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Elevated O ‐GlcNAcylation of ATP synthase β subunits in cardiomyopathic hearts in Syrian hamsters
Author(s) -
Suzuki Osamu,
Koura Minako,
Noguchi Yoko,
UchioYamada Kozue,
Matsuda Junichiro
Publication year - 2011
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.25.1_supplement.1000.9
Subject(s) - atp synthase , threonine , western blot , monoclonal antibody , protein subunit , serine , biochemistry , enzyme , cardiomyopathy , atpase , biology , chemistry , microbiology and biotechnology , antibody , medicine , heart failure , gene , immunology
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.