Porcine phosphotyrosine interaction domain containing 1 modulates 3T3-L1 preadipocyte proliferation and differentiation

• Published in: Biológia Vol. 68; no. 5; pp. 1010 - 1014
• Main Authors: Chen, Xiaoling, Huang, Zhiqing, Wang, Huan, Jia, Gang, Liu, Guangmang, Zhao, Hua, Nie, Hao
• Format: Journal Article
• Language: English
• Published: Vienna Springer-Verlag 01.10.2013; Springer Vienna; Versita
• Subjects: 3T3-L1 preadipocyte; amino acids; binding proteins; Biomedical and Life Sciences; Cell Biology; complementary DNA; differentiation; droplets; gene expression; genes; insulin resistance; Life Sciences; lipoprotein lipase; messenger RNA; Microbiology; molecular weight; nitric oxide synthase; open reading frames; Plant Sciences; porcine PID1; proliferation; Section Cellular and Molecular Biology; swine; Zoology; porcine PID1; 3T3-L1 preadipocyte; differentiation; proliferation
• ISSN: 0006-3088; 1336-9563; 1336-9563
• DOI: 10.2478/s11756-013-0240-0

The phosphotyrosine interaction domain containing 1 (PID1) gene was firstly isolated from obese subjects and involved in obesity-associated insulin resistance. In the present study, Duroc×Landrace×Yorkshire (DLY) pig PID1 cDNA was cloned. The entire open reading frame of the cloned porcine PID1 is 654 bp. The predicted protein is composed of 217 amino acids residues with a molecular mass of 24,774 Da. Over-expression of porcine PID1 significantly accelerated the proliferation of 3T3-L1 preadipocyte, but inhibited preadipocyte differentiation by decreasing the numerous fat droplets appeared and down-regulating the mRNA expression levels of peroxisome proliferators-activated receptor-γ, CCAAT/enhancer binding protein α, fat acid synthase and lipoprotein lipase. Together, these results suggest that porcine PID1 plays a role in regulating adipose development.