Proteomic profiling of human placenta-derived mesenchymal stem cells upon transforming LIM mineralization protein-1 stimulation

被引:1
作者
Zhu, Zhen [1 ]
Liu, Zhihui [1 ]
Liu, Jingyue [2 ]
Bi, Ming [1 ]
Yang, Taoyuan [1 ]
Wang, Jingyun [1 ]
机构
[1] Jilin Univ, Stomatol Hosp, Changchun 130021, Peoples R China
[2] Stomatol Hosp Zhenjiang, Zhenjiang 212002, Peoples R China
关键词
Proteomics; LMP-1; hPDMSCs; Mass spectrometry; IN-VITRO DIFFERENTIATION; GENE-EXPRESSION; OSTEOBLAST DIFFERENTIATION; MULTIPOTENT CELLS; NUCLEAR ANTIGEN; MOUSE PLACENTA; BONE; LMP-1; IDENTIFICATION; IDENTITY;
D O I
10.1007/s10616-013-9684-x
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
Human placenta-derived mesenchymal stem cells (hPDMSCs) can differentiate into different types of cells and thus have tremendous potential for cell therapy and tissue engineering. LIM mineralization protein-1 (LMP-1) plays an important role in osteoblast differentiation, maturation and bone formation. To determine a global effect of LMP-1 on hPDMSCs, we designed a study using a proteomic approach combined with adenovirus-mediated gene transfer of LMP-1 to identify LMP-1-induced changes in hPDMSCs on proteome level. We have generated proteome maps of undifferentiated hPDMSCs and LMP-1 induced hPDMSCs. Two dimensional gel electrophoresis revealed 22 spots with at least 2.0-fold changes in expression and 15 differently expressed proteins were successfully identified by MALDI-TOF-MS. The proteins regulated by LMP-1 included cytoskeletal proteins, cadmium-binding proteins, and metabolic proteins, etc. The expression of some identified proteins was confirmed by further Western blot analyses. Our results will play an important role in better elucidating the underlying molecular mechanism in LMP-1 included hPDMSCs differentiation into osteoblasts.
引用
收藏
页码:285 / 297
页数:13
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