Involvement of PTP-RQ in differentiation during adipogenesis of human mesenchymal stem cells

被引:32
|
作者
Jung, Hyeyun [1 ,2 ]
Kim, Won Kon [1 ]
Kim, Do Hyung [1 ]
Cho, Yee Sook [3 ]
Kim, Seung Jun [1 ]
Park, Sung Goo [1 ]
Park, Byoung Chul [1 ]
Lim, Heon Man [2 ]
Bae, Kwang-Hee [1 ]
Lee, Sang Chul [1 ]
机构
[1] KRIBB, Med Proteom Res Ctr, Taejon 305806, South Korea
[2] Chungnam Natl Univ, Dept Biol, Taejon 305764, South Korea
[3] KRIBB, Dev & Differentiat Res Ctr, Taejon 305806, South Korea
关键词
Adipocyte; Adipogenesis; Differentiation; Human mesenchymal stem cells; Protein tyrosine phosphatase RQ; PROTEIN-TYROSINE PHOSPHATASES; SUBSTRATE-SPECIFICITY; IN-VITRO; MODULATOR; PTEN;
D O I
10.1016/j.bbrc.2009.04.001
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Mesenchymal stem cells (MSCs) are self-renewable multipotent progenitor cells with the capacity to differentiate into several distinct mesenchymal lineages. While MSCs display significant potential in tissue engineering and therapeutic applications, the regulatory mechanisms underlying the differentiation of these cells are yet to be established. Phosphorylation is a post-translational modification that plays a significant role in diverse biological phenomena. In this study, to mine the protein tyrosine phosphatases (PTPs) involved in adipogenesis of human MSCs, differential expression of human PTPs was examined using RT-PCR analysis. Among the 107 human PTPs, PTP-RQ was dramatically downregulated during the early phase of adipogenesis. PFP-RQ is classified as a receptor-type III PTP with phosphatidylinositol phosphatase (PIPase) activity. Overexpression of PTP-RQ consistently led to reduced differentiation of MSCs into adipocytes via decreasing the phosphatidyl inositol phosphate level in cells, and consequently downregulating Akt/PKB phosphorylation. Our results collectively suggest that PFP-RQ is a useful target protein for regulating the differentiation of MSCs into adipocytes, and may be used to develop novel drugs for the treatment of obesity. (C) 2009 Elsevier Inc. All rights reserved.
引用
收藏
页码:252 / 257
页数:6
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