Oxidized albumin. The long way of a protein of uncertain function

Proteins are extremely reactive to oxidants and should represent a potential target of instable reactive oxygen. This may represent a problem for plasma proteins since they may be directly modified in vivo in a compartment where antioxidant enzymatic systems are scarcely represented. On the other ha...

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Published inBiochimica et biophysica acta Vol. 1830; no. 12; pp. 5473 - 5479
Main Authors Bruschi, Maurizio, Candiano, Giovanni, Santucci, Laura, Ghiggeri, Gian Marco
Format Journal Article
LanguageEnglish
Published Netherlands Elsevier B.V 01.12.2013
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ISSN0304-4165
0006-3002
1872-8006
DOI10.1016/j.bbagen.2013.04.017

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Abstract Proteins are extremely reactive to oxidants and should represent a potential target of instable reactive oxygen. This may represent a problem for plasma proteins since they may be directly modified in vivo in a compartment where antioxidant enzymatic systems are scarcely represented. On the other hand, it is possible that some plasma components have evolved over time to guarantee protection, in which case they can be considered as anti-oxidants. To present and discuss main studies which addressed the role of albumin in plasma antioxidant activity mainly utilizing in vitro models of oxidation. To present some advances on structural features of oxidized albumin deriving from studies carried out on in vitro models as well as albumin purified in vivo from patients affected by clinical conditions characterized by oxidative stress. There are different interaction with HOCl and chloramines. In the former case, HOCl produces an extensive alteration of 238Trp and 162Tyr, 425Tyr, 47Tyr, while thiol groups are only partially involved. Chloramines are extremely reactive with the unique free SH group of albumin (34Cys) with the formation of sulfenic and sulfinic acid as intermediates and sulfonic acid as end-product. Oxidized albumin has a modified electrical charge for the addition of an acidic residue and presents α-helix and random coil reorganization with subtle changes in domain orientation. Albumin, is the major antioxidants in plasma with a concentration (0.8mM) higher than other antioxidants by an exponential factor. Functional and protective roles in the presence of oxidative stress must be defined. This article is part of a Special Issue entitled Serum Albumin. •Albumin is the main antioxidant in plasma where classical cell antioxidants are low.•In vivo oxidized albumin has a sulfonic acid residue in place of SH at 34Cys.•It also presents a modified electrical and α-helix/random coil reorganization.•HOCl produces an extensive alteration of Trp and Tyr; thiol groups are not involved.•Chloramines are extremely reactive with the unique free SH group of albumin (34Cys).
AbstractList Proteins are extremely reactive to oxidants and should represent a potential target of instable reactive oxygen. This may represent a problem for plasma proteins since they may be directly modified in vivo in a compartment where antioxidant enzymatic systems are scarcely represented. On the other hand, it is possible that some plasma components have evolved over time to guarantee protection, in which case they can be considered as anti-oxidants.To present and discuss main studies which addressed the role of albumin in plasma antioxidant activity mainly utilizing in vitro models of oxidation. To present some advances on structural features of oxidized albumin deriving from studies carried out on in vitro models as well as albumin purified in vivo from patients affected by clinical conditions characterized by oxidative stress.There are different interaction with HOCl and chloramines. In the former case, HOCl produces an extensive alteration of 238Trp and 162Tyr, 425Tyr, 47Tyr, while thiol groups are only partially involved. Chloramines are extremely reactive with the unique free SH group of albumin (34Cys) with the formation of sulfenic and sulfinic acid as intermediates and sulfonic acid as end-product. Oxidized albumin has a modified electrical charge for the addition of an acidic residue and presents α-helix and random coil reorganization with subtle changes in domain orientation.Albumin, is the major antioxidants in plasma with a concentration (0.8mM) higher than other antioxidants by an exponential factor. Functional and protective roles in the presence of oxidative stress must be defined. This article is part of a Special Issue entitled Serum Albumin.
