REVIEW: Methylglyoxal and Small Heat Shock Proteins

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M. V. Sudnitsyna and N. B. Gusev^*

Lomonosov Moscow State University, Faculty of Biology, 119991 Moscow, Russia; E-mail: NBGusev@mail.ru

^* To whom correspondence should be addressed.

Received March 22, 2017

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Methylglyoxal is a highly reactive dicarbonyl compound formed during glucose metabolism and able to modify phospholipids, nucleic acids, and proteins belonging to the so-called dicarbonyl proteome. Small heat shock proteins participating in protection of the cell against different unfavorable conditions can be modified by methylglyoxal. The probability of methylglyoxal modification is increased in the case of distortion of glucose metabolism (diabetes), in the case of utilization of glycolysis as the main source of energy (malignancy), and/or at low rate of modified protein turnover. We have analyzed data on modification of small heat shock protein HspB1 in different tumors and under distortion of carbohydrate metabolism. Data on the effect of methylglyoxal modification on stability, chaperone-like activity, and antiapoptotic activity of HspB1 were analyzed. We discuss data on methylglyoxal modifications of lens α-crystallins. The mutual dependence and mutual effects of methylglyoxal modification and other posttranslational modifications of lens crystallins are analyzed. We conclude that although there is no doubt that the small heat shock proteins undergo methylglyoxal modification, the physiological significance of this process remains enigmatic, and new experimental approaches should be developed for understanding how this type of modification affects functioning of small heat shock proteins in the cell.

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KEY WORDS: small heat shock proteins, oligomeric structure, chaperone-like activity, dicarbonyl proteome, methylglyoxal

DOI: 10.1134/S000629791707001X

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