4.6 Article

Genetic Variation in FABP4 and Evaluation of Its Effects on Beef Cattle Fat Content

期刊

ANIMAL BIOTECHNOLOGY
卷 28, 期 3, 页码 211-219

出版社

TAYLOR & FRANCIS INC
DOI: 10.1080/10495398.2016.1262868

关键词

ALBP; beef; fatty acid; meat quality; SNPs

资金

  1. Agencia Nacional de Promocion Cientifica y Tecnologica (ANPCyT) [PICT 08-04156, PICTR2002-0017]
  2. Consejo Nacional de Investigaciones Cientificas y Tecnicas (CONICET) [PIP2010-11220090100379]
  3. Instituto Nacional de Tecnologia Agropecuaria (INTA) [PNPA-1126033, PNCAR-334]
  4. Universidad Nacional de Mar del Plata (UNMdP) [AGR456/14, AGR393/12, AGR330/10, AGR270/08, AGR202/05, AGR137/01]
  5. Universidad Nacional de La Plata (UNLP) [ID V206/12, JI 9861/3/11]

向作者/读者索取更多资源

FABP4 is a protein primarily expressed in adipocytes and macrophages that plays a key role in fatty acid trafficking and lipid hydrolysis. FABP4 gene polymorphisms have been associated with meat quality traits in cattle, mostly in Asian breeds under feedlot conditions. The objectives of this work were to characterize FABP4 genetic variation in several worldwide cattle breeds and evaluate possible genotype effects on fat content in a pasture-fed crossbred (Angus-Hereford-Limousin) population. We re-sequenced 43 unrelated animals from nine cattle breeds (Angus, Brahman, Creole, Hereford, Holstein, Limousin, Nelore, Shorthorn, and Wagyu) and obtained 22 single nucleotide polymorphisms (SNPs) over 3,164bp, including four novel polymorphisms. Haplotypes and linkage disequilibrium analyses showed a high variability. Five SNPs were selected to perform validation and association studies in our crossbred population. Four SNPs showed well-balanced allele frequencies (minor frequency>0.159), and three showed no significant deviations from Hardy-Weinberg proportions. SNPs showed significant effects on backfat thickness and fatty acid composition (P<0.05). The protein structure of one of the missense SNPs was analyzed to elucidate its possible effect on fat content in our studied population. Our results revealed a possible blockage of the fatty acid binding site by the missense mutation.

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