AlphaB-crystallin selectively targets intermediate filament proteins during thermal stress.

摘要: PURPOSE. aB-Crystallin is a small heat shock protein (sHsp) expressed at high levels in the lens of eye, where its molecular chaperone functions may protect against cataract formation vivo. The purpose this study was to identify targets for sHsp aB-crystallin cell homogenates during conditions mild thermal stress. METHODS. authors report use fusion protein, maltose-binding (MBP-aB), immobilized on amylose resin as novel method isolating endogenous aB-crystallinbinding proteins from after RESULTS. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and western immunoblot analyses showed selective interactions between MBP-aB aA- aB-crystallins, lens-specific intermediate filament phakinin (CP49) filensin (CP115), vimentin 20-minute 45°C. No were observed with /3- or y-crystallins, cytoskeletal actin, a-tubulin, spectrin, although these present homogenates. In contrast, y-crystallin actin interacted 45°C only their purified states. results obtained confirmed by immunoprecipitation reactions which native bovine heat-shocked resulted coprecipitation filensin. CONCLUSIONS. selectively target filaments protection unfolding (Invest Ophthalmol Vis Sci. 1999;40: 951-958)