BACKGROUND: Proteins are extremely reactive to oxidants and should represent a potential target of instable reactive oxygen. This may represent a problem for plasma proteins since they may be directly modified in vivo in a compartment where antioxidant enzymatic systems are scarcely represented. On the other hand, it is possible that some plasma components have evolved over time to guarantee protection, in which case they can be considered as anti-oxidants. SCOPE OF REVIEW: To present and discuss main studies which addressed the role of albumin in plasma antioxidant activity mainly utilizing in vitro models of oxidation. To present some advances on structural features of oxidized albumin deriving from studies carried out on in vitro models as well as albumin purified in vivo from patients affected by clinical conditions characterized by oxidative stress. MAJOR CONCLUSIONS: There are different interaction with HOCl and chloramines. In the former case, HOCl produces an extensive alteration of ²³⁸Trp and ¹⁶²Tyr, ⁴²⁵Tyr, ⁴⁷Tyr, while thiol groups are only partially involved. Chloramines are extremely reactive with the unique free SH group of albumin (³⁴Cys) with the formation of sulfenic and sulfinic acid as intermediates and sulfonic acid as end-product. Oxidized albumin has a modified electrical charge for the addition of an acidic residue and presents α-helix and random coil reorganization with subtle changes in domain orientation. GENERAL SIGNIFICANCE: Albumin, is the major antioxidants in plasma with a concentration (0.8mM) higher than other antioxidants by an exponential factor. Functional and protective roles in the presence of oxidative stress must be defined. This article is part of a Special Issue entitled Serum Albumin.
Proteins are extremely reactive to oxidants and should represent a potential target of instable reactive oxygen. This may represent a problem for plasma proteins since they may be directly modified in vivo in a compartment where antioxidant enzymatic systems are scarcely represented. On the other hand, it is possible that some plasma components have evolved over time to guarantee protection, in which case they can be considered as anti-oxidants. To present and discuss main studies which addressed the role of albumin in plasma antioxidant activity mainly utilizing in vitro models of oxidation. To present some advances on structural features of oxidized albumin deriving from studies carried out on in vitro models as well as albumin purified in vivo from patients affected by clinical conditions characterized by oxidative stress. There are different interaction with HOCl and chloramines. In the former case, HOCl produces an extensive alteration of (238)Trp and (162)Tyr, (425)Tyr, (47)Tyr, while thiol groups are only partially involved. Chloramines are extremely reactive with the unique free SH group of albumin ((34)Cys) with the formation of sulfenic and sulfinic acid as intermediates and sulfonic acid as end-product. Oxidized albumin has a modified electrical charge for the addition of an acidic residue and presents α-helix and random coil reorganization with subtle changes in domain orientation. Albumin, is the major antioxidants in plasma with a concentration (0.8mM) higher than other antioxidants by an exponential factor. Functional and protective roles in the presence of oxidative stress must be defined. This article is part of a Special Issue entitled Serum Albumin.
Proteins are extremely reactive to oxidants and should represent a potential target of instable reactive oxygen. This may represent a problem for plasma proteins since they may be directly modified in vivo in a compartment where antioxidant enzymatic systems are scarcely represented. On the other hand, it is possible that some plasma components have evolved over time to guarantee protection, in which case they can be considered as anti-oxidants.BACKGROUNDProteins are extremely reactive to oxidants and should represent a potential target of instable reactive oxygen. This may represent a problem for plasma proteins since they may be directly modified in vivo in a compartment where antioxidant enzymatic systems are scarcely represented. On the other hand, it is possible that some plasma components have evolved over time to guarantee protection, in which case they can be considered as anti-oxidants.To present and discuss main studies which addressed the role of albumin in plasma antioxidant activity mainly utilizing in vitro models of oxidation. To present some advances on structural features of oxidized albumin deriving from studies carried out on in vitro models as well as albumin purified in vivo from patients affected by clinical conditions characterized by oxidative stress.SCOPE OF REVIEWTo present and discuss main studies which addressed the role of albumin in plasma antioxidant activity mainly utilizing in vitro models of oxidation. To present some advances on structural features of oxidized albumin deriving from studies carried out on in vitro models as well as albumin purified in vivo from patients affected by clinical conditions characterized by oxidative stress.There are different interaction with HOCl and chloramines. In the former case, HOCl produces an extensive alteration of (238)Trp and (162)Tyr, (425)Tyr, (47)Tyr, while thiol groups are only partially involved. Chloramines are extremely reactive with the unique free SH group of albumin ((34)Cys) with the formation of sulfenic and sulfinic acid as intermediates and sulfonic acid as end-product. Oxidized albumin has a modified electrical charge for the addition of an acidic residue and presents α-helix and random coil reorganization with subtle changes in domain orientation.MAJOR CONCLUSIONSThere are different interaction with HOCl and chloramines. In the former case, HOCl produces an extensive alteration of (238)Trp and (162)Tyr, (425)Tyr, (47)Tyr, while thiol groups are only partially involved. Chloramines are extremely reactive with the unique free SH group of albumin ((34)Cys) with the formation of sulfenic and sulfinic acid as intermediates and sulfonic acid as end-product. Oxidized albumin has a modified electrical charge for the addition of an acidic residue and presents α-helix and random coil reorganization with subtle changes in domain orientation.Albumin, is the major antioxidants in plasma with a concentration (0.8mM) higher than other antioxidants by an exponential factor. Functional and protective roles in the presence of oxidative stress must be defined. This article is part of a Special Issue entitled Serum Albumin.GENERAL SIGNIFICANCEAlbumin, is the major antioxidants in plasma with a concentration (0.8mM) higher than other antioxidants by an exponential factor. Functional and protective roles in the presence of oxidative stress must be defined. This article is part of a Special Issue entitled Serum Albumin.
