Beyond Diabetes Mellitus: protein glycosylation
Keywords:
Diabetes mellitus, Hyperglycemia, Glycosylation end products advancedAbstract
The evidence supporting chronic hyperglycemia as the cause of a series of macro and microvascularcomplications are devastating. Pathophysiologic changes that result from this condition go beyond the meaning of high levels of glucose, as a result of inadequate insulin secretion or tissue resistance to the entry of glucose into cells. The consequences of these high glucose levels for prolonged periods, ultimately lead to the glycation of proteins, the consequences of a malfunction, in addition to the formation of advanced glycation end products. The evaluation of glycated hemoglobin, glycated albumin or time are indicative proteins bearing exposed to high concentrations of glucose or glycemic condition of the patient, but also involved in long-term complications as diabetic nephropathy. The consequence of these glycated proteins and the formation of advanced glycation end products are the malfunction of vital organs aging and development of degenerative diseases like Alzheimer’s.
Downloads
Download data is not yet available.
References
1. Association. AD. Diagnosis and classification of diabetes mellitus. Diabetes care. 2005; 28:S37.
2. Nenna A, Spadaccio C, Lusini M, Ulianich L, Chello M, Nappi F. Basic and clinical research against Advanced Glycation End Products (AGEs): new compounds to tackle cardiovascular disease and diabetic complications. Recent patents on cardiovascular drug discovery; 2015.
3. Thornalley P, Langborg A, Minhas H. Formation of glyoxal, methylglyoxal and 3-deoxyglucosone in the glycation of proteins by glucose. Biochem J. 1999; 344:109-16.
4. Calderón Salinas JV, Muñoz Reyes EG, Quintanar Escorza MA. Estrés oxidativo y diabetes mellitus. REB Revista de Educación Bioquímica. 2013; 32(2):53-66.
5. Gugliucci A. Glicación de proteínas: rol protagónico de la hiperglicemia en las complicaciones crónicas de la diabetes mellitus. Rev Med Uruguay. 2000; 16:58-75.
6. Atlas ID. International Diabetes Federation (2012). ISBN 2930229853. 2012:7.
7. Organization WH. Global Health Estimates: Deaths by Cause, Age, Sex and Country, 2000-2012. Geneva: WHO; 2014.
8. Mathers CD, Loncar D. Projections of global mortality and burden of disease from 2002 to 2030. Plos med. 2006; 3(11):e442.
9. Aschner P. Epidemiología de la diabetes en Colombia. Avances en diabetología. 2010; 26(2):95-100.
10. Mantilla MET. La hiperglicemia y sus efectos tóxicos. Un concepto patogénico para la micro y macroangiopatía diabética. Rev Cubana Angiol y Cir Vasc. 2001; 2(2):131-41.
11. Wiwanitkit V. Myoglobin glycosylation process in poorly controlled diabetes. Diabetes & Metabolic Syndrome: Clinical Research & Reviews. 2010; 4(1):3-4.
12. Nenna A, Nappi F, Avtaar Singh SS, Sutherland FW, Di Domenico F, Chello M, et al. Pharmacologic Approaches Against Advanced Glycation End Products (AGEs) in Diabetic Cardiovascular Disease. Research in cardiovascular medicine. 2015; 4(2).
13. Kuschnerus K, Landmesser U, Kränkel N. Vascular repair strategies in type 2 diabetes: novel insights. Cardiovascular Diagnosis and Therapy. 2015; 5(5):374.
14. Njoroge FG, Monnier VM. The chemistry of the Maillard reaction under physiological conditions: a review. Progress in clinical and biological research. 1988; 304:85-107.
15. Steinmetz PR, Balko C, Gabbay KH. The sorbitol pathway and the complications of diabetes. New England Journal of Medicine. 1973; 288(16):831-6.
16. Ziyadeh F. Mediators of hyperglycemia and the pathogenesis of matrix accumulation in diabetic renal disease. Mineral and electrolyte metabolism. 1994; 21(4-5):292-302.
17. Boel E, Selmer J, Flodgaard HJ, Jensen T. Diabetic late complications: will aldose reductase inhibitors or inhibitors of advanced glycosylation endproduct formation hold promise? Journal of Diabetes and its Complications. 1995; 9(2):104-29.
18. Giugliano D, Ceriello A, Paolisso G. Diabetes mellitus, hypertension, and cardiovascular disease: which role for oxidative stress? Metabolism. 1995; 44(3):363-8.
19. Lopes-Virella MF, Virella G. Cytokines, modified lipoproteins, and arteriosclerosis in diabetes. Diabetes. 1996; 45(Supplement 3):S40-S4.
20. Cruz Hernández J, Licea Puig M, Hernández García P, Abraham Marcel E, Yanes Quesada M. Aldosa reductasa y proteína quinasa C en las complicaciones crónicas de la diabetes mellitus. Rev Mex Patol Clin [Internet]. 2012; 58(2):102-7.
