Original Research ARTICLE
Association of µ-calpain and calpastatin polymorphisms with meat tenderness in a Brahman-Angus population
- 1Animal Sciences, University of Florida, United States
Autogenous proteolytic enzymes of the calpain family are implicated in myofibrillar protein degradation. As a result, the µ-calpain gene and its specific inhibitor, calpastatin, have been repeatedly investigated for their association with meat quality traits in cattle; however, no functional mutation has been identified for these two genes. The objectives of this study were: 1) to assess breed composition effect on tenderness; 2) to perform a linkage disequilibrium (LD) analysis in µ-calpain and calpastatin genes as well as an association analyses with tenderness; and 3) to analyze putative functional SNPs inside the significant LD block for an effect on tenderness. Tenderness measurements and genotypes for 16 SNPs in µ-calpain gene and 28 SNPs in calpastatin gene from 673 steers were analyzed. A bioinformatic analysis identified “putative functional SNPs” inside the associated LD block - polymorphisms able to produce a physical and/or chemical change in the DNA, mRNA or translated protein in-silico. Breed composition had a significant (P<0.0001) effect on tenderness where animals with more than 80% Angus composition had the most tender meat. One 11-kb LD-block and three LD-blocks of 37, 17 and 14 kb in length were identified in the µ-calpain and calpastatin genes, respectively. Out of these, the LD-block 3 in calpastatin, tagged by SNP located at 7-98566391 and 7-98581038, had a significant effect on tenderness with the TG-CG diplotype being approximately 1 kg more tender than the toughest haplotype, TG-CG. A total of 768 SNPs in the LD-block 3 of calpastatin were included in the bioinformatic analysis, and 28 markers were selected as putative functional SNPs inside the LD-block 3 of calpastatin; however, none of them were polymorphic in this population. Out of 15 initial polymorphisms segregating inside the LD-block 3 of calpastatin in this population, markers ARSUSMARC116, Cast5, rs730723459, and rs210861835 were found to be significantly associated with tenderness.
Keywords: Bioinformatic analysis, Calpain, calpastatin, putative functional SNPs, Tenderness, transcription factor binding sites
Received: 16 Nov 2017;
Accepted: 07 Feb 2018.
Edited by:Tad S. Sonstegard, Recombinetics (United States), United States
Reviewed by:Dan Nonneman, Agricultural Research Service (USDA), United States
Gerson B. Mourão, University of São Paulo, Brazil
Copyright: © 2018 Leal Gutierrez, Elzo, Johnson, Scheffler, Scheffler and Mateescu. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
* Correspondence: Mr. Joel D. Leal Gutierrez, University of Florida, Animal Sciences, 2250 Shealy Dr, Gainesville, 32608, Florida, United States, email@example.com