuel; Martínez-González,Juan C; Sifuentes-Rincón,Ana M; Moreno-Medina,Victor R; Ortega-Rivas,Eligio.
Background The Zebu cattle are represented by a diverse group of breeds in México. Traditionally these breeds have been associated with the tough beef characteristic. Validated genetic markers have the potential to be included in marker-assisted selection and management programs in order to improve traits such as beef tenderness. The incidence and distribution of Calpain and Calpastatin polymorphisms strongly associated with beef tenderness were estimated in registered cattle of five Zebu breeds in Mexico. Results A low and in some cases null frequency of favorable C allele of CAPN316 was determined in all breeds. Conversely, a more equilibrated frequency in CAPN4751 and CAST loci was observed. Conclusions Although the relatively low occurrence of...
Tipo: Journal article
Palavras-chave: Calpain; Calpastatin; Frequencies; Genotype; SNP.
Ano: 2015
URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582015000500007

Calpain and cathepsin activities in post mortem fish and meat muscles
Provedor de dados: 5
Autores: Cheret, Romuald; Delbarre Ladrat, Christine; De Lamballerie Anton, Marie; Verrez-bagnis, Veronique.
Post mortem tenderization is one of the most unfavourable quality changes in fish muscle and this contrasts with muscle of mammalian meats. The tenderization can be partly attributed to the acid lysosomal cathepsins and cytosolic neutral calcium-activated calpains. In this study, these proteases from fish and bovine muscles were quantified and compared. The cathepsin B and L activities were in more important amounts in sea bass white muscle than in bovine muscle. On the other hand, cathepsin D activity was 1.4 times higher in meat that in fish muscle, while cathepsin H was negligible in both muscles. Calpain activities were similar in both types of muscle. Moreover, calpastatin (calpain endogenous inhibitor) level is 3.9 times higher in sea bass white...
Tipo: Text
Palavras-chave: Meat; Fish; Protease; Cathepsin; Calpain.
Ano: 2007
URL: http://archimer.ifremer.fr/doc/2007/publication-3646.pdf

Proteolytic potential in white muscle of sea bass (Dicentrarchus labrax L.) during post mortem storage on ice: time-dependent changes in the activity of the components of the calpain system
Provedor de dados: 5
Autores: Delbarre Ladrat, Christine; Verrez-bagnis, Veronique; Noel, Joelle; Fleurence, Joel.
The variations in the amounts of milli-calpain and its specific inhibitor in the white muscle of sea bass (Dicentrarchus labrax) during storage at 4 degreesC for up to 7 days were determined after separation by hydrophobic chromatography on a Phenyl Sepharose vel. There was a significant decline in post-slaughter m-calpain activity with an important inter-individual variability in the rate of decrease of the total activity. In contrast with the calpastatin of mammalian post mortem muscles, calpastatin remained constant within fish muscles after death. The initial levels of protease and inhibitor activities, and their behaviour through post mortem storage. are discussed and implications for the mechanism of tenderisation of fish muscle are suggested. (C)...
Tipo: Text
Palavras-chave: Proteolysis; Post mortem; Fish muscle; Calpain; Calpastatin; Neutral calcium dependent protease.
Ano: 2004
URL: http://archimer.ifremer.fr/doc/2004/publication-1683.pdf

In vitro proteolysis of myofibrillar and sarcoplasmic proteins of European sea bass (Dicentrarchus Labrax L) by an endogenous m-calpain
Provedor de dados: 5
Autores: Verrez-bagnis, Veronique; Delbarre Ladrat, Christine; Noel, Joelle; Fleurence, Joel.
The effects of m-calpain isolated from the skeletal muscle of sea bass on sarcoplasmic and myofibrillar proteins isolated from the same tissue were examined in vitro. Incubation of sarcoplasmic proteins with m-calpain resulted in only a slight decrease (0.7 kDa) in the molecular weight (MW) of a 26.5 kDa protein. Degradation of myofibrils, monitored by quantification of TCA-soluble peptides generated, resulted in the maximum amount of peptides being generated after 1 h of incubation at 25degreesC. Noticeable modifications in the SDS-PAGE profile of digested myofibrils were observed, including partial denaturation of myosin heavy chain and the release of tropomyosin, similar to69 and similar to27 kDa doublet bands and a few polypeptides of MW lower than 20...
Tipo: Text
Palavras-chave: Dicentrarchus labrax L; Proteolysis; Sarcoplasmic protein; Calpain; Myofibrillar protein.
Ano: 2002
URL: http://archimer.ifremer.fr/doc/2002/publication-1108.pdf

Regulation of cell polarity by controlled proteolytic systems
Provedor de dados: 48
Autores: Bórquez,Daniel A; González-Billault,Christian.
Epithelial and neuronal cells are highly asymmetric, with discrete regions responsible for different roles that underlie the generation of specific compartments within cells that are distinct in biochemical composition, structure, and morphology that ultimately lead to distinct functions. Controlled and specific molecular targeting and sorting have been studied to understand the generation of asymmetric domains inside cells. Recently, a new and complementary explanation has emerged to account for the generation of domains that are enriched by a subset of proteins or polarization determinants: local proteolysis. In this review, we discuss the most conspicuous proteolytic systems that may contribute to the generation of cell polarity, namely the...
Tipo: Journal article
Palavras-chave: Calpain; Neuronal polarity; Proteolytic systems; Ubiquitin proteasome.
Ano: 2011
URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602011000100005

The inhibitory role of sympathetic nervous system in the Ca2+-dependent proteolysis of skeletal muscle
Provedor de dados: 56
Autores: Navegantes,L.C.C.; Baviera,A.M.; Kettelhut,I.C.
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 calpains and calpastatin, the physiological role and regulatory mechanisms of these proteins remain obscure. Interest in the adrenergic effect on Ca2+-dependent proteolysis has been stimulated by the finding that the administration of β2-agonists induces muscle hypertrophy and prevents the loss of muscle mass in a variety of pathologic conditions in which calpains are activated. This review summarizes...
Tipo: Info:eu-repo/semantics/article
Palavras-chave: Epinephrine; Norepinephrine; Calpastatin; Calpain; Skeletal muscle.
Ano: 2009
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2009000100005