Objective To explore the mechanism of icariin mediating migration of mesenchymal stem cells (MSC) in rat bone marrow. Methods MSC proliferation was detected by CCK-8 test. Cell apoptosis was examined with Hoechst33342 staining after the establishment of cellular oxygen and glucose deprivation model. The protein expressions of CXCR4, the receptor of SDF-1, in the surface of MSC after stimulated by icariin were detected through Western blot. The migration of MSC was observed by Transwell chemotaxis assay. Results 0.01μmol/L, 0.1μmol/L and 1μmol/L of icariin could significantly promote the proliferation of MSC, while 10μmol/L of icariin inhibited the proliferation of MSC. After treatment of oxygen and glucose deprivation in vitro, 0.1μmol/L and 1μmol/L of icariin could inhibit the apoptosis of MSC. Icariin could not only improve the expression of CXCR4 in MSC, but also increase the number of transmembrane migrated MSC. After the addition of CXCR4 antagonist AMD3100, there was no significant difference in the number of cell migration among the different groups. Conclusion Icariin with appropriate concentration can promote the proliferation, survival and migration of MSC. SDF-1/CXCR4 signaling pathway is involved in the regulation of MSC migration by icariin.

AIM: To analyze and identify the phosphoproteins associated with diazoxide preconditioning. METHODS: Proteomics technique was used to investigate the changes of phosphoprotein after diazoxide preconditioning. Adult rat ventricular myocytes were pretreated in the presence and absence of 200 ?mol/L diazoxide for 10 min. Phosphoproteins prepared and enriched respectively from control and diazoxide pretreated groups were then separated by two-dimensional (2D) gel electrophoresis and stained with sliver staining kit. Phosphoproteins of interest were further identified by mass spectrometry. RESULTS: Associated with diazoxide preconditioning, the proteins of chaperonin containing TCP-1 and hypothetical protein XP_346548 were phosphorylated significantly. The proteins of 94 kD glucose-regulated protein, calpactin I heavy chain and ferritin were dephosphorylated markedly (P