Formation of the molten globule-like state during prolonged glycation of human serum albumin

Biochimica et Biophysica Acta - General Subjects

Volumn 1770, Issue 6, 2007, Pages 933-942

  Sattarahmady, Naghmeh ^a   Moosavi Movahedi, Ali A ^a   Ahmad, Faizan ^b   Hakimelahi, Gholam H ^c   Habibi Rezaei, Mehran ^a   Saboury, Ali A ^a   Sheibani, Nader ^d  

^a UNIVERSITY OF TEHRAN   (Iran)

^b JAMIA MILLIA ISLAMIA CENTRAL UNIVERSITY   (India)

^c TaiGen Biotechnology   (Taiwan)

^d UNIVERSITY OF WISCONSIN SCHOOL OF MEDICINE AND PUBLIC HEALTH   (United States)

Author keywords

AGE; Diabetes; Glycation; Human serum albumin; Molten globule

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; ARGININE; BORONIC ACID DERIVATIVE; FLUORESCAMINE; GLUCOSE; HUMAN SERUM ALBUMIN; LYSINE; PHENANTHRENEQUINONE; TETRAZOLIUM;

AMADORI REARRANGEMENT; ARTICLE; AUTOFLUORESCENCE; CIRCULAR DICHROISM; FLUORESCENCE ANALYSIS; FLUORESCENCE SPECTROSCOPY; GLYCATION; INCUBATION TIME; PRIORITY JOURNAL; PROTEIN METABOLISM; PROTEIN STRUCTURE; VISCOSITY;

CIRCULAR DICHROISM; DIABETES MELLITUS; FLUORESCENCE; GLUCOSE; GLYCOSYLATION; GLYCOSYLATION END PRODUCTS, ADVANCED; HUMANS; MAILLARD REACTION; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; SERUM ALBUMIN;

EID: 34247330205     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2007.02.001     Document Type: Article

References (35)