Proteins are extremely reactive to oxidants and should represent a potential target of instable reactive oxygen. This may represent a problem for plasma proteins since they may be directly modified in vivo in a compartment where antioxidant enzymatic systems are scarcely represented. On the other hand, it is possible that some plasma components have evolved over time to guarantee protection, in which case they can be considered as anti-oxidants. To present and discuss main studies which addressed the role of albumin in plasma antioxidant activity mainly utilizing in vitro models of oxidation. To present some advances on structural features of oxidized albumin deriving from studies carried out on in vitro models as well as albumin purified in vivo from patients affected by clinical conditions characterized by oxidative stress. There are different interaction with HOCl and chloramines. In the former case, HOCl produces an extensive alteration of 238Trp and 162Tyr, 425Tyr, 47Tyr, while thiol groups are only partially involved. Chloramines are extremely reactive with the unique free SH group of albumin (34Cys) with the formation of sulfenic and sulfinic acid as intermediates and sulfonic acid as end-product. Oxidized albumin has a modified electrical charge for the addition of an acidic residue and presents α-helix and random coil reorganization with subtle changes in domain orientation. Albumin, is the major antioxidants in plasma with a concentration (0.8mM) higher than other antioxidants by an exponential factor. Functional and protective roles in the presence of oxidative stress must be defined. This article is part of a Special Issue entitled Serum Albumin. •Albumin is the main antioxidant in plasma where classical cell antioxidants are low.•In vivo oxidized albumin has a sulfonic acid residue in place of SH at 34Cys.•It also presents a modified electrical and α-helix/random coil reorganization.•HOCl produces an extensive alteration of Trp and Tyr; thiol groups are not involved.•Chloramines are extremely reactive with the unique free SH group of albumin (34Cys).
Author Bruschi, Maurizio
Santucci, Laura
Candiano, Giovanni
Ghiggeri, Gian Marco
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  fullname: Bruschi, Maurizio
  organization: Laboratory on Pathophysiology of Uremia, Istituto Giannina Gaslini, Genoa, Italy
– sequence: 2
  givenname: Giovanni
  surname: Candiano
  fullname: Candiano, Giovanni
  organization: Division of Nephrology, Dialysis, and Transplantation, Istituto Giannina Gaslini, Genoa, Italy
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  givenname: Laura
  surname: Santucci
  fullname: Santucci, Laura
  organization: Laboratory on Pathophysiology of Uremia, Istituto Giannina Gaslini, Genoa, Italy
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  givenname: Gian Marco
  surname: Ghiggeri
  fullname: Ghiggeri, Gian Marco
  email: labnefro@ospedale-gaslini.ge.it
  organization: Division of Nephrology, Dialysis, and Transplantation, Istituto Giannina Gaslini, Genoa, Italy
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Issue 12
Keywords LC–MS–MS
Renal diseases
Reactive oxygen species
Focal segmental glomerulosclerosis
DSC
ESI-MS
Oxidation
Serum albumin
Nephritic syndrome
HOCI
AOPPs
electrospray ionization mass spectrometry
hypochlorous acid
liquid chromatography with tandem mass spectrometry
advanced oxidation products
differential scanning calorimetry
Language English
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Snippet Proteins are extremely reactive to oxidants and should represent a potential target of instable reactive oxygen. This may represent a problem for plasma...
BACKGROUND: Proteins are extremely reactive to oxidants and should represent a potential target of instable reactive oxygen. This may represent a problem for...
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SubjectTerms antioxidant activity
antioxidants
Antioxidants - metabolism
Focal segmental glomerulosclerosis
Humans
Models, Molecular
Nephritic syndrome
oxidants
Oxidation
Oxidation-Reduction
oxidative stress
oxygen
patients
Reactive oxygen species
Renal diseases
Serum albumin
Serum Albumin - chemistry
Serum Albumin - metabolism
sulfonic acid
sulfonic acids
thiols
Title Oxidized albumin. The long way of a protein of uncertain function
URI https://dx.doi.org/10.1016/j.bbagen.2013.04.017
https://www.ncbi.nlm.nih.gov/pubmed/23618696
https://www.proquest.com/docview/1443410383
https://www.proquest.com/docview/2000085584
Volume 1830
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