21. Díaz-Flores M, Baiza-Gutman LA, Ibáñez-Hernández MÁ, Pascoe-Lira D, Guzmán-Greenfel AM, Kumate-Rodríguez J. Aspectos moleculares del daño tisular inducido por la hiperglucemia crónica. Gaceta médica de México. 2004; 140(4):437-47.
22. Chung S, Chung S. Aldose reductase in diabetic microvascular complications. Current drug targets. 2005; 6(4):475-86. 23. Mellor H, Parker P. The extended protein kinase C superfamily. Biochem J. 1998; 332:281-92.
24. Dahl-Jørgensen K, Brinchmann-Hansen O, Bangstad H-J, Hanssen K. Blood glucose control and microvascular complicationswhat do we do now? Diabetologia. 1994; 37(12):1172-7.
25. Tabit CE, Chung WB, Hamburg NM, Vita JA. Endothelial dysfunction in diabetes mellitus: molecular mechanisms and clinical implications. Reviews in Endocrine and Metabolic Disorders. 2010; 11(1):61-74.
26. Brownlee M. Advanced products of nonenzymatic glycosylation and the pathogenesis of diabetic complications. Diabetes mellitus: theory and practice. 1990; 1:279.
27. Stevens VJ, Vlassara H, Abati A, Cerami A. Nonenzymatic glycosylation of hemoglobin. Journal of Biological Chemistry. 1977; 252(9):2998-3002.
28. Shaklai N, Garlick RL, Bunn HF. Nonenzymatic glycosylation of human serum albumin alters its conformation and function. Journal of Biological Chemistry. 1984; 259(6):3812-7.
29. Vlassara H, Bucala R. Recent progress in advanced glycation and diabetic vascular disease: role of advanced glycation end product receptors. Diabetes. 1996; 45(Supplement 3):S65-S6.
30. Cohen MP. Intervention strategies to prevent pathogenetic effects of glycated albumin. Archives of biochemistry and biophysics. 2003; 419(1):25-30.
31. Jaleel A, Halvatsiotis P, Williamson B, Juhasz P, Martin S, Nair KS. Identification of Amadori-modified plasma proteins in type 2 diabetes and the effect of short-term intensive insulin treatment. Diabetes care. 2005; 28(3):645-52.
32. Takeuchi M, Takino J-I, Yamagishi S-I. Involvement of TAGE-RAGE system in the pathogenesis of diabetic retinopathy. Journal of Ophthalmology. 2010; 2010:1-12.
33. Méndez JD. Productos finales de glicación avanzada y complicaciones crónicas de la diabetes mellitus. Gac Med Mex. 2003; 139(1):49-55.
2. Nenna A, Spadaccio C, Lusini M, Ulianich L, Chello M, Nappi F. Basic and clinical research against Advanced Glycation End Products (AGEs): new compounds to tackle cardiovascular disease and diabetic complications. Recent patents on cardiovascular drug discovery; 2015.
3. Thornalley P, Langborg A, Minhas H. Formation of glyoxal, methylglyoxal and 3-deoxyglucosone in the glycation of proteins by glucose. Biochem J. 1999; 344:109-16.
4. Calderón Salinas JV, Muñoz Reyes EG, Quintanar Escorza MA. Estrés oxidativo y diabetes mellitus. REB Revista de Educación Bioquímica. 2013; 32(2):53-66.
5. Gugliucci A. Glicación de proteínas: rol protagónico de la hiperglicemia en las complicaciones crónicas de la diabetes mellitus. Rev Med Uruguay. 2000; 16:58-75.
6. Atlas ID. International Diabetes Federation (2012). ISBN 2930229853. 2012:7.
7. Organization WH. Global Health Estimates: Deaths by Cause, Age, Sex and Country, 2000-2012. Geneva: WHO; 2014.
8. Mathers CD, Loncar D. Projections of global mortality and burden of disease from 2002 to 2030. Plos med. 2006; 3(11):e442.
9. Aschner P. Epidemiología de la diabetes en Colombia. Avances en diabetología. 2010; 26(2):95-100.
10. Mantilla MET. La hiperglicemia y sus efectos tóxicos. Un concepto patogénico para la micro y macroangiopatía diabética. Rev Cubana Angiol y Cir Vasc. 2001; 2(2):131-41.
11. Wiwanitkit V. Myoglobin glycosylation process in poorly controlled diabetes. Diabetes & Metabolic Syndrome: Clinical Research & Reviews. 2010; 4(1):3-4.
12. Nenna A, Nappi F, Avtaar Singh SS, Sutherland FW, Di Domenico F, Chello M, et al. Pharmacologic Approaches Against Advanced Glycation End Products (AGEs) in Diabetic Cardiovascular Disease. Research in cardiovascular medicine. 2015; 4(2).
13. Kuschnerus K, Landmesser U, Kränkel N. Vascular repair strategies in type 2 diabetes: novel insights. Cardiovascular Diagnosis and Therapy. 2015; 5(5):374.