1. Khalifah R.G., Baynes J.W., and Hudson B.G. Amadorins: novel post-Amadori inhibitors of advanced glycation reactions. Biochem. Biophys. Res. Commun. 257 (1999) 251-258
2. Lapolla A., Traldi P., and Fedele D. Importance of measuring products of non-enzymatic glycation of proteins. Clin. Biochem. 38 (2005) 103-115
3. Shaklai N., Garlick R.L., and Franklin Bunn H. Nonenzymatic glycosylation of human serum albumin alters its conformation and function. J. Biol. Chem. 259 6 (1984) 3812-3817
4. Voziyan P.A., Khalifah R.G., Thibaudeau C., Yildiz A., Jacob J., Serianni A.S., and Hudson B.G. Modification of proteins in vitro by physiological levels of glucose. J. Biol. Chem. 278 47 (2003) 46616-46624
5. 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. Chem. 105 (2003) 743-755
6. Brownlee M. Glycosylation products as toxic mediators of diabetic complications. Annu. Rev. Med. 42 (1991) 159-166
7. Trueb B., Holenstein C.G., Fischer R.W., and Winterhalter K.H. Nonenzymatic glycosylation of proteins. J. Biol. Chem. 255 14 (1980) 6717-6720
8. He X.M., and Carter D.C. Atomic structure and chemistry of human serum albumin. Nature 358 (1992) 209-215
9. Carter D.C., He X.M., Munson S.H., Twigg P.D., Gernert K.M., Broom M.B., and Miller T.Y. Three-dimensional structure of human serum albumin. Science 244 (1989) 1195-1198
10. Bourdon E., Loreau N., and Blache D. Glucose and free radicals impair the antioxidant properties of serum albumin. FASEB J. 13 (1999) 233-243
11. Guthrow C.E., Morris M.A., Day J.F., Thorpe S.R., and Baynes J.W. Enhanced nonenzymatic glycosylation of human serum albumin in diabetes mellitus. Proc. Natl. Acad. Sci. U. S. A. 76 9 (1979) 4258-4261
12. Nakajou K., Watanabe H., Kragh-Hansen U., Maruyama T., and Otagiri M. The effect of glycation on the structure, function and biological fate of human serum albumin as revealed by recombinant mutants. Biochim. Biophys. Acta 1623 (2003) 88-97
13. Christensen H., and Pain R.H. Molten globule intermediates and protein folding. Eur. Biophys. J. 19 (1991) 221-229
14. Ptitsyn O.B. In: Creighton T.E. (Ed). The Molten Globule State in Protein Folding (1992), W.H. Freeman and Company, New York 243-300
15. Ghobadi S., Safarian S., Moosavi-Movahedi A.A., and Ranjbar B. Octyl glucoside induced formation of the molten globule-like state of glutamate dehydrogenase. J. Biochem. 130 (2001) 671-677
16. Moosavi-Movahedi A.A., Chamani J., Goto Y., and Hakimelahi G.H. Formation of the molten globule-like state of cytochrome c induced by n-alkyl sulfates at low concentrations. J. Biochem. 133 (2003) 93-102
17. Davis-Searles P.R., Morar A.S., Saunderes A.J., Erie D.A., and Pielak G.J. Suger-induced molten globule model. Biochemistry 37 (1998) 17048-17053
18. Kamiyama T., Sadahide Y., Nogusa Y., and Gekko K. Polyol-induced molten globule of cytochrome c: an evidence for stabilization by hydrophobic interaction. Biochim. Biophys. Acta 1434 (1999) 44-57
19. Mohamadi-Nejad A., Moosavi-Movahedi A.A., Hakimelahi G.H., and Sheibani N. Thermodynamic analysis of human serum albumin interactions with glucose: insights into the diabetic range of glucose concentration. Int. J. Biochem. Cell Biol. 34 (2002) 1115-1124
20. Mohamadi-Nejad A., Moosavi-Movahedi A.A., Safarian S., Naderi-Manesh M.H., Ranjbar B., Farzami B., Mostafavi H., Larijani M.B., and Hakimelahi G.H. The thermal analysis of nonenzymatic glycosylation of human serum albumin: differential scanning calorimetry and circular dichroism studies. Thermochim. Acta 389 (2002) 141-151
21. Barzegar A., Moosavi-Movahedi A.A., Sattarahmady N., Hosseinpour-Faizi M.A., Aminbakhsh M., Ahmad F., Saboury A.A., Ganjali M.R., and Norouzi P. Spectroscopic studies of the effects of glycation of human serum albumin on L-Trp binding. Protein Pept. Lett. 14 (2007) 13-18
22. Iberg N., and Fluckiger R. Nonenzymatic glycosylation of albumin in vitro (Identification of multiple glycosylated sites). J. Biol. Chem. 261 (1986) 13542-13545
23. Bayness J.W., Thorp S.R., and Murtishaw M.H. Non-enzymatic glycosylation of lysine residues in albumin. Methods Enzymol. 106 (1984) 88-98
24. Schmitt A., Schmitt J., Münch G., and Gasic-Milencovic J. Characterization of advanced glycation end products for biochemical studies: side chain modifications and fluorescence characteristics. Anal. Biochem. 338 (2005) 201-215
25. Matulis D., and Lovrien R. 1-Anilino-8-naphatahalene sulfonate anion-protein binding depends primarily on ion pair formation. Biophys. J. 74 (1998) 422-429
26. Hayashi Y., and Makino M. Fluorometric measurement of glycosylated albumin in human serum. Clin. Chim. Acta 149 (1985) 13-19
27. Westwood M.E., and Thornalley P.J. Molecular characteristics of methylglyoxal-modified bovine and human serum albumins. Comparison with glucose-derived advanced glycation endproduct-modified serum albumins. J. Protein Chem. 14 (1995) 359-372
28. Luik A.I., Naboka Y.N., Mogilevich S.E., Hushcha T.O., and Mischenko N.I. Study of human serum albumin structure by dynamic light scattering: two types of reactions under different pH and interaction with physiologically active compounds. Spectrochim. Acta, Part A 54 (1998) 1503-1507
29. Dutta U., Cohenford M.A., and Dain J.A. Monitoring the effect of glucosamine and glyceraldehyde glycation on the secondary structure of human serum albumin and immunoglobulin G: an analysis based on circular dichroism, thermal melting profiles and UV-fluorescence spectroscopy. Anal. Chim. Acta 558 (2005) 187-194
30. Coussons P.J., Jacoby J., McKay A., Kelly S.M., Price N.C., and Hunt J.V. Glucose modification of human serum albumin: a structural study. Free Radical Biol. Med. 22 (1997) 1217-1228
31. Mendez D.M., Jensen R.A., McElroy L.A., Pena J.M., and Esquerra R.M. The effect of non-enzymatic glycation on the unfolding of human serum albumin. Arch. Biochem. Biophys. 444 (2005) 92-99
32. Chamani J., Moosavi-Movahedi A.A., Rajabi O., Gharanfoli M., Momen-Heravi M., Hakimelahi G.H., Neamati-Baghsiah A., and Varasteh A.R. Cooperative α-helix formation of β-lactoglobulin induced by sodium n-alkyl sulfates. J. Colloid Interface Sci. 293 (2006) 52-60
33. Zoellner H., Hou Y.-H., Hochgrebe T., Poljak A., Duncan M.-W., Golding J., Henderson T., and Lynch G. Fluorometric and mass spectrometric analysis of nonenzymatic glycosylated albumin. Biochem. Biophys. Res. Commun. 284 (2001) 83-89
34. Hipkiss A.R. Accumulation of altered proteins and ageing: causes and effects. Exp. Gerontol. 41 (2006) 464-473
35. Biemel K.M., Friedl D.A., and Lederer M.O. Identification and quantification of major Maillard cross-links in human serum albumin and lens protein. J. Biol. Chem. 287 (2002) 24907-24915