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

Meat Sci. 2014 Apr;96(4):1501-8. doi: 10.1016/j.meatsci.2013.11.026. Epub 2013 Dec 31.

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.

Keywords: CAPN1; CAST; Hanwoo; Intramuscular fat; Shear force; Tenderness.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Breeding
  • Calcium-Binding Proteins / genetics*
  • Calpain / genetics*
  • Cattle
  • Genotype*
  • Humans
  • Meat / analysis*
  • Models, Molecular
  • Mutation*
  • Phenotype*
  • Polymorphism, Single Nucleotide*
  • Stress, Mechanical
  • Taste
  • Water

Substances

  • Calcium-Binding Proteins
  • Water
  • calpastatin
  • Calpain
  • mu-calpain