Alteration of redox state of human serum albumin in patients under anesthesia and invasive surgery

Hayakawa, Atsushi; Kuwata, Kazuo; Era, Seiichi; Sogami, Masaru; Shimonaka, Hiroyuki; Yamamoto, Michio; Dohi, Shuji; Hirose, Hajime

doi:10.1016/s0378-4347(97)00274-0

Cited by 44 publications

(25 citation statements)

References 36 publications

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“…Serum albumin concentration refl ects the nutritional condition of patients with chronic renal dysfunction, and the level of albumin mRNA in the liver was reported to decrease with the progression of renal failure [3] . Quantitative as well as qualitative changes of serum albumin have also been suggested in recent years [4,5] . Human serum albumin is composed of mercaptalbumin (HMA, reduced form) and nonmercaptalbumin (HNA, oxidized form), that is, a protein redox couple.…”

Section: Introductionmentioning

confidence: 93%

Alteration of Redox State of Human Serum Albumin before and after Hemodialysis

et al. 2004

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Background:Persistent hypoalbuminemia is a predictor of death in long-term maintenance hemodialysis patients, although cardiovascular diseases remain the leading cause of death. A decreased serum antioxidant activity in maintenance hemodialysis patients may contribute to increased oxidative damage, and may be associated with accelerated atherosclerotic changes. Methods:The aim of this study was to examine the redox state of human serum albumin in maintenance hemodialysis patients by high-performance liquid chromatography (HPLC) using a fluorescence detector. Results: HPLC of human serum albumin on a Shodex-Asahipak ES-502N column at pH 4.85 showed a clear resolution of human mercaptalbumin (HMA) and nonmercaptalbumin (HNA), which are the reduced and oxidized forms of human serum albumin, respectively. The mean ± SD percentage of the HMA fraction of human serum albumin was significantly lower in maintenance hemodialysis patients than in age-matched normal subjects. The percentage of HMA increased 3–5 h after starting the hemodialysis and then decreased to subnormal levels. Conclusion: This suggests that serum albumin may be a major extracellular antioxidant in maintenance hemodialysis patients, and that hemodialysis may rescue serum albumin reduction by inducing intermolecular sulfhydryl-disulfide exchange reaction.

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Section: Introductionmentioning

confidence: 93%

Alteration of Redox State of Human Serum Albumin before and after Hemodialysis

et al. 2004

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“…In constant, significant evidence for the presence of ROS-mediated protein damage in vivo and its possible clinical significance is not currently available. Many studies showed the presence of elevated levels of oxidized albumin, in patients with diabetes mellitus type 1 and type 2; aging [26], patients with chronic hepatitis C, oxidized albumin is a reliable marker of oxidative stress in hemodialysis patients [35,36] and alteration of redox state of HSA is also seen in patients under anesthesia and invasive surgery [37] and many other diseases. In diabetes the circulating albumin level is depressed.…”

Section: Albumin Under Oxidative Stressmentioning

confidence: 99%

Role of Human Serum Albumin and Oxidative Stress in Diabetes

Prakash

2017

JABB

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DiabetesDiabetes mellitus (DM) comprises a group of common metabolic disorders that share the phenotype of hyperglycemia. Several distinct types of DM exist and are caused by a complex interaction of genetics, environmental factors and life-style AbstractChanges in human behaviour and lifestyle over the last century have resulted in a dramatic increase in the incidence of diabetes worldwide. Albumin, a major protein in the blood circulation, can undergo increased glycation in diabetes. From recent studies, it has become evident that glycation has important implications for albumin actions and impact on cell functioning. Human serum albumin (HSA) is the most abundant serum protein whose redox modifications modulate its physiological function, as well as serves as bio-marker for oxidative stress. Previous experimental and clinical studies report that oxidative stress plays a major role in the pathogenesis and development of complications of both types of DM. Hypoalbuminemia is the strongest clinical indicator of progression of many human diseases including cancer, diabetes, rheumatic diseases, liver and other diseases. Also, there is currently great interest in the potential contribution of increased oxidative stress to the development of complications in diabetes mellitus. This mini review highlights the association of human serum albumin and oxidative stress in diabetes.

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“…Recently, a progressive oxidative modification of albumin with increasing severity of liver failure has been reported (52). The fraction of oxidized albumin is also increased in diabetes mellitus (53), disorders of the temporomandibular joint (54), senile cataract (55), and invasive surgery (56). Furthermore, it has been shown that the fraction of oxidized albumin also increases with aging (26,35) and intense exercise (57).…”

Section: Implications In Pathologymentioning

confidence: 99%

Oxidation of the albumin thiol to sulfenic acid and its implications in the intravascular compartment

Turell

Carballal

Botti

et al. 2009

Braz J Med Biol Res

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Human serum albumin (HSA) is the most abundant protein in the intravascular compartment. It possesses a single thiol, Cys34, which constitutes ~8 0% of the total thiols in plasma. This thiol is able to scavenge plasma oxidants. A central intermediate in this potential antioxidant activity of human serum albumin is sulfenic acid (HSA-SOH). Work from our laboratories has demonstrated the formation of a relatively stable sulfenic acid in albumin through complementary spectrophotometric and mass spectrometric approaches. Recently, we have been able to obtain quantitative data that allowed us to measure the rate constants of sulfenic acid reactions with molecules of analytical and biological interest. Kinetic considerations led us to conclude that the most likely fate for sulfenic acid formed in the plasma environment is the reaction with low molecular weight thiols to form mixed disulfides, a reversible modification that is actually observed in ~2 5% of circulating albumin. Another possible fate for sulfenic acid is further oxidation to sulfinic and sulfonic acids. These irreversible modifications are also detected in the circulation. Oxidized forms of albumin are increased in different pathophysiological conditions and sulfenic acid lies in a mechanistic junction, relating oxidizing species to final thiol oxidation products.

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Alteration of redox state of human serum albumin in patients under anesthesia and invasive surgery

Cited by 44 publications

References 36 publications

Alteration of Redox State of Human Serum Albumin before and after Hemodialysis

Alteration of Redox State of Human Serum Albumin before and after Hemodialysis

Role of Human Serum Albumin and Oxidative Stress in Diabetes

Oxidation of the albumin thiol to sulfenic acid and its implications in the intravascular compartment

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