Assessment of haplotype variation in bovine AMPD1 gene for association with growth and carcass traits in Qinchuan beef cattle

The AMPD1 gene plays an important role in the purine nucleotide cycle and energy metabolism in skeletal muscle. In the present study polymorphisms of the AMPD1 gene were detected by PCR-SSCP and DNA sequencing of 215 individuals of the Qinchuan beef cattle breed. DNA sequencing revealed two mutations by comparisons with the bovine genome sequence (acc. no.: NC_007301). Two single nucleotide polymorphisms (SNPs; g.19416T>C and g.19421A>G) were detected in intron 11 of the bovine AMPD1 gene. The sequencing of PCR products of animals providing different PCR-SSCP banding patterns showed that four kinds of haplotypes, named: A (T-A), B (T-G), C (C-A) and D (C-G); and the five diplotypes were segregating: AA (T-A/T-A), BC (T-G/C-A or C-G/T-A ), AC (T-A/C-A), CC (C-A/C-A) and CD (C-A/ C-G). A significant association of AMPD1 with carcass weight was shown. Animals with the new heterozygote diplotype BC (P<0.05, n=56) had greater carcass weight than those with the other diplotypes. The SNPs in AMPD1 may be used as a possible candidates for markerassisted selection in Qinchuan beef cattle breeding program.

[1]  Junya Li,et al.  Association analysis of thyroglobulin gene variants with carcass and meat quality traits in beef cattle , 2010, Journal of Applied Genetics.

[2]  Linjie Wang,et al.  Molecular characterization and expression patterns of AMP deaminase1 (AMPD1) in porcine skeletal muscle. , 2008, Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology.

[3]  Hong Chen,et al.  An AluI PCR-RFLP detecting a silent allele at the goat POU1F1 locus and its association with production traits , 2007 .

[4]  A. Komar,et al.  Silent SNPs: impact on gene function and phenotype. , 2007, Pharmacogenomics.

[5]  Hong Chen,et al.  Enhance the efficiency of single-strand conformation polymorphism analysis by short polyacrylamide gel and modified silver staining. , 2007, Analytical biochemistry.

[6]  Lippincott-Schwartz,et al.  Supporting Online Material Materials and Methods Som Text Figs. S1 to S8 Table S1 Movies S1 to S3 a " Silent " Polymorphism in the Mdr1 Gene Changes Substrate Specificity Corrected 30 November 2007; See Last Page , 2022 .

[7]  G. Moser,et al.  Linkage and QTL mapping for Sus scrofa chromosome 4 , 2003 .

[8]  G. Moser,et al.  Linkage and QTL mapping for Sus scrofa chromosome 2 , 2003 .

[9]  G. Moser,et al.  Linkage and QTL mapping for Sus scrofa chromosome 1 , 2003 .

[10]  H. Reichmann,et al.  A G468-T AMPD1 mutant allele contributes to the high incidence of myoadenylate deaminase deficiency in the Caucasian population , 2002, Neuromuscular Disorders.

[11]  R. Sabina,et al.  Towards an understanding of the functional significance of N-terminal domain divergence in human AMP deaminase isoforms. , 2000, Pharmacology & therapeutics.

[12]  H Geldermann,et al.  Combined analyses of data from quantitative trait loci mapping studies. Chromosome 4 effects on porcine growth and fatness. , 2000, Genetics.

[13]  G. Moser,et al.  The porcine adenosine monophosphate deaminase 1 (AMPD1) gene maps to chromosome 4. , 2000, Animal genetics.

[14]  R. Sabina,et al.  Cloning, sequence and characterization of the human AMPD2 gene: evidence for transcriptional regulation by two closely spaced promoters. , 1996, Biochimica et biophysica acta.

[15]  R. Sabina,et al.  Characterization of human AMP deaminase 2 (AMPD2) gene expression reveals alternative transcripts encoding variable N-terminal extensions of isoform L. , 1995, The Biochemical journal.

[16]  T. Morisaki,et al.  Identification of functional domains in AMPD1 by mutational analysis. , 1994, Biochemical and biophysical research communications.

[17]  J. Veerkamp,et al.  Immunolocalization of AMP-deaminase isozymes in human skeletal muscle and cultured muscle cells: concentration of isoform M at the neuromuscular junction. , 1994, The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society.

[18]  E. Holmes,et al.  Immunologic evidence for three isoforms of AMP deaminase (AMPD) in mature skeletal muscle. , 1993, Biochimica et biophysica acta.

[19]  T. Morisaki,et al.  Molecular cloning of AMP deaminase isoform L. Sequence and bacterial expression of human AMPD2 cDNA. , 1992, The Journal of biological chemistry.

[20]  R. Sabina,et al.  Cloning of human AMP deaminase isoform E cDNAs. Evidence for a third AMPD gene exhibiting alternatively spliced 5'-exons. , 1992, The Journal of biological chemistry.

[21]  A. C. Chinault,et al.  Deduced amino acid sequence of Escherichia coli adenosine deaminase reveals evolutionarily conserved amino acid residues: implications for catalytic function. , 1991, Biochemistry.

[22]  P. Clarke,et al.  A novel pathway for alternative splicing: identification of an RNA intermediate that generates an alternative 5' splice donor site not present in the primary transcript of AMPD1 , 1990, Molecular and cellular biology.

[23]  T. Morisaki,et al.  Adenylate deaminase. A multigene family in humans and rats. , 1990, The Journal of biological chemistry.

[24]  C. Morton,et al.  Characterization of the human and rat myoadenylate deaminase genes. , 1990, The Journal of biological chemistry.