Purification of plasma membrane proteins for the proteomic analysis of hauman msenchymal stem cells
An efficient sample preparation method was developed for the analysis of plasma membrane proteins of stem cells using ultracentrifugation and aqueous two-phase extraction. The method developed was rapid (within 4 hr) and provided a relatively high purity (26-fold of cell lysate) with a high yield (2.6％). This separation process was proven to be suitable for proteomic analysis of plasma membranes on multipotent human mesenchymal stem cells (hMSC) derived from both human umbilical cord blood (hUCB) and bone marrow. In addition, hMSCs derived from human umbilical cord blood (hUCB) and bone marrow were differentiated into adipocytes and chondrocytes. Proteins which were differentially expressed by the differentiation of hMSC from bone marrow to adipocytes were analyzed. Thirty-two protein spots were shown to have different expression levels by 2-DE analysis. Among these, eight up-regulated proteins were identified by MALDI-TOF/MS, as the following: syntaxin binding protein 3, OSBP-related protein 3, phosphodiesterase, glycophorin, immunoglobulin-|ê chain variable region, peroxisome pro-liferative activated receptor gamma (PPAR-|? ), bA528A10.3.1 (novel protein similar to K1AA01616, isoform 1), and T cell receptor V-|? 4. Four proteins: syntaxin-3, OSBP-related protein 3, PPAR-|? And glycophorin were associated with adipogenesis.
Plasma membrane proteins Msenchymal stem cell Umbilical cord blood Adipocytes, Chondrocyte
Mi Ryung Kim Seung Ah Park Ji Soo Kim ChanWha Kim
School of Life Sciences and Biotechnology, Korea University, Seoul, Korea
国际会议
The 5th International Conference on Separation Science and Technology(第五届国际分离科学与技术会议)
北京
英文
2007-10-14（万方平台首次上网日期，不代表论文的发表时间）