AMP-activated Protein Kinase (AMPK) negatively regulates Nox4-dependent activation of p53 and epithelial cell apoptosis in diabetes

Journal of Biological Chemistry

Volumn 285, Issue 48, 2010, Pages 37503-37512

  Eid, Assaad A ^a   Ford, Bridget M ^a   Block, Karen ^a,b   Kasinath, Balakuntalam S ^a,b   Gorin, Yves ^a   Ghosh Choudhury, Goutam ^a,b   Barnes, Jeffrey L ^a,b   Abboud, Hanna E ^a,b  

^a Mays Cancer Center at UT Health San Antonio   (United States)

^b SOUTH TEXAS VETERANS HEALTH CARE SYSTEM   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMP-ACTIVATED PROTEIN KINASE; APOPTOSIS; CARBOXAMIDES; EPITHELIAL CELLS; GLOMERULAR EPITHELIAL CELLS; IN-CELL; IN-VIVO; KIDNEY DISEASE; NADPH OXIDASE; NOVEL FUNCTIONS; PODOCYTES; REACTIVE OXYGEN SPECIES; RISK FACTORS; TUMOR SUPPRESSOR PROTEINS; TYPE 1 DIABETES;

ENZYME ACTIVITY; GLUCOSE; GLUCOSE OXIDASE; OXYGEN; PHOSPHORYLATION; PROTEINS;

CELL DEATH;

5 AMINO 4 IMIDAZOLECARBOXAMIDE RIBOSIDE; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE; PROTEIN KINASE LKB1; PROTEIN P53; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE 4;

ALBUMINURIA; ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; APOPTOSIS; ARTICLE; CONTROLLED STUDY; DRUG MECHANISM; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ASSAY; ENZYME INDUCTION; ENZYME REGULATION; EPITHELIUM CELL; GENETIC TRANSFECTION; GLOMERULUS BASEMENT MEMBRANE; IN VIVO STUDY; INCUBATION TIME; INSULIN DEPENDENT DIABETES MELLITUS; KIDNEY HYPERTROPHY; MOUSE; NONHUMAN; NUCLEOTIDE SEQUENCE; PODOCYTE; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PHOSPHORYLATION; REGULATORY MECHANISM;

AMP-ACTIVATED PROTEIN KINASES; ANIMALS; APOPTOSIS; DIABETES MELLITUS; DISEASE MODELS, ANIMAL; DOWN-REGULATION; FEMALE; GENE EXPRESSION REGULATION; GLUCOSE; HUMANS; MALE; MICE; NADPH OXIDASE; PHOSPHORYLATION; PODOCYTES; TUMOR SUPPRESSOR PROTEIN P53;

MUS;

EID: 78549248891     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.136796     Document Type: Article

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