The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
Physiological and pathological changes in the redox state of human serum albumin critically influence its binding properties
Open accessAbstract
Binding and transport of a number of endogenous and exogenous compounds is an important function of the main plasma protein, albumin. In vivo and in vitro, albumin may be oxidatively modified in different ways with different agents at different sites. These modifications have various consequences on the physiological functions of albumin. Diabetes mellitus, liver diseases and nephropathy are just a few examples of disorders in which oxidative stress is involved and altered albumin functions have been described. This review is focussed on the consequences of oxidative modification on the binding properties of albumin. These range from no effect to decreased or increased binding affinities depending on the ligand under investigation and the type of modification. Indicators for modification include glycosylation, disulphide formation or the content of carbonyl groups. The redox state of albumin can affect the binding properties in several ways, including altered conformation and consequently altered affinities at binding sites and altered binding when the binding reaction itself is redox sensitive. The physiological or pathophysiological concentrations of different oxidatively modified albumin molecules vary over a wide range and are crucial in assessing the clinical relevance of altered ligand binding properties of a particularly modified albumin species in various disease conditions. British Journal of Pharmacology (2007) 151, 580–590; doi:10.1038/sj.bjp.0707251
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Citations
Cites
Free Radicals in Biology and Medicine
Halliwell, B., & Gutteridge, J. M. C. (2015) · doi:10.1093/acprof:oso/9780198717478.001.0001 · Cited by 8,990
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S-Nitrosothiols: cellular formation and transport
Zhang, Y., & Hogg, N. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.12.016 · Cited by 257
S -Nitrosothiols in the Blood: Roles, Amounts, and Methods of Analysis
Stamler, J. S. (2004) · Circulation Research · doi:10.1161/01.res.0000122071.55721.bc · Cited by 170 · cited 2×
“…that the level in healthy humans is in the nanomolar range (Marley et al., 2001; Tsikas and Frölich, 2002; Tsikas et al., 2002; Ng et al., 2004; Stamler, 2004; Zhang and Hogg, 2005), while under pathological conditions, micromolar concentrations of SNO-alb may occur (Ottesen et al., 2001;…”
BackgroundDynamic state of S-nitrosothiols in human plasma and whole blood
Jourd’heuil, D., Hallén, K., Feelisch, M., & Grisham, M. B. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00257-9 · Cited by 156
Enhanced S -Nitroso-Albumin Formation From Inhaled NO During Ischemia/Reperfusion
Ng, E. S. M., Jourd’heuil, D., McCord, J. M., Hernandez, D., Yasui, M., Knight, D., & Kubes, P. (2004) · Circulation Research · doi:10.1161/01.res.0000117771.63140.d6 · Cited by 97 · cited 3×
“…is in the nanomolar range (Marley et al., 2001; Tsikas and Frölich, 2002; Tsikas et al., 2002; Ng et al., 2004; Stamler, 2004; Zhang and Hogg, 2005), while under pathological conditions, micromolar concentrations of SNO-alb may occur (Ottesen et al., 2001; Bayir et al., 2003; Ng et al., 2004).”
BackgroundAlbumin synthesis rates in cirrhosis: Correlation with child-turcotte classification
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Oxidation of Arg‐410 promotes the elimination of human serum albumin
Iwao, Y., Anraku, M., Yamasaki, K., Kragh-Hansen, U., Kawai, K., Maruyama, T., & Otagiri, M. (2006) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2006.01.011 · Cited by 53
Cited by
The antioxidant properties of serum albumin
Roche, M., Rondeau, P., Singh, N. R., Tarnus, E., & Bourdon, E. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.04.057 · Cited by 1,255
The Role of Oxidative Stress in the Pathophysiology of Gestational Diabetes Mellitus
Lappas, M., Hiden, U., Desoye, G., Froehlich, J., Mouzon, S. H.-D., & Jawerbaum, A. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3765 · Cited by 442
The glycation of albumin: Structural and functional impacts
Rondeau, P., & Bourdon, E. (2011) · Biochimie · doi:10.1016/j.biochi.2010.12.003 · Cited by 433
Current issues in measurement and reporting of urinary albumin excretion
Miller, W. G., Bruns, D. E., Hortin, G. L., Sandberg, S., Aakre, K. M., McQueen, M. J., Itoh, Y., Lieske, J. C., Seccombe, D. W., Jones, G., et al. (2009) · Clinical Chemistry · doi:10.1373/clinchem.2008.106567 · Cited by 381
Albumin and Mammalian cell culture: implications for biotechnology applications
Francis, G. L. (2010) · Cytotechnology · doi:10.1007/s10616-010-9263-3 · Cited by 376
Metadata
- Authors
- Oettl, K., & Stauber, R. E.
- Venue
- British Journal of Pharmacology
- Publisher
- Wiley
- Published
- 2007-07
- Volume
- 151
- Issue
- 5
- Pages
- 580-590
- ISSN
- 0007-1188 (ISSN-L)
- 1476-5381
- OpenAlex
- W1977892627
- Cited by
- 357
- References
- 9
- FWCI
- 5.03
- Type
- journal article
- Language
- en
- Open access
- bronze
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