Comparison of antioxidant properties of different therapeutic albumin preparations

Biologicals

Volumn 44, Issue 4, 2016, Pages 226-233

  Plantier, Jean Luc ^a   Duretz, Véronique ^a   Devos, Véronique ^a   Urbain, Rémi ^a   Jorieux, Sylvie ^a  

^a LFB Biotechnologies   (France)

Author keywords

DPPH; Free cysteine; Human albumin; Redox potential; Therapeutic preparation

Indexed keywords

1,1 DIPHENYL 2 PICRYLHYDRAZYL; ALBUMIN; ALBUMIN MICROSPHERE; ALBUMINOID; ALBUNORM; COBALT; CYSTEINE; FREE RADICAL; GLYCOSYLATED ALBUMIN; HUMAN ALBUMIN; HUMAN SERUM ALBUMIN; HYDROXYL RADICAL; PEROXY RADICAL; UNCLASSIFIED DRUG; YDRALBUM; 1,1-DIPHENYL-2-PICRYLHYDRAZYL; ANTIOXIDANT; BIPHENYL DERIVATIVE; PICRIC ACID; SCAVENGER; SERUM ALBUMIN;

ANALYTIC METHOD; ANTIOXIDANT ACTIVITY; ARTICLE; BINDING AFFINITY; DRUG IDENTIFICATION; DRUG STRUCTURE; DRUG SYNTHESIS; ELECTRON TRANSPORT; FLUOROMETRY; GLYCATION; OXIDATION REDUCTION STATE; PRIORITY JOURNAL; SPECTROPHOTOMETRY; STRUCTURE ANALYSIS; ANTAGONISTS AND INHIBITORS; CHEMISTRY; COMPARATIVE STUDY; DRUG EFFECTS; GLYCOSYLATION; HUMAN; METABOLISM; OXIDATION REDUCTION REACTION;

ANTIOXIDANTS; BIPHENYL COMPOUNDS; CYSTEINE; FREE RADICAL SCAVENGERS; FREE RADICALS; GLYCOSYLATION; HUMANS; HYDROXYL RADICAL; OXIDATION-REDUCTION; PICRATES; SERUM ALBUMIN; SPECTROPHOTOMETRY;

EID: 84964870230     PISSN: 10451056     EISSN: 10958320     Source Type: Journal    
DOI: 10.1016/j.biologicals.2016.04.002     Document Type: Article

References (48)

