Physico-Chemical Changes of Human Serum Albumin During in Vivo and in Vitro Glycation Processes

N. Sattarahmady(1*), A.A. Moosavi-Movahedi(2), M. Habibi-Rezaei(3), H. Heli(4)

(1) Department of Biochemistry, Shiraz University of Medical Sciences, Shiraz, Iran., Iran, Islamic Republic of
(2) Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran., Iran, Islamic Republic of
(3) School of Biology, College of Sceince, University of Tehran, Tehran, Iran., Iran, Islamic Republic of
(4) Department of chemistry, Islamic Azad University, Fars Science and Research Branch, Marvdasht, Iran., Iran, Islamic Republic of
(*) Corresponding author

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Glycation, a post-translational modifications, includes the arrangement of proteins with chemically reversible early glycation products, Schiff bases and Amadori adducts. These early products endure slow and complex rearrangements to create advanced glycation end-products (AGEs) that involved in diabetic complications. Here, physico-chamical characteristics of in vitro glycated human serum albumin (HSA) during 14 and 28 days incubation at the presence of glucose inquire with that happened in human serum. The formation of Amadori products, AGE-specific fluorescence intensity, extent of lysine residue modification and the changes in the content of α-helices, and also surface tension value in HSA are all in similar manners in both conditions. It was observed, however, that arginine residues were modified only under physiological conditions (in vivo), and did not occur in vitro. This difference was related to the presence of 3-deoxyglucosone, a 1,2-dicarbonyl compound derived from glucose under physiological conditions. Therefore, the biophysical studies on the HSA glycation process in vitro are credible
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Human Serum Albumin; Glycation; Diabetic Individual; Arginine Residue

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R.G. Khalifah, J.W. Baynes, B.G. Hudson, Amadorins: novel post-Amadori inhibitors of advanced glycation reactions, Biochem.Biophys.Res.Commun.Volume 257,1999, Pages 251-258.

A.Lapolla, P. Traldi, D. Fedele, Importance of measuring products of non-enzymatic glycation of proteins, Clin. Biochem. Volume 38, 2005, Pages 103-115.

N. Shaklai, R.L. Garlick, H.F. Bunn, Nonenzymatic glycosylation of human serum albumin alters its conformation and function, J. Biol. Chem. Volume 259, 1984, Pages 3812-3817.

P.A. Voziyan, R.G. Khalifah, C. Thibaudeau, A. Yildiz, J. Jacob, A.S. Serianni, B.G. Hudson, Modification of proteins In Vitro by physiological levels of glucose, J. Biol. Chem. Volume 278, 2003, Pages 46616-46624.

B.L. Cussimanio, A.A. Booth, P. Todd, B.G. Hudson, R.G. Khalifah, Unusual susceptibility of heme proteins to damage by glucose during non-enzymatic glycation, Biophys. Chem. Volume 105, 2003, Pages 743-755.

B. Trueb, C.G. Holenstein, R.W. Fischer, K.H. Winterhalter, Nonenzymatic glycosylation of proteins, J. Biol. Chem. Volume 255, 1980, Pages 6717-6720.

X.M. He, D.C. Carter, Atomic structure and chemistry of human serum albumin, Nature Volume 358, 1992, Pages 209-215.

D.C. Carter, X.M. He, S.H. Munson, P.D. Twigg, K.M. Gernert, M.B. Broom, T.Y. Miller, Three-dimensional structure of human serum albumin, Science, Volume 244, 1989, Pages 1195-1198.

E. Bourdon, N. Loreau, D. Blache, Glucose and free radicals impair the antioxidant properties of serum albumin, FASEB J., Volume 13, 1999, Pages 233-243.

N. Iberg, R. Fluckiger, Nonenzymatic glycosylation of albumin in vitro (Identification of multiple glycosylated sites), J. Biol. Chem. Volume 261, 1986, Pages 13542-13545.

P.J. Coussons, J. Jacoby, A. McKay, S.M. Kelly, N.C. Price, J. V. Hunt, Glucose modification of human serum albumin: a structural study, Free Radical Biol. Med. Volume 22, 1997, Pages 1217-1227.

