Reactivity of 6-phosphogluconolactone with hydroxylamine: The possible involvement of glucose-6-phosphate dehydrogenase in endogenous glycation reactions

Chemico-Biological Interactions

Volumn 113, Issue 3, 1998, Pages 205-216

  Rakitzis, Emmanuel T ^a   Papandreou, Photini ^b  

^a UNIVERSITY OF ATHENS MEDICAL SCHOOL   (Greece)

^b PENTELI CHILDREN S HOSPITAL   (Greece)

Author keywords

6 phosphogluconolactone; Endogenous glycation reactions; Glucose 6 phosphate dehydrogenase; Hydroxylamine; Lactone

Indexed keywords

6 PHOSPHOGLUCONOLACTONE; CARBOXYLIC ACID SALT; GLUCOSE 6 PHOSPHATE DEHYDROGENASE; HYDROXYLAMINE; UNCLASSIFIED DRUG;

ARTICLE; CHEMICAL REACTION KINETICS; GLYCATION; REACTION TIME;

FERRIC COMPOUNDS; GLUCONATES; GLUCOSE; GLUCOSEPHOSPHATE DEHYDROGENASE; HYDROXIDES; HYDROXYLAMINE; KINETICS; LACTONES; SOLUTIONS;

EID: 0031780918     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0009-2797(98)00026-X     Document Type: Article

References (45)

