A novel method to quantify in vivo transferrin glycation: Applications in diabetes mellitus

Clinica Chimica Acta

Volumn 370, Issue 1-2, 2006, Pages 115-123

  Van Campenhout, Ann ^a   Van Campenhout, Christel ^b   Olyslager, Yung S ^b   Van Damme, Oliver ^b   Lagrou, Albert R ^a   Manuel y Keenoy, Begoña ^a  

^a UNIVERSITY OF ANTWERP   (Belgium)

^b ANTWERP UNIVERSITY HOSPITAL   (Belgium)

Author keywords

Diabetes mellitus; Fructosamine; Glycation; Iron; Oxidative stress; Transferrin

Indexed keywords

ANTIBODY; ANTIGEN; FRUCTOSAMINE; INSULIN; IRON; NITROBLUE TETRAZOLIUM; TRANSFERRIN;

ADULT; AGED; ANALYTIC METHOD; ANTIGEN ANTIBODY COMPLEX; ARTICLE; CONTROLLED STUDY; CORRELATION ANALYSIS; FEMALE; GLYCATION; GLYCEMIC CONTROL; HUMAN; IN VIVO STUDY; INSULIN DEPENDENT DIABETES MELLITUS; IRON BINDING CAPACITY; IRON BLOOD LEVEL; MAJOR CLINICAL STUDY; MALE; NON INSULIN DEPENDENT DIABETES MELLITUS; PRIORITY JOURNAL; QUANTITATIVE ANALYSIS; STATISTICAL SIGNIFICANCE; TECHNIQUE;

DIABETES MELLITUS; FEMALE; GLYCOSYLATION; HUMANS; IMMUNOASSAY; IRON; MALE; MIDDLE AGED; TRANSFERRIN;

EID: 33746085228     PISSN: 00098981     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cca.2006.01.028     Document Type: Article

References (51)

