Abstract
In recent years, the posttranslational modification of serine and threonine residues of heart proteins by O‐linked attachment of the monosaccharide β‐N‐acetylglucosamine (O‐GlcNAc) has received a lot of attention as a key regulator in the cardiovascular function. To study the possible involvement of the O‐GlcNAcylation in the cardiomyopathy, we examined the O‐GlcNAcylation status of ventricular proteins from both normal (J2N‐n strain) and cardiomyopathic (J2N‐k strain) Syrian hamsters. Soluble fractions of heart proteins were extracted from left ventricles of both strains using a ReadyPrep sequential extraction kit (Bio‐Rad). Western blot analysis of the soluble fractions with a mouse monoclonal antibody against O‐GlcNAc (clone CTD110.6) indicated one J2N‐k specific band (~52 kDa). After isolation by monoclonal antibody columns and SDS‐PAGE, the band was suggested to be an ATP synthase β subunit (ATP5B) by mass spectrometry. These results suggest that the energy production machinery is modulated by O‐GlcNAcylation in the cardiomyopathy. This work was supported by a grant from the Ministry of Health, Labor, and Welfare of Japan.
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