1. [1] Halliwell, B., Biochemistry of oxidative stress. Biochem Soc Trans 35 (2007), 1147–1150.
2. [2] Ames, B.N., Shigenaga, M.K., Hagen, T.M., Oxidants, antioxidants, and the degenerative diseases of aging. Proc Natl Acad Sci U. S. A 90 (1993), 7915–7922.
3. [3] Gutteridge, J.M., Halliwell, B., Comments on review of free radicals in biology and medicine, second edition, by Barry Halliwell and John M. C. Gutteridge. Free Radic Biol Med 12 (1992), 93–95.
4. [4] Bernardi, M., Maggioli, C., Zaccherini, G., Human albumin in the management of complications of liver cirrhosis. Crit Care, 16, 2012, 211.
5. [5] Turell, L., Radi, R., Alvarez, B., The thiol pool in human plasma: the central contribution of albumin to redox processes. Free Radic Biol Med 65 (2013), 244–253.
6. [6] Halliwell, B., Gutteridge, J.M., The antioxidants of human extracellular fluids. Arch Biochem Biophys 280 (1990), 1–8.
7. [7] Roche, M., Rondeau, P., Singh, N.R., Tarnus, E., Bourdon, E., The antioxidant properties of serum albumin. FEBS Lett 582 (2008), 1783–1787.
8. [8] Quinlan, G.J., Martin, G.S., Evans, T.W., Albumin: biochemical properties and therapeutic potential. Hepatology 41 (2005), 1211–1219.
9. [9] Bourdon, E., Loreau, N., Lagrost, L., Blache, D., Differential effects of cysteine and methionine residues in the antioxidant activity of human serum albumin. Free Radic Res 39 (2005), 15–20.
10. [10] Quinlan, G.J., Mumby, S., Martin, G.S., Bernard, G.R., Gutteridge, J.M., Evans, T.W., Albumin influences total plasma antioxidant capacity favorably in patients with acute lung injury. Crit Care Med 32 (2004), 755–759.
11. [11] Kremer, H., Baron-Menguy, C., Tesse, A., Gallois, Y., Mercat, A., Henrion, D., et al. Human serum albumin improves endothelial dysfunction and survival during experimental endotoxemia: concentration-dependent properties. Crit Care Med 39 (2011), 1414–1422.
12. [12] Peters, T., All about albumin. Biochemistry, genetics and medical applications. 2008, Academic Press Publisher, San Diego (CA).
13. [13] Eom, J.E., Lee, E., Jeon, K.H., Sim, J., Suh, M., Jhon, G.J., et al. Development of an albumin copper binding (ACuB) assay to detect ischemia modified albumin. Anal Sci 30 (2014), 985–990.
14. [14] Wu, T.W., Wu, J., Li, R.K., Mickle, D., Carey, D., Albumin-bound bilirubins protect human ventricular myocytes against oxyradical damage. Biochem Cell Biol 69 (1991), 683–688.
15. [15] King, T.P., On the sulfhydryl group of human plasma albumin. J Biol Chem, 236, 1961 Pc5.
16. [16] Era, S., Kuwata, K., Imai, H., Nakamura, K., Hayashi, T., Sogami, M., Age-related change in redox state of human serum albumin. Biochim Biophys Acta 1247 (1995), 12–16.
17. [17] Oettl, K., Stauber, R.E., Physiological and pathological changes in the redox state of human serum albumin critically influence its binding properties. Br J Pharmacol 151 (2007), 580–590.
18. [18] Okazaki, T., Okudaira, N., Ishii, N., Yotsuyanagi, H., Nagai, T., Tokudome, S., et al. Comparison of the antioxidant activity of albumin from various animal species. Zool Sci 25 (2008), 172–177.
19. [19] Bar-Or, D., Bar-Or, R., Rael, L.T., Gardner, D.K., Slone, D.S., Craun, M.L., Heterogeneity and oxidation status of commercial human albumin preparations in clinical use. Crit Care Med 33 (2005), 1638–1641.
20. [20] Kleinova, M., Belgacem, O., Pock, K., Rizzi, A., Buchacher, A., Allmaier, G., Characterization of cysteinylation of pharmaceutical-grade human serum albumin by electrospray ionization mass spectrometry and low-energy collision-induced dissociation tandem mass spectrometry. Rapid Commun Mass Spectrom 19 (2005), 2965–2973.
21. [21] Matejtschuk, P., Dash, C.H., Gascoigne, E.W., Production of human albumin solution: a continually developing colloid. Br J Anaesth 85 (2000), 887–895.
22. [22] Leitch, A., Craig, G., Sadler, P., Human albumin solution resuscitation in severe sepsis and septic shock. JICS 14 (2013), 45–52.
23. [23] Turell, L., Carballal, S., Botti, H., Radi, R., Alvarez, B., Oxidation of the albumin thiol to sulfenic acid and its implications in the intravascular compartment. Braz J Med Biol Res 42 (2009), 305–311.
24. [24] Bar-Or, D., Lau, E., Winkler, J.V., A novel assay for cobalt-albumin binding and its potential as a marker for myocardial ischemia-a preliminary report. J Emerg Med 19 (2000), 311–315.
25. [25] Cao, G., Alessio, H.M., Cutler, R.G., Oxygen-radical absorbance capacity assay for antioxidants. Free Radic Biol Med 14 (1993), 303–311.
26. [26] Lobo, V., Patil, A., Phatak, A., Chandra, N., Free radicals, antioxidants and functional foods: impact on human health. Pharmacogn Rev 4 (2010), 118–126.