1. Baynes J.W. Role of oxidative stress in development of complications in diabetes. Diabetes 40 (1991) 405-412
2. Brownlee M. Biochemistry and molecular cell biology of diabetic complications. Nature 414 (2001) 813-820
3. Griesmacher A., Kindhauser M., Andert S.E., et al. Enhanced serum levels of thiobarbituric-acid-reactive substances in diabetes mellitus. Am J Med 98 (1995) 469-475
4. Dandona P., Thusu K., Cook S., et al. Oxidative damage to DNA in diabetes mellitus. Lancet 347 (1996) 444-445
5. Hunt J.V., Dean R.T., and Wolff S.P. Hydroxyl radical production and autoxidative glycosylation. Glucose autoxidation as the cause of protein damage in the experimental glycation model of diabetes mellitus and ageing. Biochem J 256 (1988) 205-212
6. Mullarkey C., Edelstein D., and Brownlee M. Free radical generation by early glycation products: a mechanism for accelerated atherogenesis in diabetes. Biochem Biophys Res Commun 173 (1990) 932-939
7. Hiramatsu K., and Arimori S. Increased superoxide production by mononuclear cells of patients with hypertriglyceridemia and diabetes. Diabetes 37 (1988) 832-837
8. Salas A., Panes J., Elizalde J.I., Granger D.N., and Pique J.M. Reperfusion-induced oxidative stress in diabetes: cellular and enzymatic sources. J Leukoc Biol 66 (1999) 59-66
9. Nishikawa T., Edelstein D., Du X.L., et al. Normalizing mitochondrial superoxide production blocks three pathways of hyperglycaemic damage. Nature 404 (2000) 787-790
10. Sulieman M., Asleh R., Cabantchik Z.I., et al. Serum chelatable redox-active iron is an independent predictor of mortality after myocardial infarction in individuals with diabetes. Diabetes Care 27 (2004) 2730-2732
11. Phelps G., Chapman I., Hall P., Braund W., and Mackinnon M. Prevalence of genetic haemochromatosis among diabetic patients. Lancet 2 (1989) 233-234
12. Tuomainen T.P., Nyyssonen K., Salonen R., et al. Body iron stores are associated with serum insulin and blood glucose concentrations. Population study in 1013 eastern Finnish men. Diabetes Care 20 (1997) 426-428
13. Ford E.S., and Cogswell M.E. Diabetes and serum ferritin concentration among U.S. adults. Diabetes Care 22 (1999) 1978-1983
14. De Block C.E., Van Campenhout C.M., De Leeuw I.H., et al. Soluble transferrin receptor level: a new marker of iron deficiency anemia, a common manifestation of gastric autoimmunity in type 1 diabetes. Diabetes Care 23 (2000) 1384-1388
15. Telci A., Cakatay U., Kayali R., et al. Oxidative protein damage in plasma of type 2 diabetic patients. Horm Metab Res 32 (2000) 40-43
16. Van Campenhout A., Van Campenhout C.M., Lagrou A.R., and Manuel-y-Keenoy B. Transferrin modifications and lipid peroxidation: implications in diabetes mellitus. Free Radic Res 37 (2003) 1069-1077
17. 3+ isoforms of transferrin. Clin Chem 50 (2004) 1640-1649
18. Gutteridge J.M., Rowley D.A., and Halliwell B. Superoxide-dependent formation of hydroxyl radicals in the presence of iron salts. Detection of 'free' iron in biological systems by using bleomycin-dependent degradation of DNA. Biochem J 199 (1981) 263-265
19. Potter B.J., Chapman R.W., Nunes R.M., Sorrentino D., and Sherlock S. Transferrin metabolism in alcoholic liver disease. Hepatology 5 (1985) 714-721
20. Johnson R.N., Metcalf P.A., and Baker J.R. Fructosamine: a new approach to the estimation of serum glycosylprotein. An index of diabetic control. Clin Chim Acta 127 (1983) 87-95
21. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72 (1976) 248-254
22. Baker J.R., O'Connor J.P., Metcalf P.A., Lawson M.R., and Johnson R.N. Clinical usefulness of estimation of serum fructosamine concentration as a screening test for diabetes mellitus. Br Med J (Clin Res Ed) 287 (1983) 863-867
23. Kennedy L., Mehl T.D., Riley W.J., and Merimee T.J. Non-enzymatically glycosylated serum protein in diabetes mellitus: an index of short-term glycaemia. Diabetologia 21 (1981) 94-98
24. Austin G.E., Mullins R.H., and Morin L.G. Non-enzymic glycation of individual plasma proteins in normoglycemic and hyperglycemic patients. Clin Chem 33 (1987) 2220-2224
25. Peters T. Metabolism: albumin in the body. All about Albumin: Biochemistry, Genetics, and Medical Applications (1996), Academic Press Limited, London 188-250
26. Zoppi F., Mosca A., Granata S., and Montalbetti N. Glycated proteins in serum-effect of their relative proportions on their alkaline reducing activity in the fructosamine test. Clin Chem 33 (1987) 1895-1897
