1996. Donald A- McClain and Errol D. Crook.
Hexosamines and insulin resistance.
Hexosamines and insulin resistance.
https://pdfs.semanticscholar.org/0ef8/e53ad88bf9cbe23618ddba0fa4d50e01af0a.pdf
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Over 500 articles, 11.12. 2018
1.
Padma Bhonagiri, Guruprasad R. Pattar, Kirk M. Habegger, Alicia M. McCarthy, Lixuan Tackett, Jeffrey S. Elmendorf
Endocrinology. 2011 Sep; 152(9): 3373–3384. Published online 2011 Jun 28. doi: 10.1210/en.2011-1295
- PMCID:
- PMC3159786
2.
Wei Zhang, Jiarong Liu, Ling Tian, Qinglan Liu, Yuchang Fu, W. Timothy Garvey
Diabetes. 2013 Dec; 62(12): 4192–4200. Published online 2013 Nov 16. doi: 10.2337/db13-0312
3.
Hexosamines, insulin resistance and the complications of diabetes: current status.
Maria G. Buse
Am J Physiol Endocrinol Metab. Author manuscript; available in PMC 2007 Jan 1.
Published in final edited form as: Am J Physiol Endocrinol Metab. 2006 Jan; 290(1): E1–E8. doi: 10.1152/ajpendo.00329.2005
4.
Chin Fen Teo, Edith E. Wollaston-Hayden, Lance Wells
Mol Cell Endocrinol. Author manuscript; available in PMC 2011 Apr 29.
Published in final edited form as: Mol Cell Endocrinol. 2010 Apr 29; 318(1-2): 44–53. Published online 2009 Sep 30. doi: 10.1016/j.mce.2009.09.022
5.
Francine
H. Einstein, Sigal Fishman, Jeffery Bauman, Reid F. Thompson, Derek M.
Huffman, Gil Atzmon, Nir Barzilai, Radhika H. Muzumdar
FASEB J. 2008 Oct; 22(10): 3450–3457. doi: 10.1096/fj.08-109041
Results of chronic but physiologic changes in hexosamine flux induced by tissue-specific over expression of the rate-limiting enzyme in the HBP, glutamine:fructose-6-P amidotransferase (GFA) have shown that the HBP serves a nutrient sensing function and affects metabolism in a wide-ranging manner in liver, muscle, fat, and beta cells (Hebert et al. 1996; Cooksey et al. 1999; McClain et al. 2000; Tang et al. 2000; Veerababu et al. 2000; Hazel et al. 2003). The insulin resistance induced by HBP flux mimics that of type 2 diabetes in being characterized by decreased recruitment of GLUT4 to the plasma membrane and reversibility by the antidiabetic drug troglitazone (Baron et al. 1995; Cooksey et al. 1999).
Results of chronic but physiologic changes in hexosamine flux induced by tissue-specific over expression of the rate-limiting enzyme in the HBP, glutamine:fructose-6-P amidotransferase (GFA) have shown that the HBP serves a nutrient sensing function and affects metabolism in a wide-ranging manner in liver, muscle, fat, and beta cells (Hebert et al. 1996; Cooksey et al. 1999; McClain et al. 2000; Tang et al. 2000; Veerababu et al. 2000; Hazel et al. 2003). The insulin resistance induced by HBP flux mimics that of type 2 diabetes in being characterized by decreased recruitment of GLUT4 to the plasma membrane and reversibility by the antidiabetic drug troglitazone (Baron et al. 1995; Cooksey et al. 1999).
6.
Brent A. Penque, April M. Hoggatt, B. Paul Herring, Jeffrey S. Elmendorf
Mol Endocrinol. 2013 Mar; 27(3): 536–547. Published online 2013 Jan 11. doi: 10.1210/me.2012-1213
Increased caloric intake and/or obesity are currently the greatest
predisposing risk factors for the development of type 2 diabetes (T2D).
Recent study implicates increased nutrient flux through the hexosamine
biosynthesis pathway (HBP) as an underlying basis for the development
and exacerbation of insulin resistance and β-cell failure, hallmark
events in the pathology of T2D. As such, a concerted research effort has
been underway to gain mechanistic insight into how HBP activity results
in desensitization of the glucose transport system.
7.
Increased hexosamine pathway flux and high fat feeding are not additive in inducing insulin resistance: evidence for a shared pathway Robert C. Cooksey, Donald A. McClain
Amino Acids. Author manuscript; available in PMC 2012 Mar 1. Published in final edited form as: Amino Acids. 2011 Mar; 40(3): 841–846. Published online 2010 Jul 24. doi: 10.1007/s00726-010-0701-5
(Baron et al. 1995; Cooksey et al. 1999). These data are consistent with a shared nutrient sensing pathway for
high fat and carbohydrate fluxes and a common pathway by which glucose
and lipids induce insulin resistance.
8.
