title: [Effect of depside salt from salvia miltiorrhizae in repairing advanced glycation end products-induced late endothelial progenitor cell dysfunction and its molecular mechanism].
abstract: OBJECTIVE
  To investigate the effects of depside salt from salvia miltiorrhizae (DSSM) in repairing advanced glycation end products (AGE)-induced late endothelial progenitor cell (EPC) dysfunction, and its possible molecular mechanism.
  
  
  METHODS
  Mononuclear cells (MNCs) were separated using density gradient centrifugation from human umbilical cord blood, and cultured with EGM-2-MV culture fluid to late EPCs. Then the EPCs were divided into 5 groups: Group A incubated with 200 microg/mL AGE-modified bovine serum albumin (AGE-albumin) alone (A), Groups B, C and D with equal dosage of AGE-albumin plus DSSM at different dosages (0.1 microg/mL, 1 microg/mL, and 10 microg/mL), Group E with 200 microg/mL of unmodified-AGE. The late EPCs apoptosis was detected by Annexin V+/PI double-stain, angiogenic capacity was detected by ECMatrix-gel, mRNA expressions of the receptor for AGE (RAGE) and endothelial nitric oxide synthase (eNOS) were measured by reverse-transcriptase polymerase chain reaction (RT-PCR), and the protein expressions of RAGE, eNOS and protein kinase (Akt) were measured by Western blot.
  
  
  RESULTS
  Compared with Group E, in Group A, the Annexin V+/PI- ratio and expression of RAGE in EPCs increased, the angiogenic capacity, mRNA and protein expressions of eNOS, and protein expression of Akt decreased significantly. These abnormal changes in Groups C and D were significantly smaller than those in Group A (P < 0.05 or P < 0.01). And all the indices in Group D were adjacent to those in Group E, showing insignificant difference between the two groups (P > 0.05).
  
  
  CONCLUSIONS
  AGE could injure the function of EPCs, revealing increase of cell apoptosis and migration, deprivation of angiogenic capacity in vitro. DSSM could repair the EPCs dysfunction induced by AGE-albumin. Up-regulation of eNOS and Akt in these cells may be involved in the mechanism.
authors.affiliation: Affiliated Drum Tower Hospital, Medical School of Nanjing University, Nanjing.
authors.forename: Qin
authors.initials: Q
authors.lastname: Chen
authors.forename: Ming-Han
authors.initials: MH
authors.lastname: Huang
authors.forename: Shi-Sen
authors.initials: SS
authors.lastname: Jiang
mesh_terms: D000328:Adult; D017209:Apoptosis / Q000187:drug effects; D002465:Cell Movement / Q000187:drug effects; D002478:Cells, Cultured; D053630:Depsides / Q000302:isolation & purification / Q000494:pharmacology*; D004730:Endothelium, Vascular / Q000166:cytology* / Q000187:drug effects / Q000378:metabolism; D005260:Female; D017127:Glycation End Products, Advanced / Q000037:antagonists & inhibitors / Q000494:pharmacology; D006801:Humans; D052250:Nitric Oxide Synthase Type III / Q000378:metabolism; D051057:Proto-Oncogene Proteins c-akt / Q000378:metabolism; D000067759:Receptor for Advanced Glycation End Products; D011971:Receptors, Immunologic / Q000378:metabolism; D027561:Salvia miltiorrhiza / Q000737:chemistry*; D013234:Stem Cells / Q000187:drug effects / Q000378:metabolism / Q000502:physiology*; D055815:Young Adult
chemical_list: D053630:Depsides; D017127:Glycation End Products, Advanced; D000067759:Receptor for Advanced Glycation End Products; D011971:Receptors, Immunologic; C496314:NOS3 protein, human; D052250:Nitric Oxide Synthase Type III; D051057:Proto-Oncogene Proteins c-akt