Targeted Drug Delivery Systems of Fusion Proteins for the Treatment of Ischemic Heart Disease

초록

Heat shock proteins (Hsp) are essential proteins that act as molecular chaperones by assisting in the folding of cellular proteins for maintenance of proper functional conformation. They thus promote cell survival, particularly in response to a large variety of environmental stress signals which induce the expression of these proteins (1). They are also expressed during ischemic heart disease conditions as the result of hypoxia, reperfusion, and oxidative stress, and prevent apoptosis of myocytes after ischemia/reperfusion injury (2, 3). Many heat shock proteins such as Hsp60/65, Hsp70/72 and Hsp90, have been implicated to be associated with ischemic heart disease (4, 5). While Hsp27 has been shown to have a strong protective function against apoptotic events on myocardic cells (6), there are very few studies exploring whether Hsp27 has a beneficial role in myocardic infarctions. Heat shock protein 27 (Hsp27) is a member of the small Hsp family of proteins with molecular weight of approximately 27kDa (7) and is known to regulate apoptosis through by interacting with key components of the apoptotic signaling pathway, in particular, those involved in caspase activation and apoptosis (8). We are investigating whether Hsp27 can rescue cells from apoptosis in ischemic heart disease conditions.