Protective effects of carnosine against protein modification mediated by malondialdehyde and hypochlorite.
Malondialdehyde (MDA) and hypochlorite anions are deleterious products of oxygen free-radical metabolism. The effects of carnosine, a naturally occurring dipeptide (beta-alanyl-L-histidine), on protein modification mediated by MDA and hypochlorite have been studied. MDA and hypochlorite induced formation of carbonyl groups and high molecular weight and cross-linked forms of crystallin, ovalbumin and bovine serum albumin. The presence of carnosine effectively inhibited these modifications in a concentration-dependent manner. It is proposed that relatively non-toxic carnosine and related peptides might be explored as potential therapeutic agents for pathologies that involve protein modification mediated by MDA or hypochlorite.
Hipkiss
A R
AR
Molecular Biology and Biophysics Group, King's College London, UK.
Worthington
V C
VC
Himsworth
D T
DT
Herwig
W
W
D000818:Animals; D002336:Carnosine / Q000494:pharmacology*; D002417:Cattle; D003432:Cross-Linking Reagents; D003459:Crystallins / Q000737:chemistry / Q000187:drug effects; D006997:Hypochlorous Acid / Q000037:antagonists & inhibitors* / Q000633:toxicity*; D066298:In Vitro Techniques; D008315:Malondialdehyde / Q000037:antagonists & inhibitors* / Q000633:toxicity*; D008970:Molecular Weight; D010047:Ovalbumin / Q000737:chemistry / Q000187:drug effects; D011506:Proteins / Q000737:chemistry* / Q000187:drug effects*; D012710:Serum Albumin, Bovine / Q000737:chemistry / Q000187:drug effects
D003432:Cross-Linking Reagents; D003459:Crystallins; D011506:Proteins; D012710:Serum Albumin, Bovine; D008315:Malondialdehyde; D006997:Hypochlorous Acid; D002336:Carnosine; D010047:Ovalbumin