S.D. Sharma, B.N. Pandey, K.P. Mishra, S. Sivakami, Amadori product and AGE formation during nonenzymatic glycosylation of bovine serum albumin In Vitro, J. Biochem. Mol. Biol. Biophys. Volume 6, 2002, Pages 233-242.

N. Shaklai, R.L. Garlick, H.F. Bunn, Nonenzymatic glycosylation of human serum albumin alters its conformation and function, J. Biol. Chem. Volume 259, 1984, Pages 3812-3817.

D.M. Mendez, R.A. Jensen, L.A. McElroy, J.M. Pena, R.M. Esquerra, The effect of non-enzymatic glycation on the unfolding of human serum albumin, Arch. Biochem. Biophys. Volume 444, 2005, Pages 92-99.

H. Zoellner, Y.H. Hou, T. Hochgrebe, A. Poljak, M.W. Duncan, J. Golding, T. Henderson, G. Lynch, Fluorometric and mass spectrometric analysis of nonenzymatic glycosylated albumin, Biochem. Biophys. Res. Commun. Volume 284, 2001, Pages 83-89.

B. Bouma, L.M.J. Kroon-Batenburg, Y.P. Wu, B. Brunjes, G. Posthuma, O. Kranenburg, P.G. Groot, E.E. Voest, M.F.B.G. Gebbink, Glycation induces formation of amyloid cross-β structure in albumin, J. Biol. Chem. Volume 278, 2003, Pages 41810-41819.

M.E. Westwood, P.J. Thornalley, Molecular characteristics of methylglyoxal-modified bovine and human serum albumins. Comparison with glucose-derived advanced glycation end product-modified serum albumins, J. Protein Chem. Volume 4, 1995, Pages 359-372.

K.M. Biemel, D.A. Friedl, M.O. Lederer, Identification and quantification of major Maillard cross-links in human serum albumin and lens protein, J. Biol. Chem. Volume 277, 2002, Pages 24907-24915.

N. Sattarahmady, A.A. Moosavi-Movahedi, F. Ahmad, G.H. Hakimelahi, M. Habibi-Rezaei, A.A. Saboury, N. Sheibani, Formation of the Molten Globule-Like State during Prolonged Glycation of Human Serum Albumin, Biochim. Biophys. Acta Volume 1770, 2007, Pages 933-942.

N. Sattarahmady, F. Khodagholi, A.A. Moosavi-Movahedi, H. Heli, G.H. Hakimelahi, Alginate as antiglycating agent for human serum albumin, Int. J. Biol. Macromol. Volume 41, 2007, Pages 180-184.

N.Sattarahmady,A.A.Moosavi-Movahedi,M.Habibi-Rezaei, S.Ahmadian,A.A.Saboury,H.Heli,N.Sheibani,Detergency effect of nanofibrillar amyloid formation on glycation of human serum albumin, Carbohydrate Res.Volume 343, 2008, Pages 2229-2234.

Z.Y. Ma, Y.P. Guan, H.Z. Liu, Affnity adsorption of albumin on Cibacron Blue F3GA-coupled non-porous micrometer-sized magnetic polymer microspheres, React. Funct. Polym. Volume 66, 2006, Pages 618-624.

D.J. Ledden, R.C. Feldhoff, S.K. Chan, Characterization of fragments of human albumin purified by Cibacron Blue F3GA affinity chromatography, Biochem. J. Volume 205, 1982, Pages 331-337.

U.K. Laemmli, Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature, Volume 227, 1970, Pages 680-685.

C. Wilson, Staining of proteins on gels: comparison of dyes and procedures, Methods Enzymol, Volume 91, 1983, Pages 236-247.

A.Schmitt,J.Schmitt,G.Munch,J.Gasic-Milencovic,Characteri-zation of advanced glycation end products for biochemical studies: side chain modifications and fluorescence characteristics, Anal. Biochem. Volume 338, 2005, Pages 201-215.


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