Pharmaceutically Important Pre- and Posttranslational Modifications on Human Serum Albumin

Otagiri, Masaki; Chuang, Victor Tuan Giam

doi:10.1248/bpb.32.527

Cited by 48 publications

(44 citation statements)

References 90 publications

(90 reference statements)

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“…Albumin is widely used in clinical settings as a biomaterial for medical and pharmaceutical applications because of its availability, biodegradability, lack of toxicity, and non-immunogenicity. 51,52 Thus, our studies may not only bring new insights into the pathogenesis of FAP, but also suggest novel therapeutic strategies for FAP.…”

Section: Discussionmentioning

confidence: 93%

Loss of functional albumin triggers acceleration of transthyretin amyloid fibril formation in familial amyloidotic polyneuropathy

Kugimiya

Jono

Saito

et al. 2011

Laboratory Investigation

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Transthyretin (TTR)-related familial amyloidotic polyneuropathy (FAP) is characterized by systemic accumulation of amyloid fibrils caused by a point mutation in the TTR gene. Despite the urgent need for alternative therapeutic strategies, the pathogenesis of FAP still remains elusive. In our study reported here, we focused on albumin, the most abundant protein in plasma, and described the role of albumin in the TTR amyloid-formation process. Patients with FAP evidenced significantly decreased serum albumin levels as the disease progressed. Biacore analysis showed that albumin had a binding affinity for TTR and exhibited higher affinity for TTR amyloid than native TTR. Albumin functioning as an antioxidant effectively suppressed TTR amyloid formation. In patients with FAP, albumin was significantly oxidized as the disease progressed. Moreover, loss of functional albumin accelerated TTR deposition in analbuminemic rats possessing a human variant TTR gene. Taken together, these results indicate that albumin may have an inhibitory role in the TTR amyloid-formation process.

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Section: Discussionmentioning

confidence: 93%

Loss of functional albumin triggers acceleration of transthyretin amyloid fibril formation in familial amyloidotic polyneuropathy

Kugimiya

Jono

Saito

et al. 2011

Laboratory Investigation

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“…Human serum albumin (HSA) is a single polypeptide consisting of 585 amino acids, including 35 cysteines and 17 disulfide bridges (104). In human plasma, S-nitroso-serum albumin (SNO-SA) accounts for an impressive 82% of all Snitrosothiols; thus, it follows that the single free cysteine (Cys34) (pKa = *5) is observed to be highly reactive with nitrogen oxide species (126).…”

Section: Human Serum Albuminmentioning

confidence: 99%

S-Nitrosothiols and theS-Nitrosoproteome of the Cardiovascular System

Maron

Tang²,

Loscalzo³

2013

Antioxidants & Redox Signaling

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Significance: Since their discovery in the early 1990's, S-nitrosylated proteins have been increasingly recognized as important determinants of many biochemical processes. Specifically, S-nitrosothiols in the cardiovascular system exert many actions, including promoting vasodilation, inhibiting platelet aggregation, and regulating Ca 2+ channel function that influences myocyte contractility and electrophysiologic stability. Recent Advances: Contemporary developments in liquid chromatography-mass spectrometry methods, the development of biotin-and His-tag switch assays, and the availability of cyanide dye-labeling for S-nitrosothiol detection in vitro have increased significantly the identification of a number of cardiovascular protein targets of S-nitrosylation in vivo. Critical Issues: Recent analyses using modern S-nitrosothiol detection techniques have revealed the mechanistic significance of S-nitrosylation to the pathophysiology of numerous cardiovascular diseases, including essential hypertension, pulmonary hypertension, ischemic heart disease, stroke, and congestive heart failure, among others. Future Directions: Despite enhanced insight into S-nitrosothiol biochemistry, translating these advances into beneficial pharmacotherapies for patients with cardiovascular diseases remains a primary as-yet unmet goal for investigators within the field. Antioxid. Redox Signal. 18, 270-287.

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“…In concert with progress in genetic engineering, physicochemical characterization methods for proteins in microscale HSA have also developed substantially, although posttranslational modifications remain a bottleneck in such characterizations. 1) HSA is a globular monomeric protein with a molecular weight of 66.5 kDa, and contains 35 cysteinyl residues, 34 of which participate in 17 disulfide bridges.…”

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confidence: 99%

Characterization of Sulfhydryl Heterogeneity in Human Serum Albumin and Recombinant Human Serum Albumin for Clinical Use

Ikegaya¹,

Nokihara

Yasuhara

2010

Bioscience, Biotechnology, and Biochemistry

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Since human serum albumin has one sulfhydryl group and 17 disulfides, reactive sulfhydryl groups give rise to heterogeneity. The present paper presents a comparison of sulfhydryl heterogeneity in human serum albumin and recombinant human serum albumin for clinical use. Low molecular weight sulfhydryl compounds were identified from both sources. The recombinant albumin had a much higher sulfhydryl content than plasma serum albumin.

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Pharmaceutically Important Pre- and Posttranslational Modifications on Human Serum Albumin

Cited by 48 publications

References 90 publications

Loss of functional albumin triggers acceleration of transthyretin amyloid fibril formation in familial amyloidotic polyneuropathy

Loss of functional albumin triggers acceleration of transthyretin amyloid fibril formation in familial amyloidotic polyneuropathy

S-Nitrosothiols and theS-Nitrosoproteome of the Cardiovascular System

Characterization of Sulfhydryl Heterogeneity in Human Serum Albumin and Recombinant Human Serum Albumin for Clinical Use

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