Oxidizing free radicals reduce the chaperone activity of lens a-crystallin and increase the susceptibility of lens proteins to serve as substrate for transglutaminase (TGase) activity, thereby leading to the protein crosslinking and cataractogenesis typical of aging and diabetes. To evaluate whether L-carnitine protects a-crystallin function in its ability to prevent aberrant protein associations and inhibits TGase-induced protein crosslinking, we measured the molecular chaperone activity of a-crystallin and isopeptide cross-links in rat lenses exposed in vitro to H2O2 in the presence and absence of L-carnitine and in control (untreated) lenses.
Carnitine protects the molecular chaperone activity of lens alpha-crystallin and decreases the post-translational protein modifications induced by oxidative stress
BARBARISI, Alfonso;MELONE, Mariarosa Anna Beatrice;
2001
Abstract
Oxidizing free radicals reduce the chaperone activity of lens a-crystallin and increase the susceptibility of lens proteins to serve as substrate for transglutaminase (TGase) activity, thereby leading to the protein crosslinking and cataractogenesis typical of aging and diabetes. To evaluate whether L-carnitine protects a-crystallin function in its ability to prevent aberrant protein associations and inhibits TGase-induced protein crosslinking, we measured the molecular chaperone activity of a-crystallin and isopeptide cross-links in rat lenses exposed in vitro to H2O2 in the presence and absence of L-carnitine and in control (untreated) lenses.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
