4.7 Article

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 in the calpastatin/μ-calpain complex

Journal

MEAT SCIENCE
Volume 96, Issue 4, Pages 1501-1508

Publisher

ELSEVIER SCI LTD
DOI: 10.1016/j.meatsci.2013.11.026

Keywords

CAST; CAPN1; Tenderness; Shear force; Intramuscular fat; Hanwoo

Funding

  1. AGENDA project [PJ907008062012]
  2. Molecular Breeding Program of Next Generation BIOGREEN 21 project in the National Institute of Animal Science, Rural Development Administration (RDA) [PJ0081882012]

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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. (C) 2013 Published by Elsevier Ltd.

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