| Literature DB >> 26899869 |
Jin Ma1, Qiuyan Li1, Yan Li2, Xiao Wen2, Zhiyuan Li2, Zaihu Zhang3, Jiuming Zhang3, Zhengquan Yu1, Ning Li4.
Abstract
Human α-lactalbumin (HLA) has very high nutritional value and important physiological functions during the neonatal period. The peptides derived from HLA provide diverse health benefits including antimicrobial, antiviral, immune-modulating, and antihypertensive effects. Thus, it is worth investigating the effects on offspring development of increasing HLA in milk. In this study, we found that recombinant human α-lactalbumin (rHLA) exhibits efficient inhibition of dipeptidyl peptidase-IV (DPP-IV) activity in an in vitro simulated gastrointestinal digestion system. Using a BAC clone containing the complete HLA gene as a candidate vector, we generated two lines of transgenic cloned sows via somatic cell nuclear transfer that over-expressed rHLA. The average concentrations of rHLA in milk from the two lines of transgenic cloned sows were 2.24 ± 0.71 mg/ml and 2.67 ± 1.29 mg/ml. The feeding experiments revealed that rHLA represses dipeptidyl peptidase-IV (DPP-IV) activity in vivo. Furthermore, the piglets reared by rHLA transgenic cloned sows exhibit better performance in gain of body weight and intestine growth than the control piglets reared by non-transgenic sows. Therefore, these findings indicate that rHLA could serve as a natural precursor for a DPP-IV inhibitor, and the transgenic technology that produced the over-expression of rHLA could be a useful method for pig breeders to improve lactation performance.Entities:
Keywords: Dipeptidyl peptidase-IV inhibitory activity; Human α-lactalbumin; Piglet growth; Transgenic cloned pig
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Year: 2016 PMID: 26899869 DOI: 10.1016/j.gene.2016.02.024
Source DB: PubMed Journal: Gene ISSN: 0378-1119 Impact factor: 3.688