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Altered neddylation in the heart of a mouse model for cardiomyopathy
Author(s) -
Suzuki Osamu,
Koura Minako,
Noguchi Yoko,
Uchio-Yamada Kozue,
Matsuda Junichiro
Publication year - 2012
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.26.1_supplement.1036.3
Subject(s) - neddylation , cardiomyopathy , dilated cardiomyopathy , genetically modified mouse , medicine , glycosylation , heart failure , transgene , strain (injury) , endocrinology , western blot , nedd8 , blot , diabetic cardiomyopathy , biology , microbiology and biotechnology , chemistry , biochemistry , ubiquitin , ubiquitin ligase , gene
We reported that a strain (4C30 strain) of mice with sialyltransferase (ST3GalII) transgenes would be a new mouse model for adult‐onset dilated cardiomyopathy (Proc Jpn Acad Ser B Phys Biol Sci. 2011; 87(8):550–562). Overexpression of ST3GalII perturbed protein glycosylation in 4C30 hearts, suggesting alteration of folding, translocation, and degradation of various proteins in 4C30 hearts. To study a possible involvement of protein degradation mechanisms in the cardiomyopathy, we compared neddylation statuses of heart proteins in our cardiomyopathic 4C30 mice with those in normal controls (C57BL/6NCr). Quantitative Western blots (QWB) for NEDD8 with GAPDH as a loading control revealed that two bands (100 and 105 kDa), but not four additional bands (90, 70, 60, or 40 KDa), were significantly denser in 4C30 hearts than in control hearts (p<0.05). QWB for culins with GAPDH indicated that culin‐2, but not culin‐1 or ‐3, was significantly more abundant (p<0.05). These results suggest that the protein degradation is altered in cardiomyopathic hearts.