[Nonenzymatic glycosylation of and oxidative damage to actin in vitro and in vivo].
A study was made the influence exerted by non-enzymatic glycosylation (glycation) and oxidative destruction on structural and functional parameters of actin (free NH2-groups, advanced glycation end product and bityrosine cross-linking content, DNase inhibition by G-actin and myosin Mg(2+)-ATPase activation by F-actin). The functional properties of actin were shown to change under high molecular weight product formation and oxidative destruction: the extent of DNAase I inhibition decreases (from 70 to 40%) and the extent of myosin Mg(2+)-ATPase decreases (by 40%). Carnosine prevents actin oligomer formation and oxidative destruction which favours preservation of the protein functional properties.
Kuleva
N V
NV
St. Petersburg State University.
Zalesova
Z S
ZS
D000199:Actins / Q000187:drug effects / Q000378:metabolism*; D000818:Animals; D017301:Ca(2+) Mg(2+)-ATPase / Q000378:metabolism; D017127:Glycation End Products, Advanced; D005985:Glyceraldehyde / Q000494:pharmacology; D006031:Glycosylation; D009132:Muscles / Q000187:drug effects / Q000378:metabolism; D018384:Oxidative Stress; D011817:Rabbits; D051381:Rats
D000199:Actins; D017127:Glycation End Products, Advanced; D005985:Glyceraldehyde; D017301:Ca(2+) Mg(2+)-ATPase