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

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
Publication Date
2014
Author(s)
Lee, Seung-Hwan
Kim, Seung-Chang
Yang, Boh-Suk
Hong, Seong-Koo
Chai, Han-Ha
Cho, Soo-Hyun
Kim, Hyeong-Cheol
Lim, Dajeong
Choi, Bong-Hwan
Dang, Chang-Gwan
Sharma, Aditi
Gondro, Cedric
( author )
OrcID: https://orcid.org/0000-0003-0666-656X
Email: cgondro2@une.edu.au
UNE Id une-id:cgondro2
Type of document
Journal Article
Language
en
Entity Type
Publication
Publisher
Elsevier BV
Place of publication
Netherlands
DOI
10.1016/j.meatsci.2013.11.026
UNE publication id
une:15505
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.
Link
Citation
Meat Science, 96(4), p. 1501-1508
ISSN
1873-4138
0309-1740
Start page
1501
End page
1508

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