Padma Bhonagiri, Guruprasad R. Pattar, Emily M. Horvath, Kirk M. Habegger, Alicia M. McCarthy, Jeffrey S. Elmendorf
Endocrinology. 2009 Apr; 150(4): 1636–1645. Published online 2008 Nov 26. doi: 10.1210/en.2008-1102
- Retraction in:
- Endocrinology. 2010 Jun; 151(6): 2967.
9.
L F Hebert, Jr, M C Daniels, J Zhou, E D Crook, R L Turner, S T Simmons, J L Neidigh, J S Zhu, A D Baron, D A McClain
J Clin Invest. 1996 Aug 15; 98(4): 930–936. doi: 10.1172/JCI118876
10.
Jérémie Boucher, André Kleinridders, C. Ronald Kahn
Cold Spring Harb Perspect Biol. 2014 Jan; 6(1): a009191. doi: 10.1101/cshperspect.a009191
- In the wake of the worldwide increase in type-2 diabetes, a major focus of research is understanding the signaling pathways impacting this disease. Insulin signaling regulates glucose, lipid, and energy homeostasis, predominantly via action on liver, skeletal muscle, and adipose tissue. Precise modulation of this pathway is vital for adaption as the individual moves from the fed to the fasted state. The positive and negative modulators acting on different steps of the signaling pathway, as well as the diversity of protein isoform interaction, ensure a proper and coordinated biological response to insulin in different tissues. Whereas genetic mutations are causes of rare and severe insulin resistance, obesity can lead to insulin resistance through a variety of mechanisms. Understanding these pathways is essential for development of new drugs to treat diabetes, metabolic syndrome, and their complications.
11.
Ronald J. Copeland, John W. Bullen, Gerald W. Hart
Am J Physiol Endocrinol Metab. 2008 Jul; 295(1): E17–E28. doi: 10.1152/ajpendo.90281.2008
O-linked β-N-acetylglucosamine (O-GlcNAc)
is a dynamic posttranslational modification that, analogous to
phosphorylation, cycles on and off serine and/or threonine hydroxyl
groups. Cycling of O-GlcNAc is regulated by the concerted actions of O-GlcNAc transferase and O-GlcNAcase.
GlcNAcylation is a nutrient/stress-sensitive modification that
regulates proteins involved in a wide array of biological processes,
including transcription, signaling, and metabolism. GlcNAcylation is
involved in the etiology of glucose toxicity and chronic
hyperglycemia-induced insulin resistance, a major hallmark of type 2
diabetes. Several reports demonstrate a strong positive correlation
between GlcNAcylation and the development of insulin resistance.
However, recent studies suggest that inhibiting GlcNAcylation does not
prevent hyperglycemia-induced insulin resistance, suggesting that other
mechanisms must also be involved. To date, proteomic analyses have
identified more than 600 GlcNAcylated proteins in diverse functional
classes. However, O-GlcNAc sites have been mapped on only a
small percentage (<15 also="" and="" antibodies="" between="" both="" brain="" but="" complex="" cord="" cross-talk="" decipher="" design="" elucidate="" em="" for="" from="" further="" generation="" glcnacylation="" help="" is="" isolated="" key="" mapping="" metabolically="" most="" mutational="" necessary="" not="" of="" only="" or="" other="" phosphorylation="" proteins="" relevant="" site-specific="" sites="" spinal="" studies="" the="" these="" tissue="" tissues.="" to="" were="" which="" will="">O
12.
Meghana Pansuria, Hang Xi, Le Li, Xiao-Feng Yang, Hong Wang
Front Biosci (Schol Ed) Author manuscript; available in PMC 2012 Apr 4.
Published in final edited form as: Front Biosci (Schol Ed). 2012 Jan 1; 4: 916–931. Published online 2012 Jan 1.
14.
M C Daniels, T P Ciaraldi, S Nikoulina, R R Henry, D A McClain
J Clin Invest. 1996 Mar 1; 97(5): 1235–1241. doi: 10.1172/JCI118538
17.
Patrice
E. Fort, Mandy K. Losiewicz, Chad E. N. Reiter, Ravi S. J. Singh,
Makoto Nakamura, Steven F. Abcouwer, Alistair J. Barber, Thomas W.
Gardner
PLoS One. 2011; 6(10): e26498. Published online 2011 Oct 26. doi: 10.1371/journal.pone.0026498
18.
Inken
Padberg, Erik Peter, Sandra González-Maldonado, Henning Witt, Matthias
Mueller, Tanja Weis, Bianca Bethan, Volker Liebenberg, Jan Wiemer, Hugo
A. Katus, Dietrich Rein, Philipp Schatz
PLoS One. 2014; 9(1): e85082. Published online 2014 Jan 17. doi: 10.1371/journal.pone.0085082
19.
