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 working with M CD eliminates the potential of ischemia and pharmacological preconditioning to protect the cardiac myocyte from injury [81]. This is also supported by the decreased capability of Cav1 KO mice to undergo pharmacological preconditioning [82]. Current investigations also showed that prosurvival signaling elements (e.g., ERK1/ 2, HO1, eNOS and p38MAPK ) translocate and/or interact with Verubecestat Protocol 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 significantly less exposed to death signaling elements and more abundant to prosurvival signaling components [83, 84]. While detail mechanism of action of caveolin will not be extremely clear, but evidence indicates that proteasomes play a very vital part inside the interaction amongst caveolin and signaling elements. Even so, all round observation indicates that caveolin plays a pivotal part in cardioprotection against ischemic injury (Fig. 1). CONCLUSION Caveolae and caveolins are undoubtedly regulating various elements of cardiovascular program. Clearly loss of caveolin1 has profound impact around the eNOS pathway, indicating the value of this interaction, whereas the loss of caveolin3 impacts NOS too as MAPK activation. Although detail mechanisms of actions are certainly not extremely clear, experimental evidences demonstrate the predominant role of caveolin in cardiac hypertrophy, atherosclerosis, ischemic injury and distinctive myocardial functions. Current investigations are disentangling the complex processes of caveolin regulated signaling systems inside the myocardium and building novel approaches, aimed at counteracting cardiomyocyte apoptosis in heart failure and/or cardiovascular ailments. 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 health and illness. Biol Cell 2007; 99: 12940. Wyse BD, Prior IA, Qian H, et al. Caveolin interacts together with the angiotensin II sort 1 receptor in the course of 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 wellness and disease. Physiol Rev 2004; 84: 134179. Insel PA, Patel HH. Do studies in caveolinknockouts teach us about physiology and pharmacology or instead, the techniques 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 web page (Cys156) controls its coupling to the cSrc tyrosine kinase: targeting of dually acylated molecules (GPIlinked, transmembrane, or cytoplasmic) to caveolae correctly 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,.
