Resumen de Nuevo SNP de la calpastatina (CAST) asociado con la terneza de la carne de bovino
L.P. Iguacel, Jorge Hugo Calvo Lacosta, Jackeline Karsten Kirinus, M. Serrano, Guillermo Ripoll García, Isabel Casasús Pueyo, Margalida Joy Torrens, L. Pérez Velasco, P. Sarto, Pere Albertí Lasalle, Mireia Blanco Alibés
Calpastatin (CAST) inhibits μ- and m-calpain activity and, therefore, regulates post-mortem proteolysis, being some SNPs in CAST gen associated to meat tenderness. In this work, a new SNP located at exon 7 (position BTA29: 98535683 on UMD 3.0) was associated to meat tenderness (P= 0.001). Beef from GG genotype was tenderer than that from AG and AA genotypes, which had similar tenderness. This mutation change the amino acid sequence at position Thr182Ala and could change the electrostatic charges localized in the interacting regions between the calpastatin L-domain and calpain. Moreover, heterozygous genotypes did not show either differences with the tender genotype or intermediate tenderness indicating an autosomal recessive inheritance effect of the Thr182Ala mutation for beef tenderness. The effect of the genotype of the Thr182Ala mutation on tenderness was higher (0.65 SD and 0.84 SD for the Total and Parda de Montaña populations, respectively) than those found previously for other SNPs in the CAST gene. Further studies are necessary to test the effect of the CAST Thr182Ala genotypes on calpastatin activity to confirm the effects of this new SNP found in the current experiment.
