Oxidation of the albumin thiol to sulfenic acid and its implications in the intravascular compartment
Human serum albumin (HSA) is the most abundant protein in the intravascular compartment. It possesses a single thiol, Cys34, which constitutes ~80% of the total thiols in plasma. This thiol is able to scavenge plasma oxidants. A central intermediate in this potential antioxidant activity of human se...
| Main Authors: | , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Associação Brasileira de Divulgação Científica
2009-04-01
|
| Series: | Brazilian Journal of Medical and Biological Research |
| Subjects: | |
| Online Access: | http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2009000400001 |
| _version_ | 1818963731547160576 |
|---|---|
| author | L. Turell S. Carballal H. Botti R. Radi B. Alvarez |
| author_facet | L. Turell S. Carballal H. Botti R. Radi B. Alvarez |
| author_sort | L. Turell |
| collection | DOAJ |
| description | Human serum albumin (HSA) is the most abundant protein in the intravascular compartment. It possesses a single thiol, Cys34, which constitutes ~80% 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 ~25% 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. |
| first_indexed | 2024-12-20T12:49:53Z |
| format | Article |
| id | doaj.art-d5da0553b40b45fcb5bd0d317f202cc4 |
| institution | Directory Open Access Journal |
| issn | 0100-879X 1414-431X |
| language | English |
| last_indexed | 2024-12-20T12:49:53Z |
| publishDate | 2009-04-01 |
| publisher | Associação Brasileira de Divulgação Científica |
| record_format | Article |
| series | Brazilian Journal of Medical and Biological Research |
| spelling | doaj.art-d5da0553b40b45fcb5bd0d317f202cc42022-12-21T19:40:11ZengAssociação Brasileira de Divulgação CientíficaBrazilian Journal of Medical and Biological Research0100-879X1414-431X2009-04-0142430531110.1590/S0100-879X2009000400001Oxidation of the albumin thiol to sulfenic acid and its implications in the intravascular compartmentL. TurellS. CarballalH. BottiR. RadiB. AlvarezHuman serum albumin (HSA) is the most abundant protein in the intravascular compartment. It possesses a single thiol, Cys34, which constitutes ~80% 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 ~25% 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.http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2009000400001ThiolSulfhydrylAlbuminSulfenic acidMixed disulfidesPlasma |
| spellingShingle | L. Turell S. Carballal H. Botti R. Radi B. Alvarez Oxidation of the albumin thiol to sulfenic acid and its implications in the intravascular compartment Brazilian Journal of Medical and Biological Research Thiol Sulfhydryl Albumin Sulfenic acid Mixed disulfides Plasma |
| title | Oxidation of the albumin thiol to sulfenic acid and its implications in the intravascular compartment |
| title_full | Oxidation of the albumin thiol to sulfenic acid and its implications in the intravascular compartment |
| title_fullStr | Oxidation of the albumin thiol to sulfenic acid and its implications in the intravascular compartment |
| title_full_unstemmed | Oxidation of the albumin thiol to sulfenic acid and its implications in the intravascular compartment |
| title_short | Oxidation of the albumin thiol to sulfenic acid and its implications in the intravascular compartment |
| title_sort | oxidation of the albumin thiol to sulfenic acid and its implications in the intravascular compartment |
| topic | Thiol Sulfhydryl Albumin Sulfenic acid Mixed disulfides Plasma |
| url | http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2009000400001 |
| work_keys_str_mv | AT lturell oxidationofthealbuminthioltosulfenicacidanditsimplicationsintheintravascularcompartment AT scarballal oxidationofthealbuminthioltosulfenicacidanditsimplicationsintheintravascularcompartment AT hbotti oxidationofthealbuminthioltosulfenicacidanditsimplicationsintheintravascularcompartment AT rradi oxidationofthealbuminthioltosulfenicacidanditsimplicationsintheintravascularcompartment AT balvarez oxidationofthealbuminthioltosulfenicacidanditsimplicationsintheintravascularcompartment |