Effect of different glycation agents on Cu(II) binding to human serum albumin, studied by liquid chromatography, nitrogen microwave-plasma atomic-emission spectrometry, inductively-coupled-plasma mass spectrometry, and high-resolution molecular-mass spectrometry

Analytical and Bioanalytical Chemistry

Volumn 407, Issue 4, 2015, Pages 1149-1157

  Corrales Escobosa, Alma Rosa ^a   Wrobel, Katarzyna ^a   Yanez Barrientos, Eunice ^a   Jaramillo Ortiz, Sarahi ^a   Ramirez Segovia, Alejandra Sarahi ^a   Wrobel, Kazimierz ^a  

^a UNIVERSITY OF GUANAJUATO   (Mexico)

Author keywords

Copper; Glycation; Human serum albumin; Molecular mass spectrometry; Nitrogen microwave plasma atomic emission spectrometry; Size exclusion chromatography

Indexed keywords

ATOMS; BINDING SITES; BODY FLUIDS; CHROMATOGRAPHY; COPPER; ELECTROSPRAY IONIZATION; GLYCOSYLATION; INDUCTIVELY COUPLED PLASMA MASS SPECTROMETRY; IONIZATION OF LIQUIDS; LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; MICROWAVES; MOLECULAR MASS; NITROGEN; NITROGEN PLASMA; PROTEINS; SPECTROMETRY;

CHROMATOGRAPHIC SEPARATIONS; DETECTION AND IDENTIFICATIONS; GLYCATION; HIGH-RESOLUTION TANDEM MASS SPECTROMETRIES; HUMAN SERUM ALBUMINS; MICROWAVE PLASMA; QUADRUPOLE TIME-OF-FLIGHT TANDEM MASS SPECTROMETRIES; REVERSED PHASE LIQUID-CHROMATOGRAPHY;

SIZE EXCLUSION CHROMATOGRAPHY;

COPPER SULFATE; GLUCOSE; GLYOXAL; GLYOXYLIC ACID; GLYOXYLIC ACID DERIVATIVE; METHYLGLYOXAL; PROTEIN BINDING; SERUM ALBUMIN;

ATOMIC ABSORPTION SPECTROMETRY; BINDING SITE; CHEMISTRY; ELECTROSPRAY MASS SPECTROMETRY; GLYCOSYLATION; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HUMAN; PROTEIN TERTIARY STRUCTURE; REVERSED PHASE LIQUID CHROMATOGRAPHY; SIZE EXCLUSION CHROMATOGRAPHY; TANDEM MASS SPECTROMETRY;

BINDING SITES; CHROMATOGRAPHY, GEL; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CHROMATOGRAPHY, REVERSE-PHASE; COPPER SULFATE; GLUCOSE; GLYCOSYLATION; GLYOXAL; GLYOXYLATES; HUMANS; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; PYRUVALDEHYDE; SERUM ALBUMIN; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION; SPECTROPHOTOMETRY, ATOMIC; TANDEM MASS SPECTROMETRY;

EID: 84938229365     PISSN: 16182642     EISSN: 16182650     Source Type: Journal    
DOI: 10.1007/s00216-014-8335-1     Document Type: Article

References (39)

