Heat shock proteins (HSP) are a highly conserved family of proteins that are expressed at low level under normal physiological conditions but dramatically increased in response to different cellular online casino stresses. HSPs function primarily as molecular chaperones participating in different intracellular processes: proteins folding, prevention of protein aggregation, transporting of newly synthesized polypeptides to organelles, degradation of miss folding proteins, apoptosis regulation, etc. HSP hyper expression is a substantial mechanism of cytoprotection. Hsp60 one of representatives of HSP-family proteins, that participate in assembling and transporting of mitochondrial proteins and prevention of their aggregation. The aim of investigation was to study the peculiarities of Hsp60 expression and intracellular localization in the heart at dilated cardiomyopathy. In normal cardiomyocytes 70–80% of Hsp60 is located in mitochondria and 20–30% in cytoplasm. In our study we used GroEL – prokaryotic homology of Hsp60 (sequence homology > 50%). Hsp60 expression was evaluated by Western-blot analysis in pathomorphologic specimens of three DCM-affected human myocardia and samples of left ventricular myocardium of three practically healthy men who died from casual trauma as a control. The expression Hsp60 at mRNA level was determined by 3T-PCR. Anti-Hsp60 autoantibodies (autoAB) level was determined by ELISA method in sera of 24 DCM patients and 38 healthy donors as a control. We revealed no
differences in anti-Hsp60 autoAB”s level (both IgG and IgM) in DCM patients” and healthy donors sera. The results show the increased expression of Hsp60 in human DCM myocardium total lysates (more than twice –
2.36) compared to normal. It was also revealed the Hsp60 intracellular re-distribution at DCM – augmentation in mitochondrial (for 66%) and decrease in cytoplasmic fraction (for 59%) compared to normal hearts.