Dial ischemia and ischemia/reperfusion injury [79]. Ischemia/reperfusion injury activates p42/44 and p38MAPK, redistributes caveolin3 and downregulates expression of caveolin1 [80]. Disruption of caveolae using M CD eliminates the potential of ischemia and pharmacological preconditioning to defend the cardiac myocyte from injury [81]. This can be also supported by the decreased ability of Cav1 KO mice to undergo pharmacological preconditioning [82]. Current investigations also showed that prosurvival signaling components (e.g., ERK1/ 2, HO1, eNOS and p38MAPK ) translocate and/or interact with caveolin in ischemia/reperfusion heart and render the heart less abundance to prosurvival signal and induces myocardial injury. Similarly, in preconditioned heart death signaling components (e.g., p38MAPK , JNK and Src) translocates and/or interact with caveolin in preconditioned heart and rendering the heart much less exposed to death signaling elements and much more abundant to prosurvival signaling elements [83, 84]. Even though detail mechanism of action of caveolin isn’t quite clear, but proof indicates that proteasomes play an extremely essential function in the Aif Inhibitors targets interaction in between caveolin and signaling elements. On the other hand, general observation indicates that caveolin plays a pivotal role in cardioprotection against ischemic injury (Fig. 1). CONCLUSION Caveolae and caveolins are undoubtedly regulating various aspects of cardiovascular system. Clearly loss of caveolin1 has profound effect around the eNOS pathway, indicating the value of this interaction, whereas the loss of caveolin3 impacts NOS at the same time as MAPK activation. Though detail mechanisms of actions are usually not incredibly clear, experimental evidences demonstrate the predominant part of caveolin in cardiac hypertrophy, atherosclerosis, ischemic injury and different myocardial functions. Recent investigations are disentangling the complicated processes of caveolin regulated signaling systems within the myocardium and establishing novel approaches, aimed at counteracting cardiomyocyte apoptosis in heart failure and/or cardiovascular illnesses. REFERENCE[1] Pike LJ. Lipid rafts: bringing order to chaos. J Lipid Res 2003; 44: 6557.[4] [5] [6][7][8] [9][10][11] [12][13] [14] [15][16] [17][18][19] [20][21][22][23][24]Michel V, Bakovic M. Lipid rafts in well being and disease. Biol Cell 2007; 99: 12940. Wyse BD, Prior IA, Qian H, et al. Caveolin interacts together with the angiotensin II kind 1 receptor during Adrenergic Receptor Modulators medchemexpress exocytic transport but not at the plasma membrane. J Biol Chem 2003; 278: 2373846. Cohen AW, Hnasko R, Schubert W, Lisanti MP. Role of caveolae and caveolins in well being and disease. Physiol Rev 2004; 84: 134179. Insel PA, Patel HH. Do studies in caveolinknockouts teach us about physiology and pharmacology or alternatively, the approaches mice compensate for `lost proteins’ Br J Pharmacol 2007; 150: 25154. Lee H, Woodman SE, Engelman JA, et al. Palmitoylation of caveolin1 at a single site (Cys156) controls its coupling towards the cSrc tyrosine kinase: targeting of dually acylated molecules (GPIlinked, transmembrane, or cytoplasmic) to caveolae proficiently uncouples cSrc and caveolin1 (TYR14). J Biol Chem 2001; 276: 3515058. Parat MO, Fox PL. Palmitoylation of caveolin1 in endothelial cells is posttranslational but irreversible. J Biol Chem 2001; 276: 1577682. GarciaCardena G, Fan R, Stern DF, Liu J, Sessa WC. Endothelial nitric oxide synthase is regulated by tyrosine phosphorylation and interacts with caveolin1. J Biol Chem 1996; 271: 2723740. Venema VJ,.