1. Cooper GJ (2012) Selective divalent copper chelation for the treatment of diabetes mellitus. Curr Med Chem 19:2828-2860
2. Rodriguez Flores C, Preciado Puga M, Wrobel K, Garay Sevilla ME, Wrobek K (2011) Trace element status in diabetes mellitus 2: possible role of the interaction between molybdenum and copper in the progress of typical complications. Diabetes Res Clin Pract 91:333-341
3. Valko M, Morris H, Cronin MT (2005) Metals, toxicity and oxidative stress. Curr Med Chem 12:1161-1208
4. Meyer JA, Spence DM (2009) A perspective on the role of metals in diabetes: past findings and possible future directions. Metallomics 1:32-49
5. Tanaka A, Kaneto H, Miyatsuka T, Yamamoto K, Yoshiuchi K et al (2009) Role of copper ion in the pathogenesis of type 2 diabetes. Endocr J 56:699-706
6. Kozlowski H, Janicka-Klos A, Brasun J, Gaggelli E, Valensinc D et al (2009) Copper, iron, and zinc ions homeostasis and their role in neurodegenerative disorders (metal uptake, transport, distribution and regulation). Coord Chem Rev 253:2665-2685
7. Taverna M, Marie AL, Mira JP, Guidet B (2013) Specific antioxidant properties of human serum albumin. Ann Intensive Care 3:1-7
8. Argirova MD, Ortwerth BJ (2003) Activation of protein-bound copper ions during early glycation: study on two proteins. Arch Biochem Biophys 420:176-184
9. Roche M, Rondeau P, Singh NR, Tarnus E, Bourdon E (2008) The antioxidant properties of serum albumin. FEBS Lett 582:1783-1787
10. Bal W, Sokołowska M, Kurowska E, Faller P (2013) Binding of transition metal ions to albumin: sites, affinities and rates. Biochim Biophys Acta 1830:5444-5455
11. Rondeau P, Singh NR, Caillens H, Tallet F, Bourdon E (2008) Oxidative stresses induced by glycoxidized human or bovine serum albumin on human monocytes. Free Radic Biol Med 45:799-812
12. Guerin-Dubourg A, Catan A, Bourdon E, Rondeau P (2012) Structural modifications of human albumin in diabetes. Diabetes Metab 38:171-178
13. Zhang S, Liu H, Amarsingh GV, Cheung CCH, Hogl S et al (2014) Diabetic cardiomyopathy is associated with defective myocellular copper regulation and both defects are rectified by divalent copper chelation. Cardiovasc Diabetol 13:100-118
14. Baraka-Vidot J, Navarra G, Leone M, Bourdon E, Militello V et al (2014) Deciphering metal-induced oxidative damages on glycated albumin structure and function. Biochim Biophys Acta 1840:1712-1724
15. Bettmer J, Bayon MM, Encinar JR, Sanchez MLF, de la Campa MDF et al (2009) The emerging role of ICP-MS in proteomic analysis. J Proteome 72:989-1005
16. Manley SA, Byrns S, Lyon AW, Brown P, Gailer J (2009) Simultaneous Cu-, Fe-, and Zn-specific detection of metalloproteins contained in rabbit plasma by size-exclusion chromatography-inductively coupled plasma atomic emission spectroscopy. J Biol Inorg Chem 14:61-74
17. Jin Q, Zhu C, Borer MW, Hieftje GM (1991) A microwave plasma torch assembly for atomic emission spectrometry. Spectrochim Acta B 46:417-430
18. Sadi BB, Wrobel K, Kannamkumarath SS, Castillo JR, Caruso JA (2002) SEC-ICP-MS studies for elements binding to different molecular weight fractions of humic substances in compost extract obtained from urban solid waste. J Environ Monit 4:1010-1016
19. El Balkhi S, Poupon JI, Trocello JM, Massicot F, Woimant F et al (2010) Human plasma copper proteins speciation by size exclusion chromatography coupled to inductively coupled plasma mass spectrometry. Solutions for columns calibration by sulfur detection. Anal Chem 82:6904-6910
20. Cabrera A, Alonzo E, Sauble E, Chu YL, Nguyen D et al (2008) Copper binding components of blood plasma and organs, and their responses to influx of large doses of 65Cu, in the mouse. Biometals 21:525-543
21. Lopez-Avila V, Sharpe O, Robinson WH (2006) Determination of ceruloplasmin in human serum by SEC-ICPMS. Anal Bioanal Chem 386:180-187
22. Wang M, Feng W, Lu W, Li B, Wang B et al (2007) Quantitative analysis of proteins via sulfur determination by HPLC coupled to isotope dilution ICPMS with a hexapole collision cell. Anal Chem 79:9128-9134
23. Eaton JW, Qian M (2002) Interactions of copper with glycated proteins: possible involvement in the etiology of diabetic neuropathy. Mol Cell Biochem 234(235):135-142
24. Khan MW, Rasheed Z, Khan WA, Ali R (2007) Biochemical, biophysical, and thermodynamic analysis of in vitro glycated human serum albumin. Biochemistry (Mosc) 72:146-152
25. Qian Y, Zheng Y, Abraham L, Ramos KS, Tiffany-Castiglioni E (2005) Differential profiles of copper-induced ROS generation in human neuroblastoma and astrocytoma cells. Brain Res Mol Brain Res 134:323-332
26. Thornalley PJ (2005) Dicarbonyl intermediates in the Maillard reaction. Ann N Y Acad Sci 1043:111-117
27. Rondeau P, Bourdon E (2011) The glycation of albumin: Structural and functional impacts. Biochimie 93:645-658
28. Polec-Pawlak K, Ruzik R, Lipiec E (2007) Investigation of Cd(II), Pb(II) and Cu(I) complexation by glutathione and its component amino acids by ESI-MS and size exclusion chromatography coupled to ICP-MS and ESI-MS. Talanta 72:1564-1572
29. Masouka J, Hegenauer J, Van Dyke BR, Saltman P (1992) Intrinsic stoichiometric equilibrium constants for the binding of zinc(II) and copper(II) to the high affinity site of serum albumin. J Biol Chem 268:21533-21537
30. da Silveira VC, Caramori GF, Abbott MP, Goncalves MB, Petrilli HM et al (2007) Oxindole-Schiff base copper(II) complexes interacions with human serum albumin: spectroscopic, oxidative damage, and computational studies. J Inorg Biochem 103:1331-1341
31. Trapaidze A, Hureau C, Bal W, Winterhalter M, Faller P (2012) Thermodynamic study of Cu2+ binding to the DAHK and GHK peptides by isothermal titration calorimetry (ITC) with the weaker competitor glycine. J Biol Inorg Chem 17:37-47
32. (2012 ICH) ICH Harmonized Tripartite Guideline. Validation of analytical procedures: text and methodology (Q2/R1). http://www.ish.org/fileadmin/Public-Web-Site/ICH-Products/Guidelines/Quality/Q2-R1/Step4/Q2-R1-Guideline.pdf
33. Anguizola J, Matzuda R, Barnaby OS, Hoy KS, Wa C et al (2013) Review: glycation of human serum albumin. Clin Chim Acta 425:64-76
34. Schmitt A, Gasic-Milenkovic J, Schmitt J (2005) Characterization of advanced glycation end products: mass changes in correlation to side chain modifications. Anal Biochem 346:101-106
35. Oettl K, Stauber RE (2007) Physiological and pathological changes in the redox state of human serum albumin critically influence its binding properties. Br J Pharmacol 151:580-590
36. Frolov A, Hoffmann R (2010) Identification and relative quantification of specific glycation sites in human serum albumin. Anal Bioanal Chem 379:2349-2356
37. Barnaby OS, Cerny RL, Clarke W, Hage DS (2011) Comparison of modification sites formed on human serum albumin at various stages of glycation. Clin Chim Acta 412:277-285
38. Hureau C, Eury H, Guillot R, Bijani C, Sayen S et al (2011) X-ray and solution structures of Cu(II) GHK and Cu(II) DAHK complexes: influence on their redox properties. Chem Eur J 17:10151-10160
39. Lapolla A, Fedele D, Reitano R, Arico NC, Seraglia R et al (2004) Enzymatic digestion and mass spectroemtry in the study of advanced glycation end products/peptides. J Am Soc Mass Spectrom 15:496-509