Change in the Functional Properties of Actin by Its Glycation in vitro

N. V. Kuleva^1,2 and Z. S. Kovalenko¹

¹Department of Biochemistry, School of Biology and Soil Sciences, St. Petersburg State University, Universitetskaya Naberezhnaya 7/9, Vasil'evskii Ostrov, St. Petersburg, 199034 Russia; fax: (812) 213-2454; E-mail: vm@vm1616.spb.edu

²To whom correspondence should be addressed.

Submitted May 25, 1997; revision submitted June 19, 1997.

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The influence of glycation (non-enzymatic glycosylation) on structural and functional properties of actin of rabbit skeletal muscle and the effects of the natural anti-glycating dipeptide carnosine were studied. Glucose (0.5 M), fructose (0.5 M), and glyceraldehyde (0.05 M) were used as glycating agents. Marked changes in the structural and functional properties were observed in the presence of glyceraldehyde when high-molecular-weight components appear. This was followed by a decrease in the ability of actin to activate myosin ATPase, to polymerize, and to inhibit DNase I. In the presence of 0.05 M carnosine, the quantity of high-molecular-weight products decreased and myosin ATPase activation was retained. Since muscle tissue contains millimolar quantities of carnosine, glycation of actin associated with changes in its properties is evidently more likely to occur in non-muscle cells.

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KEY WORDS: glycation, monosaccharide, actin, advanced glycosylation end products, carnosine.

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