Open AccessTHIS ARTICLE HAS BEEN RETRACTED: Differential proteomic profiling to study the mechanism of cardiac pharmacological preconditioning by resveratrol
Author(s) -
Bezstarosti Karel,
Das Samarjit,
Lamers Jos. M. J.,
Das Dipak K.
Publication year - 2006
Publication title -
journal of cellular and molecular medicine
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.44
H-Index - 130
eISSN - 1582-4934
pISSN - 1582-1838
DOI - 10.1111/j.1582-4934.2006.tb00533.x
Subject(s) - resveratrol , hsp27 , proteome , cardioprotection , chemistry , proteomics , biochemistry , microbiology and biotechnology , heat shock protein , ischemia , biology , pharmacology , hsp70 , medicine , gene
Recent studies demonstrated that resveratrol, a grape‐derived polyphenolic phytoalexin, provides pharmacological preconditioning of the heart through a NO‐dependent mechanism. To further explore the molecular mechanisms involved in resveratrol‐mediated cardioprotection, we monitored the effects of resveratrol treatment after ischemia‐reperfusion on the protein profile by implementation of proteomic analysis. Two groups of rats were studied; one group of animals was fed resveratrol for 7 days, while the other group was given vehicle only. The rats were sacrificed for the isolated working heart preparation and for isolation of cytoplasmic fraction from left ventricle homogenates to carry out the proteomic as well as immunoblot at baseline and at the end of 30 min ischemia/2‐h perfusion. The results demonstrate significant cardiopro‐tection with resveratrol evidenced by improved ventricular recovery and reduced infarct size and cardiomyocyte apopto‐sis. The left ventricular cytoplasmic fractions were separated by two‐dimensional electrophoresis (2‐DE). Differentially regulated proteins were detected with quantitative computer analysis of the Coomassie blue stained 2‐DE images and identified by MALDI‐TOF (MS) and nanoLC‐ESI‐Q‐TOF mass spectrometry (MS/MS). Five redox‐regulated and precondi‐tioning‐related proteins were identified that were all upregulated by resveratrol: MAPKK, two different aB‐crystallin species, HSP 27 and PE binding protein. Another HSP27 species and aldose reductase were downregulated and peroxire‐doxin‐2 remained constant. The results of the immunoblot analysis of phosphorylated MAPKK, ‐HSP27 and ‐aB‐crys‐tallin and PE binding protein were consistent with the proteomic findings, but not with peroxiredoxin‐2. The proteomic analysis showed also downregulation of some proteins in the mitochondrial respiratory chain and matrix and the myofila‐ment regulating protein MLC kinase‐2. The results of the present study demonstrate that proteomic profiling enables the identification of resveratrol induced preconditioning‐associated proteins which reflects not only changes in their expression level but also isoforms, post‐translational modifications and regulating binding or activating partner proteins.