Abstract
Insulin-like growth factor binding protein-4 (IGFBP-4) is a member of the IGF super family, and regulates the action of IGFs. The polymorphism of porcine IGFBP-4 gene in 17 pig breeds (total n = 570) was detected by PCR-SSCP, and alleles A and B were detected. In these pig breeds, it was found that exotic pig breeds carried high frequencies of allele A, while Chinese native pig breeds carried high frequencies of allele B. The role of porcine IGFBP-4 was investigated in 172 F2 offspring of a Lantang×Lantang population. Forty eight growth traits were recorded for analyzing the association between IGFBP-4 gene polymorphism and quantitative performance traits. In this resource family, pigs with AA genotype had higher fore-body weight, bone weight of mid-body, bone weight of rear-body, fore-leg weight and rear-leg weight than those pigs with BB genotype (p<0.05); while pigs which carried BB genotype had higher back-fat thickness at C point and lard weight than those pigs with AA genotype (p<0.05); pigs with AA genotype had higher body weight than those with BB genotype; for meat quality traits, pigs with AA genotype had higher meat color than those of BB genotype (p<0.01), and pigs with BB genotype had higher marbling than those of AA and AB genotypes (p<0.01 and p<0.05, respectively).Based on these results, it is necessary to do more studies on IGFBP-4 before using the IGFBP-4 locus for the application of
Highlights
The insulin-like growth factor (IGF) system includes two ligands, IGF1 and IGF2; a membrane-spanning, tyrosine kinase receptor that transduces both ligands known as the IGF1 receptor (Le Roith et al, 2001); and a family of high-affinity IGF binding proteins (IGFBPs 1-6)
As a member of IGFBPs, Insulin-like growth factor binding protein-4 (IGFBP-4) mostly inhibits the activity of IGF-1
While the study of porcine IGFBP-4 gene is a blank, only we previously mapped the gene on SSC12 q21-24 (Wenjun et al, 2005)
Summary
The insulin-like growth factor (IGF) system includes two ligands, IGF1 and IGF2; a membrane-spanning, tyrosine kinase receptor that transduces both ligands known as the IGF1 receptor (Le Roith et al, 2001); and a family of high-affinity IGF binding proteins (IGFBPs 1-6). As one of the members of the IGFs superfamily, IGFBP-4, a nonglycosylated protein of 25 kDa and 32-36 kDa, was first isolated from medium conditioned by human osteosarcoma TE-89 cells (Mohan et al, 1989) and from adult rat serum (Shimonaka et al, 1989). IGFBP-4’s function is unique in that it inhibits IGF actions in all cell systems studied in vitro far (Lawrence et al, 1999). This has been shown to occur via high-affinity binding to both IGF-I and IGF-II, preventing interaction of either IGF with its receptor (Kelly et al, 1996).
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