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Stress induced increase in protein O‐linked‐N‐acetylglucosamine (O‐GlcNAc) levels is CaMKII dependent
Author(s) -
Zou Luyun,
Zou Chenhang,
Chatham John C.
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.1127.6
Subject(s) - hek 293 cells , c2c12 , chemistry , heat shock protein , heat shock , microbiology and biotechnology , biophysics , endocrinology , biochemistry , in vitro , biology , receptor , gene , myogenesis
Acute cellular stress increases O‐linked‐N‐acetylglucosamine (O‐GlcNAc) modification of proteins; however, the mechanisms by which this occurs is not known. We have previously shown that in cardiomyocytes glucose deprivation (GD) is a potent stimulus for increasing cellular O‐GlcNAc levels and that this response was Ca2+ dependent. To determine whether Ca2+ contributed to increased O‐GlcNAcylation in response to other stress stimuli and in other cell types, C2C12 and HEK293 cells were subjected to either GD or heat shock in the presence or absence of KN93 a CaMKII inhibitor. Similar to cardiomyocytes both C2C12 and HEK293 cells exhibited a marked increased in O‐GlcNAc levels following 24hrs GD and in both cases this was significantly attenuated by treatment with KN93. Heat shock in HEK293 cells (42C for 1 hour) and C2C12 cells (45C for 1 hour) exhibited a clear time dependent increase in O‐GlcNAc following recovery at 37C, reaching a maximum at 30min and 3hrs in HEK293 and C2C12 cells respectively. Pretreatment with KN93 significantly attenuated the heat shock induced increase in O‐GlcNAc levels in both C2C12 and HEK293 cells. These data suggest that both GD and heat shock induced increase in O‐GlcNAcylation are mediated at least in part by Ca2+ induced activation of CaMKII; thereby providing new insights into the mechanisms underlying regulation of O‐GlcNAc cycling in cells subjected to acute stress.