RGD Reference Report - Ischemia-induced association of the stress protein alpha B-crystallin with I-band portion of cardiac titin. - Rat Genome Database
During ischemia the cardiac stress protein, alpha B-crystallin, was shown by immunoelectron microscopy to translocate to the N(2)-line area of myofibrillar I-bands of rat cardiomyocytes where alpha B-crystallin resisted extraction with 1 m NaSCN and 2 m urea as did titin. Actin became completely extracted under these conditions, indicating association of alpha B-crystallin with titin the only remaining non-actin cytoskeletal component of I-bands outside Z-disks. Titin, extracted from ischemic pig myocardium, was shown to copurify with alpha B-crystallin. Further evidence for binding of alpha B-crystallin to titin was obtained by dot-blot assays in which biotinylated alpha B-crystallin was demonstrated to bind to the titin-enriched fraction immobilized on nitrocellulose. Binding of alpha B-crystallin to titin during cardiac ischemia could serve to stabilize titin against denaturation and might provide an endogenous mechanism to delay ischemic damage of this important elastic component of myofibrils.