14. Njoroge FG, Monnier VM. The chemistry of the Maillard reaction under physiological conditions: a review. Progress in clinical and biological research. 1988; 304:85-107.
15. Steinmetz PR, Balko C, Gabbay KH. The sorbitol pathway and the complications of diabetes. New England Journal of Medicine. 1973; 288(16):831-6.
16. Ziyadeh F. Mediators of hyperglycemia and the pathogenesis of matrix accumulation in diabetic renal disease. Mineral and electrolyte metabolism. 1994; 21(4-5):292-302.
17. Boel E, Selmer J, Flodgaard HJ, Jensen T. Diabetic late complications: will aldose reductase inhibitors or inhibitors of advanced glycosylation endproduct formation hold promise? Journal of Diabetes and its Complications. 1995; 9(2):104-29.
18. Giugliano D, Ceriello A, Paolisso G. Diabetes mellitus, hypertension, and cardiovascular disease: which role for oxidative stress? Metabolism. 1995; 44(3):363-8.
19. Lopes-Virella MF, Virella G. Cytokines, modified lipoproteins, and arteriosclerosis in diabetes. Diabetes. 1996; 45(Supplement 3):S40-S4.
20. Cruz Hernández J, Licea Puig M, Hernández García P, Abraham Marcel E, Yanes Quesada M. Aldosa reductasa y proteína quinasa C en las complicaciones crónicas de la diabetes mellitus. Rev Mex Patol Clin [Internet]. 2012; 58(2):102-7.
21. Díaz-Flores M, Baiza-Gutman LA, Ibáñez-Hernández MÁ, Pascoe-Lira D, Guzmán-Greenfel AM, Kumate-Rodríguez J. Aspectos moleculares del daño tisular inducido por la hiperglucemia crónica. Gaceta médica de México. 2004; 140(4):437-47.
22. Chung S, Chung S. Aldose reductase in diabetic microvascular complications. Current drug targets. 2005; 6(4):475-86. 23. Mellor H, Parker P. The extended protein kinase C superfamily. Biochem J. 1998; 332:281-92.
24. Dahl-Jørgensen K, Brinchmann-Hansen O, Bangstad H-J, Hanssen K. Blood glucose control and microvascular complicationswhat do we do now? Diabetologia. 1994; 37(12):1172-7.
25. Tabit CE, Chung WB, Hamburg NM, Vita JA. Endothelial dysfunction in diabetes mellitus: molecular mechanisms and clinical implications. Reviews in Endocrine and Metabolic Disorders. 2010; 11(1):61-74.
26. Brownlee M. Advanced products of nonenzymatic glycosylation and the pathogenesis of diabetic complications. Diabetes mellitus: theory and practice. 1990; 1:279.
27. Stevens VJ, Vlassara H, Abati A, Cerami A. Nonenzymatic glycosylation of hemoglobin. Journal of Biological Chemistry. 1977; 252(9):2998-3002.
28. Shaklai N, Garlick RL, Bunn HF. Nonenzymatic glycosylation of human serum albumin alters its conformation and function. Journal of Biological Chemistry. 1984; 259(6):3812-7.
29. Vlassara H, Bucala R. Recent progress in advanced glycation and diabetic vascular disease: role of advanced glycation end product receptors. Diabetes. 1996; 45(Supplement 3):S65-S6.
30. Cohen MP. Intervention strategies to prevent pathogenetic effects of glycated albumin. Archives of biochemistry and biophysics. 2003; 419(1):25-30.
31. Jaleel A, Halvatsiotis P, Williamson B, Juhasz P, Martin S, Nair KS. Identification of Amadori-modified plasma proteins in type 2 diabetes and the effect of short-term intensive insulin treatment. Diabetes care. 2005; 28(3):645-52.
32. Takeuchi M, Takino J-I, Yamagishi S-I. Involvement of TAGE-RAGE system in the pathogenesis of diabetic retinopathy. Journal of Ophthalmology. 2010; 2010:1-12.
33. Méndez JD. Productos finales de glicación avanzada y complicaciones crónicas de la diabetes mellitus. Gac Med Mex. 2003; 139(1):49-55.
Downloads
Published
2016-06-01
Issue
Section
Articles
License
-
Reconocimiento — Debe reconocer adecuadamente la autoría, proporcionar un enlace a la licencia e indicar si se han realizado cambios<. Puede hacerlo de cualquier manera razonable, pero no de una manera que sugiera que tiene el apoyo del licenciador o lo recibe por el uso que hace.
-
NoComercial — No puede utilizar el material para una finalidad comercial.
-
CompartirIgual — Si remezcla, transforma o crea a partir del material, deberá difundir sus contribuciones bajo la misma licencia que el original.
- No hay restricciones adicionales — No puede aplicar términos legales o medidas tecnológicas que legalmente restrinjan realizar aquello que la licencia permite.
How to Cite
Beyond Diabetes Mellitus: protein glycosylation. (2016). Biociencias, 11(1), 105-111. https://revistas.unilibre.edu.co/index.php/biociencias/article/view/2875
