Up-regulation of O-GlcNAc transferase with glucose deprivation in HepG2 cells is mediated by decreased hexosamine pathway flux

Journal of Biological Chemistry

Volumn 284, Issue 6, 2009, Pages 3425-3432

  Taylor, Rodrick P ^a   Geisler, Taylor S ^a   Chambers, Jefferson H ^a   McClain, Donald A ^a,b  

^a UNIVERSITY OF UTAH SCHOOL OF MEDICINE   (United States)

^b VETERANS AFFAIRS MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACETAMIDO; DEGLYCOSYLATION; DOWN-REGULATION; ENERGY DEPLETION; GLUCOSAMINE; GLUCOSE DEPRIVATION; GLYCOGEN SYNTHASE ACTIVITIES; HEPG2 CELLS; N-ACETYLGLUCOSAMINE; NEGATIVE FEEDBACK; NUCLEOCYTOPLASMIC; O-LINKED; POST-TRANSLATIONAL MODIFICATIONS; PROTEIN LEVEL; PROTEIN MODIFICATIONS; SENSING MECHANISM; UP-REGULATION;

AMINES; CELL MEMBRANES; ENZYMES; FEEDBACK; LAWS AND LEGISLATION; PROTEINS; SUGAR (SUCROSE);

GLUCOSE;

ADENYLATE KINASE; GLUCOSAMINE; GLUCOSE; GLYCOGEN SYNTHASE; HEXOSAMINE; MESSENGER RNA; N ACETYLGLUCOSAMINE; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE; N ACETYLGLUCOSAMINYLTRANSFERASE; UDP N ACETYLGLUCOSAMINE PEPTIDE BETA N ACETYLGLUCOSAMINYLTRANSFERASE; UDP-N-ACETYLGLUCOSAMINE-PEPTIDE BETA-N-ACETYLGLUCOSAMINYLTRANSFERASE;

ACYLATION; ARTICLE; CELL LEVEL; CONTROLLED STUDY; DEPLETION; DOWN REGULATION; ENZYME MODIFICATION; GENE INDUCTION; HUMAN; HUMAN CELL; PRIORITY JOURNAL; PROTEIN GLYCOSYLATION; PROTEIN MODIFICATION; PROTEIN PHOSPHORYLATION; REGULATORY MECHANISM; SIGNAL TRANSDUCTION; UPREGULATION; BIOSYNTHESIS; CELL NUCLEUS; CYTOPLASM; DRUG EFFECT; ENZYME INDUCTION; ENZYMOLOGY; METABOLISM; PHOSPHORYLATION; PHYSIOLOGY; PROTEIN PROCESSING; TUMOR CELL LINE;

ACETYLGLUCOSAMINE; AMP-ACTIVATED PROTEIN KINASES; CELL LINE, TUMOR; CELL NUCLEUS; CYTOPLASM; ENZYME INDUCTION; GLUCOSE; GLYCOGEN SYNTHASE; HUMANS; N-ACETYLGLUCOSAMINYLTRANSFERASES; PHOSPHORYLATION; PROTEIN PROCESSING, POST-TRANSLATIONAL; RNA, MESSENGER;

EID: 63649085232     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M803198200     Document Type: Article

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