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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Cites
Free Radicals in Biology and Medicine
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Enhanced S -Nitroso-Albumin Formation From Inhaled NO During Ischemia/Reperfusion
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Oxidation of Arg‐410 promotes the elimination of human serum albumin
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The antioxidant properties of serum albumin
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The Role of Oxidative Stress in the Pathophysiology of Gestational Diabetes Mellitus
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The glycation of albumin: Structural and functional impacts
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Current issues in measurement and reporting of urinary albumin excretion
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Albumin and Mammalian cell culture: implications for biotechnology applications
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Structural and biochemical features of human Serum albumin essential for eukaryotic cell culture
Mishra, V., & Heath, R. J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22168411 · Cited by 295
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Human albumin in the management of complications of liver cirrhosis
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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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