27. Armbruster D.A. Fructosamine: structure, analysis, and clinical usefulness. Clin Chem 33 (1987) 2153-2163
28. Lloyd D., and Marples J. Simple colorimetry of glycated serum-protein in a centrifugal analyzer. Clin Chem 30 (1984) 1686-1688
29. Baker J.R., Metcalf P.A., Johnson R.N., Newman D., and Rietz P. Use of protein-based standards in automated colorimetric determinations of fructosamine in serum. Clin Chem 31 (1985) 1550-1554
30. Monnier V.M., Vishwanath V., Frank K.E., Elmets C.A., Dauchot P., and Kohn R.R. Relation between complications of type I diabetes mellitus and collagen-linked fluorescence. N Engl J Med 314 (1986) 403-408
31. Dolhofer R., and Wieland O.H. Preparation and biological properties of glycosylated insulin. FEBS Lett 100 (1979) 133-136
32. Brownlee M., Vlassara H., and Cerami A. Non-enzymatic glycosylation reduces the susceptibility of fibrin to degradation by plasmin. Diabetes 32 (1983) 680-684
33. Brownlee M., Vlassara H., and Cerami A. Inhibition of heparin-catalyzed human antithrombin Iii activity by nonenzymatic glycosylation-possible role in fibrin deposition in diabetes. Diabetes 33 (1984) 532-535
34. Kennedy D.M., Skillen A.W., and Self C.H. Glycation of monoclonal-antibodies impairs their ability to bind antigen. Clin Exp Immunol 98 (1994) 245-251
35. Kar M., and Chakraborti A.S. Release of iron from haemoglobin-a possible source of free radicals in diabetes mellitus. Indian J Exp Biol 37 (1999) 190-192
36. Cussimanio B.L., Booth A.A., Todd P., Hudson B.G., and Khalifah R.G. Unusual susceptibility of heme proteins to damage by glucose during non-enzymatic glycation. Biophys Chemist 105 (2003) 743-755
37. Roy A., Sen S., and Chakraborti A.S. In vitro nonenzymatic glycation enhances the role of myoglobin as a source of oxidative stress. Free Radic Res 38 (2004) 139-146
38. Sen S., Kar M., Roy A., and Chakraborti A.S. Effect of nonenzymatic glycation on functional and structural properties of hemoglobin. Biophys Chemist 113 (2005) 289-298
39. Inouye M., Mio T., and Sumino K. Glycated hemoglobin and lipid peroxidation in erythrocytes of diabetic patients. Metabolism 48 (1999) 205-209
40. Kemp S.F., Creech R.H., and Horn T.R. Glycosylated albumin and transferrin: short-term markers of blood glucose control. J Pediatr 105 (1984) 394-398
41. Schleicher E., and Wieland O.H. Protein glycation: measurement and clinical relevance. J Clin Chem Clin Biochem 27 (1989) 577-587
42. Jaleel A., Halvatsiotis P., Williamson B., Juhasz P., Martin S., and Nair K.S. Identification of Amadori-modified plasma proteins in type 2 diabetes and the effect of short-term intensive insulin treatment. Diabetes Care 28 (2005) 645-652
43. Memisogullari R., and Bakan E. Levels of ceruloplasmin, transferrin, and lipid peroxidation in the serum of patients with Type 2 diabetes mellitus. J Diabetes Its Complicat 18 (2004) 193-197
44. Jarnum S., and Lassen N.A. Albumin and transferrin metabolism in infectious and toxic diseases. Scand J Clin Lab Invest 13 (1961) 357-368
45. Odonnell M.J., Martin P., Florkowski C.M., et al. Urinary transferrin excretion in type-1 (insulin-dependent) diabetes-mellitus. Diabet Med 8 (1991) 657-661
46. Cheung C.K., Cockram C.S., Yeung V.T.F., and Swaminathan R. Urinary-excretion of transferrin by non-insulin-dependent diabetics-a marker for early complications. Clin Chem 35 (1989) 1672-1674
47. McCormick C.P., Konen J.C., and Shihabi Z.K. Microtransferrinuria and microalbuminuria: I. In the diabetic human. Clin Physiol Biochem 8 (1990) 53-58
48. Implications of the diabetes control and complications trial. Diabetes Care 26 Suppl 1 (2003) S25-S27
49. Fujimoto S., Kawakami N., and Ohara A. Nonenzymatic glycation of transferrin: decrease of iron-binding capacity and increase of oxygen radical production. Biol Pharm Bull 18 (1995) 396-400
50. Esposito B.P., Breuer W., Slotki I., and Cabantchik Z.I. Labile iron in parenteral iron formulations and its potential for generating plasma nontransferrin-bound iron in dialysis patients. Eur J Clin Invest 32 Suppl 1 (2002) 42-49
51. Esposito B.P., Breuer W., Sirankapracha P., Pootrakul P., Hershko C., and Cabantchik Z.I. Labile plasma iron in iron overload: redox activity and susceptibility to chelation. Blood 102 (2003) 2670-2677