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Title: Mutations in calpastatin and µ-calpain are associated with meat tenderness, flavor and juiciness in Hanwoo (Korean cattle): Molecular modeling of the effects of substitutions on the calpastatin/µ-calpain complex
Contributor(s): Lee, Seung-Hwan (author); Kim, Seung-Chang (author); Yang, Boh-Suk (author); Hong, Seong-Koo (author); Chai, Han-Ha (author); Cho, Soo-Hyun (author); Kim, Hyeong-Cheol (author); Lim, Dajeong (author); Choi, Bong-Hwan (author); Dang, Chang-Gwan (author); Sharma, Aditi (author); Gondro, Cedric  (author)orcid 
Publication Date: 2014
DOI: 10.1016/j.meatsci.2013.11.026
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Abstract: The objective of this study was to evaluate the effects of seven single nucleotide polymorphisms (SNPs) in Calpain 1 and Calpastatin genes previously associated with meat tenderness attributes in other cattle breeds in Korean Hanwoo cattle. The Hanwoo resource population was used to study association of 7 SNPs with beef tenderness, flavor, juiciness, intramuscular fat and shear force. In this association study, CAST:c.182A > G (+ 0.14, P = 0.04) and CAST:c.1985G > C (- 0.12, P = 0.02) had significant effects on juiciness, but no effects on other traits. In contrast, CAPN1:c.1589G > A was associated with meat tenderness (P = 0.01) and juiciness (P = 0.04). The CAPN1:c.1589G > A (Val530Ile) SNP marker displayed significant effect on the meat tenderness score which is strongly supported by molecular modeling of the CAPN1:c.1589G > A (Val530Ile) variant that inhibits CAST protein from binding more strongly than the wild-type protein, which may explain its effect on meat tenderness.
Publication Type: Journal Article
Source of Publication: Meat Science, 96(4), p. 1501-1508
Publisher: Elsevier BV
Place of Publication: Amsterdam, The Netherlands
ISSN: 1873-4138
Field of Research (FOR): 070202 Animal Growth and Development
Socio-Economic Outcome Codes: 970106 Expanding Knowledge in the Biological Sciences
Peer Reviewed: Yes
HERDC Category Description: C1 Refereed Article in a Scholarly Journal
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