Alpha-crystallin-like molecular chaperone against the thermal denaturation of lens aldose reductase: the effect of divalent metal ions.

A chaperone-like activity of bovine lens alpha-crystallin against the thermal-induced aggregation of bovine lens aldose reductase is reported. While the precipitation of aldose reductase at 55 degrees C is prevented by alpha-crystallin present at a ratio of aldose reductase: alpha-crystallin as low as 1:0.5 (w:w), the heat-induced inactivation of the enzyme occurs regardless of the presence of alpha-crystallin. This would suggest that, irrespective of the functional integrity of the target protein, alpha-crystallin interferes only with aggregation phenomena, having the potential to preserve the lens transparency. Calcium and magnesium ions at mM levels affect the antiaggregation action exerted by alpha-crystallin either interfering on the formation or reducing the stability of the aldose reductase: alpha-crystallin complex.