Open AccessAn insulin response element in the glyceraldehyde-3-phosphate dehydrogenase gene binds a nuclear protein induced by insulin in cultured cells and by nutritional manipulations in vivo.
Author(s) -
Nargis Nasrin,
Louis Ercolani,
Maria Denaro,
Xiangfu Kong,
Inwha Kang,
Maria C. Alexander
Publication year - 1990
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.87.14.5273
Subject(s) - glyceraldehyde 3 phosphate dehydrogenase , electrophoretic mobility shift assay , microbiology and biotechnology , biology , nad+ kinase , dehydrogenase , biochemistry , glyceraldehyde , insulin , phosphorylation , gene , nuclear protein , gene expression , transcription factor , enzyme , endocrinology
Two independent cis-acting insulin response elements (IREs) in the gene encoding glyceraldehyde-3-phosphate dehydrogenase [D-glyceraldehyde-3-phosphate: NAD+ oxidoreductase (phosphorylating), EC 1.2.1.12], designated IRE-A and IRE-B, are sufficient to direct insulin-inducible gene expression. Using the electrophoretic mobility shift assay, a 4-fold increase in the amount of IRE-A DNA bound to nuclear proteins was detected when extracts isolated from insulin-stimulated differentiated 3T3-L1 cells or from the liver of rats refed a high-carbohydrate/low-fat diet after a 72-hr fast were compared to control nuclear extracts. The points of contact between protein and IRE-A DNA may represent a sequence recognized by at least one class of insulin-sensitive transcription factor(s).