Carvajal-Sandoval G, Zamudio-Cortes P, Carvajal-Juárez ME, Juárez-de Carvajal E

Language: Spanish
References: 24
Page: 51-59
PDF size: 200.18 Kb.

ABSTRACT

Diabetes mellitus and aging are two similar health problems where causes of death are the same for both. Recently they described that damages produced are the result of “non enzymatic glycosylation” (“glycation”) that leads to the formation of a wide variety of advanced products of glycosylation, known as AGE’s (Advanced Glycosylation End products). Research with streptozotocin-induced diabetic rats (60 mg/kg of weight) that consumed glycine 1% ad libitum in drinking water measured the concentration of glycosylate hemoglobin (HbA1c), and showed that glycine avoids the “glycation” of proteins. We administered 20 gr of glycine four times per day and also observed a decrease of HbA1c in diabetic patients. In animal experiments glycine corrected the diabetic neuropathy modifying the speed conduction of the sciatic nerve. Also among diabetic rats it diminished erythrocyte deformity whereas those who took glycine improved the deformity associated with having passed through a membrane. Glycine increased the capacity of mononuclear proliferation of peripheral blood among rats exposed to mitogens. The improvement has been described in the humoral immunity of diabetic rats that took glycine (Cunningham plaques). Leucocoria (first stage cataracts) were not observed among diabetic rats that took glycine. The hypertrygliceridaemia brought about in diabetic rats can produce hypertension and excessive deposit of retroperitoneal fat whereas in rats that take glycine this phenomenon is not observed. In addition hypertrygliceridaemic rats display an increase of serum free acids whereas among rats that take glycine this diminishes to normal values. Decrease of microalbuminuria observed in diabetic rats, suggests protection against renal damage. The most striking case was seen in a diabetic patient who presented initially very high hyperglycemia and 21%, HbA1c. Six months after glycine intake, values showed a normal tolerance curve to glucose and normal HbA1c.

REFERENCES

1. Kumate Rodríguez J. Atlas de la salud. 1a impresión 1993. pp 39 y XI.

2. Monnier VM, Cerami A. Nonenzymatic Browning in vivo: Possible Process for Aging of Long-Lived Proteins. Science 1981;211:491-493.

3. Brownlee M. Cerami A. The biochemistry of the complications of diabetes mellitus. Ann Rev Biochem 1991;50:385-432.

4. Brownlee M. Advanced Glycation End products in diabetes and ageing. Ann Rev Med 1995;46:223-234.

5. Borsook H, Abrams A, Lowy PH. Fructose-amino acids in liver: Stimuli of amino acid incorporation “in vitro” 1. BioI Chem 1995;215: 111-124.

6. New and nonofficial remedies. J Am Med Assoc 1935;104:1241.

7. Rahbar S. An abnormal hemoglobin in red cell of diabetes. Clin Chim Acta 1968;22:296-298.

8. Koenig R, Peterson CM, Kilo C, Cerami A, Williamson JR. Hemoglobin A1c as an indicator of the degree of glucose intolerance in diabetes. Diabetes 1976;25(3)230-232.

9. Koenig R, Peterson CM, Jones RL, Saudek C, Lehrman M, Cerami A. Correlation of Glucose Regulation and Hemoglobin A1c in Diabetes mellitus. New Engl J Med 1976;295(8)417-420.

10. Brownlee M, Vlassara H, Cerami A. Nonenzymatic Glycosylation and the Pathogenesis of Diabetic Complications. Ann Intern Med 1984;101:527-537.

11. Brownlee M, Cerami A, Vlassara H. The biochemistry of the complications of Diabetes mellitus. Ann Rev Biochem 1981;50:385-432. Vlassara H, Palace MR. Diabetes and advanced glycation endproducts. J Intern Med 2002;251:87-101.

12. Koenig R, Peterson CM, Vlassara H. Advanced glycosylation end products in tissues and the biochemical basis of diabetic complications. New EngI J Med 1988;318:1315-1321.

13. Pierpaoli W, Fabris N. Physiological Senescence and its Postponement. Ann NY Acad Sci 1991; Vol 621.

14. Harman D, Holliday R, Meydani M. Towards prolongation of the healthy life span. Practical Approches to Intervention. Ann NY Acad Sci 1998; Vol. 854.

15. Park SCh. Hwang ES, Kim HS, Park WY. Healthy Aging for Functional Longevity., Molecular & Cellular Interactions in Senescence. Ann NY Acad Sci 2001; Vol. 928.

16. Nakhoda A, Y Wong HA, The induction of diabetes in rats by intramuscular administration of streptozotocin. Experientia. 1979;35:1679-1680.

17. Velasco DE, De la Cruz LF, Chambert CG, De Carvajal EJ, Ramos MG, Carvajal-S G. Efecto protector de la glicina sobre la velocidad de conducción del nervio ciático de ratas diabéticas. Cong Nac Cienc Fisiol Puebla (México) Ago. (1985) Trabajo No. 230.

18. Birrell AM, Hefferman SJ, Ansselin AD, Mc Lennan S, Church DK, Gitlin AG, et al. Functional and Structural abnormalities in the nerves of Type I diabetec baboons: aminoguanidine treatment does not improve nerve function. Diabetologia 2000;43:110-116.

19. Lazcano MD. Efecto de la Glicina en la respuesta inmune a eritrocitos de borrego en ratas. Tesis de Maestría. ENCB. IPN, México, 1996.

20. McMillan DE, Utterback NG, La Puma J. Reduced Erythrocyte Deformability in Diabetes. Diabetes. 1978;27:895-901.

21. Miller JA, Gravallese E, Bunn HF. Nonenzymatic Glycosylation of Erythrocyte Membrane Proteins. J Clin Invest 1980;65:896-901.

22. El Hafidi M, Pérez l, Zamora J, Soto V, Carvajal SG, Baños G. Glycine Intake Decreases Rat Plasma Free Fatty Acids. Adipose cell size, Visceral Fat Accumulation and Blood Pressure in Sucrose fed rats. Am J Physiol Regul Integr Comp Physiol 2004;287:R1387-R1393.

23. Carvajal SG, Juárez de CE, Ramos MG, Carvajal JME. “Curación o Regresión espontánea de la Diabetes mellitus Tipo II tratada con Glicina”. Taxco, Guerrero. México: Resúmenes XI Cong Nac De Farmacol 1987, pp 45.

24. Carvajal-Sandoval G, Juárez de Carvajal E, Ramos-Martínez G, Carvajal-Juárez ME. Inhibición de la glicosilación no enzimática de la hemoglobina