27. [27] Brand-Williams, W., Cuvelier, M., Berset, C., Use of a free radical method to evaluate antioxidant activity. Food Sci Technol 28 (1995), 25–30.
28. (2+) binding amino-acid residues of the N-terminus of human albumin. An insight into the mechanism of a new assay for myocardial ischemia. Eur J Biochem 268 (2001), 42–47.
29. [29] Bar-Or, D., Rael, L.T., Bar-Or, R., Slone, D.S., Mains, C.W., Rao, N.K., et al. The formation and rapid clearance of a truncated albumin species in a critically ill patient. Clin Chim Acta 365 (2006), 346–349.
30. [30] Arasteh, A., Farahi, S., Habibi-Rezaei, M., Moosavi-Movahedi, A.A., Glycated albumin: an overview of the in Vitro models of an in Vivo potential disease marker. J Diabetes Metab Disord, 13, 2014, 49.
31. [31] Atmeh, R.F.A.I., Al-Khateeb, M., Albumin aggregates: hydrodynamic shape and physico-chemical properties. Jordan J Chem 2 (2007), 169–182.
32. [32] Lee, E., Eom, J.E., Jeon, K.H., Kim, T.H., Kim, E., Jhon, G.J., et al. Evaluation of albumin structural modifications through cobalt-albumin binding (CAB) assay. J Pharm Biomed Anal 91 (2014), 17–23.
33. [33] Minami, T., Terada, T., Takahashi, T., Arikawa, H., Matsuyama, Y., Kizaki, K., et al. Comparative studies on the heterogeneity of plasma-derived and recombinant human albumins in laboratory use. Int J Biol Macromol 69 (2014), 79–87.
34. [34] Sokolowska, M., Wszelaka-Rylik, M., Poznanski, J., Bal, W., Spectroscopic and thermodynamic determination of three distinct binding sites for Co(II) ions in human serum albumin. J Inorg Biochem 103 (2009), 1005–1013.
35. [35] Dimitrova, A.A., Atanasova, A.M., Georgieva, M.N., Russeva, A.L., Strashimirov, D.S., Baydanoff, S.I., Anti-age antibodies and markers of oxidative stress in spontaneously hypertensive rats at different ages. J Biomed Clin Res 3 (2010), 33–39.
36. [36] Guerin-Dubourg, A., Catan, A., Bourdon, E., Rondeau, P., Structural modifications of human albumin in diabetes. Diabetes Metab 38 (2012), 171–178.
37. [37] Taverna, M., Marie, A.L., Mira, J.P., Guidet, P., Specific antioxidant properties of human serum albumin. Ann Intensive Care, 3, 2013, 4.
38. [38] McCann, K.B., Vucica, Y., Famulari, S., Bertolini, J., Effect of processing methods on colouration of human serum albumin preparations. Biologicals 37 (2009), 32–36.
39. [39] Frei, B., Stocker, R., Ames, B.N., Antioxidant defenses and lipid peroxidation in human blood plasma. Proc Natl Acad Sci U. S. A 85 (1988), 9748–9752.
40. [40] Weisiger, R.A., Ostrow, J.D., Koehler, R.K., Webster, C.C., Mukerjee, P., Pascolo, L., et al. Affinity of human serum albumin for bilirubin varies with albumin concentration and buffer composition: results of a novel ultrafiltration method. J Biol Chem 276 (2001), 29953–29960.
41. [41] Brito, M.A., Brites, D., Butterfield, D.A., A link between hyperbilirubinemia, oxidative stress and injury to neocortical synaptosomes. Brain Res 1026 (2004), 33–43.
42. [42] Cao, G., Verdon, C.P., Wu, A.H., Wang, H., Prior, R.L., Automated assay of oxygen radical absorbance capacity with the COBAS FARA II. Clin Chem 41 (1995), 1738–1744.
43. [43] Molyneux, P., The use of the stable free radical diphenylpicrylhydrazyl (DPPH) for estimating antioxidant activity. Songklanakarin J Sci Technol 26 (2004), 211–219.
44. [44] Ali, H.M., Abo-Shady, A., Sharaf Eldeen, H.A., Soror, H.A., Shousha, W.G., Abdel-Barry, O.A., et al. Structural features, kinetics and SAR study of radical scavenging and antioxidant activities of phenolic and anilinic compounds. Chem Cent J, 7, 2013, 53.
45. [45] Kawakami, A., Kubota, K., Yamada, N., Tagami, U., Takehana, K., Sonaka, I., et al. Identification and characterization of oxidized human serum albumin. A slight structural change impairs its ligand-binding and antioxidant functions. FEBS J 273 (2006), 3346–3357.
46. [46] Anraku, M., Tsurusaki, Y., Watanabe, H., Maruyama, T., Kragh-Hansen, U., Otagiri, M., Stabilizing mechanisms in commercial albumin preparations: octanoate and N-acetyl-L-tryptophanate protect human serum albumin against heat and oxidative stress. Biochim Biophys Acta 1702 (2004), 9–17.
47. [47] Turell, L., Botti, H., Bonilla, L., Torres, M.J., Schopfer, F., Freeman, B.A., et al. HPLC separation of human serum albumin isoforms based on their isoelectric points. J Chromatogr B Anal Technol Biomed Life Sci 944 (2014), 144–151.
48. [48] Mera, K., Anraku, M., Kitamura, K., Nakajou, K., Maruyama, T., Otagiri, M., The structure and function of oxidized albumin in hemodialysis patients: its role in elevated oxidative stress via neutrophil burst. Biochem Biophys Res Commun 334 (2005), 1322–1328.