Kazuhiro Yanagida, Yuko Maejima, Putra Santoso, Zesemdorj Otgon-Uul, Yifei Yang, Kazuya Sakuma, Kenju Shimomura, Toshihiko Yada
Aging (Albany NY) 2014 Mar; 6(3): 207–214. Published online 2014 Mar 29. doi: 10.18632/aging.100647
Hyperglycemia (HG) impairs insulin secretion as well as insulin action, being recognized as the glucotoxicity that accelerates diabetes. However, the mechanism underlying the glucotoxicity in pancreatic β-cells is not thoroughly understood. Hyperglycemia alters glucose metabolism within β-cells and interstitial conditions around β-cells, including elevated osmolarity and increased concentrations of insulin and ATP released from overstimulated β-cells..
. These results suggest that the HG-associated abnormal glucose metabolism through hexosamine pathway, but not elevated osmolarity, insulin and ATP, plays a major role in the glucotoxicity to impair the secretory function of pancreatic
Hyperglycemia (HG) impairs insulin secretion as well as insulin action, being recognized as the glucotoxicity that accelerates diabetes. However, the mechanism underlying the glucotoxicity in pancreatic β-cells is not thoroughly understood. Hyperglycemia alters glucose metabolism within β-cells and interstitial conditions around β-cells, including elevated osmolarity and increased concentrations of insulin and ATP released from overstimulated β-cells..
. These results suggest that the HG-associated abnormal glucose metabolism through hexosamine pathway, but not elevated osmolarity, insulin and ATP, plays a major role in the glucotoxicity to impair the secretory function of pancreatic
20.
Arthur D. Zimmerman, Ruth B. S. Harris
Am J Physiol Regul Integr Comp Physiol. 2015 Mar 15; 308(6): R543–R555. Published online 2015 Jan 7. doi: 10.1152/ajpregu.00347.2014
the cytokine leptin is released primarily from white adipose tissue and is hypothesized to function as a negative feedback signal in the control of energy balance (52) by inhibiting food intake and causing weight loss in normal weight animals (12, 14).
Activity of the hexosamine biosynthetic pathway (HBP) increases in response to increased substrate availability. Therefore, the HBP has been proposed to serve as a nutrient sensor that can modify metabolism and energy expenditure
Once glucose enters a cell it is rapidly converted to glucose-6-phosphate and then fructose-6-phosphate, a majority of which enters glycolysis. Normally, 1–3% of the fructose-6-phosphate enters the HBP, Hexose Biosynthesis Pathway (27).
. When nutrient availability is increased, a greater percentage of the fructose-6-phosphate is shunted to the HBP where it is converted into glucosamine-6-phosphate (GlcN-6P) by glutamine fructose-6-phosphate amidotransferase (GFAT), the rate-limiting enzyme for glucose entry into the HBP (5, 29).
The product of the pathway, uridine 5′-diphospho-N-acetylglucosamine (UDP-GlcNAc), is the substrate for O-linked β-N-acetylglucosamine (O-GlcNAc) modification of serine or threonine residues of cytosolic and nuclear proteins.
This reversible reaction is catalyzed by O-GlcNAc transferase (OGT) (45). The removal of O-GlcNAc is dependent on the enzyme β-d-N acetylglucosaminidase (O-GlcNAcase) (25, 51).
Hundreds of proteins critical to the cell cycle, embryonic survival, the cellular stress response, and many other cellular functions are O-GlcNAc modified (25, 47, 51).
the cytokine leptin is released primarily from white adipose tissue and is hypothesized to function as a negative feedback signal in the control of energy balance (52) by inhibiting food intake and causing weight loss in normal weight animals (12, 14).
Activity of the hexosamine biosynthetic pathway (HBP) increases in response to increased substrate availability. Therefore, the HBP has been proposed to serve as a nutrient sensor that can modify metabolism and energy expenditure
Once glucose enters a cell it is rapidly converted to glucose-6-phosphate and then fructose-6-phosphate, a majority of which enters glycolysis. Normally, 1–3% of the fructose-6-phosphate enters the HBP, Hexose Biosynthesis Pathway (27).
. When nutrient availability is increased, a greater percentage of the fructose-6-phosphate is shunted to the HBP where it is converted into glucosamine-6-phosphate (GlcN-6P) by glutamine fructose-6-phosphate amidotransferase (GFAT), the rate-limiting enzyme for glucose entry into the HBP (5, 29).
The product of the pathway, uridine 5′-diphospho-N-acetylglucosamine (UDP-GlcNAc), is the substrate for O-linked β-N-acetylglucosamine (O-GlcNAc) modification of serine or threonine residues of cytosolic and nuclear proteins.
This reversible reaction is catalyzed by O-GlcNAc transferase (OGT) (45). The removal of O-GlcNAc is dependent on the enzyme β-d-N acetylglucosaminidase (O-GlcNAcase) (25, 51).
Hundreds of proteins critical to the cell cycle, embryonic survival, the cellular stress response, and many other cellular functions are O-GlcNAc modified (25, 47, 51).
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