calpastatin

calpastatin

[¦kal·pə′stat·ən]
(cell and molecular biology)
A protein found in all cells that is both the specific inhibitor and substrate of calpains.
References in periodicals archive ?
Tenders are invited for Supply of Antibody Histone H3 (He2K9), Histone H4 (K5), Calpastatin Anitbody
Association of a single nucleotide polymorphism in the calpastatin gene with carcass and meat quality traits of beef cattle.
Obesity-associated dysregulation of calpastatin and MMP-15 in adiposederived stromal cells results in their enhanced invasion.
Greenbaum and his collaborators examined the crystal structure of calpastatin, a natural calpain inhibitor, for clues.
Autoantigens defined by experimental serum and B-cell analysis in RA syndromes in animals and humans (10) Type/nature Specificity Autoantigen Citrulline-containing peptide Keratin Perinuclear factor Savoy antigen Filaggrin Human leukocyte antigen Calpastatin Immunoglobulin (rheumatoid factor) Calreticulin Antineutrophil cytoplasmic antigen Antinuclear antibody Immunoglobulin heavy-chain protein / p68 Heteronuclear ribonucleoprotein A2 (RA33) Glucose-6-phosphate isomerase Cartilage (organ Collagen type II specific) Chondrocyte antigen 65 Large aggregating chondroitin sulfate proteoglycan (aggrecan) Human chondrocyte glycoprotein 39 Cartilage oligomeric matrix protein Non-autoantigens Bacterial heat shock protein
Effects of calpastatin and (micro)-calpain markers in beef cattle on tenderness traits.
The University of Missouri-Columbia (MU) has been developing a novel biosensor technique to predict meat tenderness through the detection of calpastatin.
Although [micro]-calpain causes the protein degradation that improves tenderness, it's actually the activity of the protein calpastatin that determines how much calpain is active--and thus how tender the steak will be.
Goldberg E (1999) Calpastatin testis-specific isoform peptides for contreceptive vaccines and fertility diagnosis.
There is evidence to show that proteasome and calpain inhibitors such as MG132, lactacystin, and calpastatin are potent inhibitors of NF-[kappa]B activation.
This is due to the fact that a greater calpastatin activity is commonly observed in Zebu cattle, which inhibits calpain activity leading to a less tenderization of beef (Curi et al.
Shackelford found that although [mu]-calpain causes the protein degradation that improves tenderness, it's actually the activity of a protein called calpastatin that determines how much calpain is active--and thus how tender the steak will be.