- ►diabetesjournals.org LR James, D Tang, A Ingram, H Ly, K Thai, L Cai, JW … - Diabetes, 2002 - Am Diabetes Assoc The hexosamine pathway may mediate some of the toxic effects of glucose. We hypothesized
that flux through this pathway might regulate the activity of nuclear factor κB (NF-κB)-dependent
genes in mesangial cells (MCs). In MCs, RT-PCR revealed that high glucose (30 mmol/l) ... Cited by 51 - Related articles - BL Direct - All 5 versions
- ►physiology.org MG Buse, KA Robinson, BA Marshall, RC … - American Journal of …, 2002 - Am Physiological Soc O-linked glycosylation on Ser/Thr with single N-acetylglucosamine (O-GlcNAcylation) is a reversible
modification of many cytosolic/nuclear proteins, regulated in part by UDP-GlcNAc levels. Transgenic
(T) mice that overexpress GLUT1 in muscle show increased basal muscle glucose ... Cited by 39 - Related articles - BL Direct - All 3 versions
DJ Burt, G Gruden, SM Thomas, P Tutt, C Dell'Anna, … - Diabetologia, 2003 - Springer Aims/hypothesis. The hexosamine pathway has been implicated in the induction of TGFβ1 expression
and in the pathophysiology of diabetic glomerulopathy. Glucose-induced TGFβ1 expression
is mediated by p38 mitogen-activated-protein-kinase (p38-MAPK) and this kinase is ... Cited by 27 - Related articles - BL Direct - All 3 versions
L Wells, Y Gao, JA Mahoney, K Vosseller, C Chen, … - Journal of Biological …, 2002 - ASBMB Multiple nucleocytoplasmic proteins, including transcription factors, cytoskeletal proteins,
oncogenes, and kinases, are post-translationally modified with β-N-acetylglucosamine
(O-GlcNAc) 1 (1-3). In each case studied, the glycan has a turnover rate that is much ... Cited by 107 - Related articles - BL Direct - All 6 versions
- ►jbc.org ZT Kneass, RB Marchase - Journal of Biological Chemistry, 2005 - ASBMB The modification of serine/threonine residues on cytoplasmic and nuclear proteins by N-acetylglucosamine
(O-GlcNAc) is suggested to play a role in the regulation of a variety of signal transduction
pathways. We have previously shown that glucosamine (GlcNH 2 ), a metabolic precursor ... Cited by 30 - Related articles - All 4 versions
- ►fasebj.org [PDF] C D'Alessandris, F Andreozzi, M Federici, M Cardellini, … - The FASEB Journal, 2004 - FASEB Page 1. The FASEB Journal express article 10.1096/fj.03-0725fje. Published online April
1, 2004. Increased O-glycosylation of insulin signaling proteins results in their impaired
activation and enhanced susceptibility to apoptosis in pancreatic β-cells ... Cited by 27 - Related articles - BL Direct - All 5 versions
HJ Goldberg, CI Whiteside, IG Fantus - Journal of Biological Chemistry, 2002 - ASBMB Increased flux through the hexosamine biosynthesis pathway (HBP) has been shown to stimulate
the expression of a number of genes. We previously demonstrated in glomerular mesangial and
endothelial cells that both high glucose concentrations and glucosamine activated the ... Cited by 53 - Related articles - BL Direct - All 5 versions
- ►pnas.org DA McClain, WA Lubas, RC Cooksey, M … - Proceedings of the …, 2002 - National Acad Sciences Insulin resistance and β cell toxicity are key features of type 2 diabetes. One leading hypothesis
suggests that these abnormalities result from excessive flux of nutrients through the UDP–hexosamine
biosynthetic pathway leading to “glucose toxicity.” How the products of the hexosamine ... Cited by 103 - Related articles - BL Direct - All 10 versions
- ►endojournals.org HJ Goldberg, CI Whiteside, GW Hart, IG Fantus - Endocrinology, 2006 - Endocrine Soc Metabolic flux through the hexosamine biosynthetic pathway (HBP) is increased in the presence
of high glucose (HG) and potentially stimulates the expression of genes associated with the development
of diabetic nephropathy. A number of synthetic processes are coupled to the HBP, ... Cited by 28 - Related articles - BL Direct - All 4 versions
- ►ahajournals.org M Federici, R Menghini, A Mauriello, ML Hribal, F … - Circulation, 2002 - Am Heart Assoc Methods and Results— O-GlcNAcylation impaired the metabolic branch of insulin signaling,
ie, insulin receptor (IR) activation of the IR substrate (IRS)/phosphatidylinositol 3-kinase
(PI3-K)/Akt, whereas it enhanced the mitogenic branch, ie, ERK-1/2 and p38 (mitogen- ... Cited by 136 - Related articles - BL Direct - All 7 versions