1. 1c. Biochemistry. 5:1966;2489-2503.
2. Beswick H.T., Harding J.J. Aldehydes or dicarbonyls in non-enzymic glycation of proteins. Biochem. J. 226:1985;385-389.
3. Paul R.G., Bailey A.J. Glycation of collagen: the basis of its central role in the late complications of ageing and diabetes. Int. J. Biochem. Cell Biol. 28:1996;1297-1310.
4. Hoshi A., Takahashi M., Fujii J., Myint T., Kaneto H., Suzuki K., Yamasaki Y., Kamada T., Taniguchi N. Glycation and inactivation of sorbitol dehydrogenase in normal and diabetic rats. Biochem. J. 318:1996;119-123.
5. Rao G.N., Cottier E. Aspirin prevents the nonenzymic glycosylation and carbamylation of human lens crystallins in vitro. Relevance to cataract. Biochem. Biophys. Res. Commun. 151:1988;991-996.
6. Flückiger R., Harmon W., Meier W., Loo S., Gabbay K.H. Hemoglobin carbamylation in ureamia. New Engl. J. Med. 304:1981;823-827.
7. Beswick H.T., Harding J.J. Conformational changes induced in bovine lens α crystallin by carbamylation. Relevance to cataract. Biochem. J. 223:1984;221-227.
8. Baer R.W. Myocardial oxygen transport during leftward shifts of the oxygen dissociation curve by carbamylation and hypothermia. Adv. Exp. Med. Biol. 248:1989;325-333.
9. Horkko S., Savolainen M.J., Kervinen K., Kesaniemi Y.A. Carbamylation-induced alterations in low density lipoprotein metabolism. Kidney Int. 41:1992;1175-1181.
10. Ationu A. Carbamylation and glycosylation of haemoglobin in vitro: Effects of cyanate and glucose. Med. Lab. Sci. 49:1992;34-37.
11. Liu M., Subbaiah P.V. Hydrolysis and transesterification of platelet-activating factor by lecithin-cholesterol acyltransferase. Proc. Natl. Acad. Sci. USA. 91:1994;6035-6039.
12. 1: Viscosity effects indicate that the rate-limiting step of GpN transesterification depends on the nature of N. Biochemistry. 30:1991;8661-8665.
13. Pincard R.N., Hawkins D., Farr R.S. In vitro acetylation of plasma proteins, enzymes and DNA by Aspirin. Nature. 219:1968;68-69.
14. D. Hawkins, R.N. Pinkard, R.S. Farr, Acetylation of human serum albumin by acetylsalicylic acid, Science 160 (1968) 780-781.
15. Barton P., Laws A.P., Page M.I. Structure-activity relationships in the esterase catalysed hydrolysis and transesterification of esters and lactones. J. Chem. Soc. Perkin Trans. 2:1994;2021-2029.
16. Dickens F., Jones H.E.H. Carcinogenic activity of a series of reactive lactones and related substances. Br. J. Cancer. 15:1961;85-100.
17. Dickens F., Cooke J. Rates of hydrolysis and interaction with cysteine of carcinogenic lactones and related substances. Br. J. Cancer. 19:1965;404-410.
18. Roberts J.J., Warwick G.P. The reaction of β-propionolactone with guanosine, deoxyguanylic acid and RNA. Biochem. Pharmacol. 12:1963;1441-1442.
19. Taubman M.A., Atassi M.Z. Reaction of β-propionolactone with amino acids and its specificity for methionine. Biochem. J. 106:1968;829-834.
20. Dijkstra J. In vitro reaction of β-propionolactone and γ-butyrolactone with glutathione and cysteine. Chem.-Biol. Interact. 10:1975;115-121.
21. Wounarowska B., Wikiel H., Sharma M., Carpenter N., Fleet W.J., Bernacki R. Inhibition of human ovarian carcinoma cell and hexosaminidase-mediated degradation of extracellular matrix by sugar analogs. Anticancer Res. 12:1992;161-166.
22. Hestrin S. The reaction of acetylcholine and other carboxylic acid derivatives with hydroxylamine, and its analytical application. J. Biol. Chem. 180:1949;249-261.
23. Horecker B.L., Smyrniotis P.Z. Reversibility of glucose-6-phosphate oxidation. Biochim. Biophys. Acta. 12:1953;98-102.
24. Brodie A.F., Lipmann F. Identification of a gluconolactonase. J. Biol. Chem. 212:1955;677-685.
25. Lipmann F., Tuttle L.C. A specific micromethod for the determinations of acyl phosphates. J. Biol. Chem. 159:1945;21-28.
26. E.T. Rakitzis, Purification and Properties of Human Erythrocyte Acyl Phosphatase, Dissertation for the Ph.D. Degree, University of Texas Medical Branch, Galveston, Texas (1969).
27. A.A. Frost, R.G. Pearson, Kinetics and Mechanism, Wiley, New York, 1961, pp. 160-165 and 185-189.
28. A. Cornish-Bowden, Principles of Enzyme Kinetics, Buttersworth, London, 1976, pp. 7-9.
29. Rakitzis E.T. Kinetic analysis of chemical and enzymic reactions: an algorithm for the determination of the initial velocity of product formation by the use of a Taylor series in reaction time. J. Theor. Biol. 188:1997;387-389.
30. Rakitzis E.T. Kinetic analysis of biphasic protein modification reactions. J. Math. Biol. 10:1980;79-87.
31. Takahashi T., Mitsumoto M. Transformation and hydrolysis of D-glucono-γ and δ-lactone. Nature. 199:1963;765-767.
32. Lindsay R.M., Smith W., Lee W.K., Dominiczak M.H., Baird J.D. The effect of δ-gluconolactone, an oxidised analogue of glucose, on the nonenzymatic glycation of human and rat haemoglobin. Clin. Chim. Acta. 263:1977;239-247.
33. Van Duuren B.L., Nelson N., Orris L., Palmes E.D., Schmitt F.L. Carcinogenicity of epoxides, lactones and peroxy compounds. J. Nat. Cancer Inst. 31:1963;41-55.
34. Van Duuren B.L., Orris L., Nelson N. Carcinogenicity of epoxides, lactones and peroxy compounds, Part II. J. Nat. Cancer Inst. 35:1965;707-717.
35. Jermyn M.A. Studies on the glucono-δ-lactonase of Pseudomonas fluorescens. Biochem. Biophys. Acta. 37:1960;78-92.
36. Ueberschär K.H., Blachnitzky E.O., Kurz G. Reaction mechanism of D-galactose dehydrogenase from Pseudomonas saccharophila and Pseudomonas fluorescens. Eur. J. Biochem. 48:1974;389-405.
37. Jarori G.K., Maitra P.K. Nature of primary product(s) of D-glucose-6-phosphate dehydrogenase reaction. FEBS Lett. 278:1991;247-251.
38. Thornburn D.R., Kuchel P.W. Regulation of the human erythrocyte hexose monophosphate shunt under conditions of oxidative stress. Eur. J. Biochem. 150:1985;371-386.
39. Rakitzis E.T., Papandreou P. Kinetic analysis of 6-phosphogluconolactone hydrolysis in hemolysates. Biochem. Int. 37:1995;747-755.
40. Beutler E., Kuhl W., Gelbart T. 6-Phosphogluconolactonase deficiency, a hereditary erythrocyte enzyme deficiency: possible interaction with glucose-6-phosphate dehydrogenase deficiency. Proc. Natl. Acad. Sci. USA. 82:1985;3876-3878.
41. Liguri G., Camici G., Manao G., Capuggi G., Nessi P., Modesti A., Ramponi G. A new acylphosphatase isoenzyme from human erythrocytes: Purification, characterization, and primary structure. Biochemistry. 25:1986;8089-8094.
42. Bunn H.F., Higgins P.J. Reaction of monosaccharides with proteins: Possible evolutionary significance. Science. 213:1981;222-224.
43. Chan T.K., Todd D., Wong C.G. Tissue enzyme levels in erythrocyte glucose-6-phosphate dehydrogenase deficiency. J. Lab. Clin. Med. 66:1965;937-942.
44. Dessi S., Batetta B., Cherchi R., Omnis R., Pisano M., Pani P. Hexose monophosphate shunt enzymes in lung tumors from normal and glucose-6-phosphate dehydrogenase deficient subjects. Oncology. 45:1988;287-291.
45. Cocco P., Dessi S., Avataneo G., Picchiri G., Heinemann E. Glucose-6-phosphate dehydrogenase deficiency and cancer in a Sardinian male population: A case-control study. Carcinogenesis. 10:1989;813-816.