S-Thiolation Targets Albumin in Heart Failure
Human serum albumin (HSA) is associated with several physiological functions, such as maintaining oncotic pressure and microvascular integrity, among others. It also represents the major and predominant antioxidant in plasma due to the presence of the Cys34 sulfhydryl group. In this study, we assess...
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| Format: | Article |
| Language: | English |
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MDPI AG
2020-08-01
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| Series: | Antioxidants |
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| Online Access: | https://www.mdpi.com/2076-3921/9/8/763 |
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| author | Maura Brioschi Erica Gianazza Alice Mallia Beatrice Zoanni Alessandra Altomare Alma Martinez Fernandez Piergiuseppe Agostoni Giancarlo Aldini Cristina Banfi |
| author_facet | Maura Brioschi Erica Gianazza Alice Mallia Beatrice Zoanni Alessandra Altomare Alma Martinez Fernandez Piergiuseppe Agostoni Giancarlo Aldini Cristina Banfi |
| author_sort | Maura Brioschi |
| collection | DOAJ |
| description | Human serum albumin (HSA) is associated with several physiological functions, such as maintaining oncotic pressure and microvascular integrity, among others. It also represents the major and predominant antioxidant in plasma due to the presence of the Cys34 sulfhydryl group. In this study, we assessed qualitative and quantitative changes in HSA in patients with heart failure (HF) and their relationship with the severity of the disease. We detected by means of mass spectrometry a global decrease of the HSA content in the plasma of HF patients in respect to control subjects, a significant increase of thio-HSA with a concomitant decrease in the reduced form of albumin. Cysteine and, at a lesser extent, homocysteine represent the most abundant thiol bound to HSA. A strong inverse correlation was also observed between cysteine-HSA and peak VO<sub>2</sub>/kg, an index of oxygen consumption associated with HF severity. Moreover, in HL-1 cardiomyocytes incubated with H<sub>2</sub>O<sub>2</sub>, we showed a significant decrease of cell viability in cells treated with thio-HSA in respect to restored native-HSA. In conclusion, we found for the first time that S-thiolation of albumin is increased in the plasma of HF patients and induced changes in the structure and antioxidant function of HSA, likely contributing to HF progression. |
| first_indexed | 2024-03-10T17:17:50Z |
| format | Article |
| id | doaj.art-07e505e441324c54a1d044ff82718607 |
| institution | Directory Open Access Journal |
| issn | 2076-3921 |
| language | English |
| last_indexed | 2024-03-10T17:17:50Z |
| publishDate | 2020-08-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Antioxidants |
| spelling | doaj.art-07e505e441324c54a1d044ff827186072023-11-20T10:25:14ZengMDPI AGAntioxidants2076-39212020-08-019876310.3390/antiox9080763S-Thiolation Targets Albumin in Heart FailureMaura Brioschi0Erica Gianazza1Alice Mallia2Beatrice Zoanni3Alessandra Altomare4Alma Martinez Fernandez5Piergiuseppe Agostoni6Giancarlo Aldini7Cristina Banfi8Centro Cardiologico Monzino, IRCCS, 20138 Milano, ItalyCentro Cardiologico Monzino, IRCCS, 20138 Milano, ItalyCentro Cardiologico Monzino, IRCCS, 20138 Milano, ItalyCentro Cardiologico Monzino, IRCCS, 20138 Milano, ItalyDipartimento di Scienze Farmaceutiche, Università di Milano, 20133 Milano, ItalyCentro Cardiologico Monzino, IRCCS, 20138 Milano, ItalyCentro Cardiologico Monzino, IRCCS, 20138 Milano, ItalyDipartimento di Scienze Farmaceutiche, Università di Milano, 20133 Milano, ItalyCentro Cardiologico Monzino, IRCCS, 20138 Milano, ItalyHuman serum albumin (HSA) is associated with several physiological functions, such as maintaining oncotic pressure and microvascular integrity, among others. It also represents the major and predominant antioxidant in plasma due to the presence of the Cys34 sulfhydryl group. In this study, we assessed qualitative and quantitative changes in HSA in patients with heart failure (HF) and their relationship with the severity of the disease. We detected by means of mass spectrometry a global decrease of the HSA content in the plasma of HF patients in respect to control subjects, a significant increase of thio-HSA with a concomitant decrease in the reduced form of albumin. Cysteine and, at a lesser extent, homocysteine represent the most abundant thiol bound to HSA. A strong inverse correlation was also observed between cysteine-HSA and peak VO<sub>2</sub>/kg, an index of oxygen consumption associated with HF severity. Moreover, in HL-1 cardiomyocytes incubated with H<sub>2</sub>O<sub>2</sub>, we showed a significant decrease of cell viability in cells treated with thio-HSA in respect to restored native-HSA. In conclusion, we found for the first time that S-thiolation of albumin is increased in the plasma of HF patients and induced changes in the structure and antioxidant function of HSA, likely contributing to HF progression.https://www.mdpi.com/2076-3921/9/8/763s-thiolationalbuminheart failureoxidative stress |
| spellingShingle | Maura Brioschi Erica Gianazza Alice Mallia Beatrice Zoanni Alessandra Altomare Alma Martinez Fernandez Piergiuseppe Agostoni Giancarlo Aldini Cristina Banfi S-Thiolation Targets Albumin in Heart Failure Antioxidants s-thiolation albumin heart failure oxidative stress |
| title | S-Thiolation Targets Albumin in Heart Failure |
| title_full | S-Thiolation Targets Albumin in Heart Failure |
| title_fullStr | S-Thiolation Targets Albumin in Heart Failure |
| title_full_unstemmed | S-Thiolation Targets Albumin in Heart Failure |
| title_short | S-Thiolation Targets Albumin in Heart Failure |
| title_sort | s thiolation targets albumin in heart failure |
| topic | s-thiolation albumin heart failure oxidative stress |
| url | https://www.mdpi.com/2076-3921/9/8/763 |
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