Post-Translational Modifications of Circulating Alpha-1-Antitrypsin Protein
Alpha-1-antitrypsin (AAT), an acute-phase protein encoded by the <i>SERPINA1</i> gene, is a member of the serine protease inhibitor (SERPIN) superfamily. Its primary function is to protect tissues from enzymes released during inflammation, such as neutrophil elastase and proteinase 3. In...
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MDPI AG
2020-12-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/21/23/9187 |
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doaj-e9199b9c1c4448ffb2f5bba429ff05412020-12-03T00:00:51ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672020-12-01219187918710.3390/ijms21239187Post-Translational Modifications of Circulating Alpha-1-Antitrypsin ProteinUrszula Lechowicz0Stefan Rudzinski1Aleksandra Jezela-Stanek2Sabina Janciauskiene3Joanna Chorostowska-Wynimko4Department of Genetics and Clinical Immunology, National Institute of Tuberculosis and Lung Diseases, 01-138 Warsaw, PolandDepartment of Genetics and Clinical Immunology, National Institute of Tuberculosis and Lung Diseases, 01-138 Warsaw, PolandDepartment of Genetics and Clinical Immunology, National Institute of Tuberculosis and Lung Diseases, 01-138 Warsaw, PolandDepartment of Genetics and Clinical Immunology, National Institute of Tuberculosis and Lung Diseases, 01-138 Warsaw, PolandDepartment of Genetics and Clinical Immunology, National Institute of Tuberculosis and Lung Diseases, 01-138 Warsaw, PolandAlpha-1-antitrypsin (AAT), an acute-phase protein encoded by the <i>SERPINA1</i> gene, is a member of the serine protease inhibitor (SERPIN) superfamily. Its primary function is to protect tissues from enzymes released during inflammation, such as neutrophil elastase and proteinase 3. In addition to its antiprotease activity, AAT interacts with numerous other substances and has various functions, mainly arising from the conformational flexibility of normal variants of AAT. Therefore, AAT has diverse biological functions and plays a role in various pathophysiological processes. This review discusses major molecular forms of AAT, including complex, cleaved, glycosylated, oxidized, and S-nitrosylated forms, in terms of their origin and function.https://www.mdpi.com/1422-0067/21/23/9187alpha-1-antitrypsinAAT<i>SERPINA1</i>chronic obstructive pulmonary diseaseprotease inhibitorS-nitrosylation |
| collection |
DOAJ |
| language |
English |
| format |
Article |
| sources |
DOAJ |
| author |
Urszula Lechowicz Stefan Rudzinski Aleksandra Jezela-Stanek Sabina Janciauskiene Joanna Chorostowska-Wynimko |
| spellingShingle |
Urszula Lechowicz Stefan Rudzinski Aleksandra Jezela-Stanek Sabina Janciauskiene Joanna Chorostowska-Wynimko Post-Translational Modifications of Circulating Alpha-1-Antitrypsin Protein International Journal of Molecular Sciences alpha-1-antitrypsin AAT <i>SERPINA1</i> chronic obstructive pulmonary disease protease inhibitor S-nitrosylation |
| author_facet |
Urszula Lechowicz Stefan Rudzinski Aleksandra Jezela-Stanek Sabina Janciauskiene Joanna Chorostowska-Wynimko |
| author_sort |
Urszula Lechowicz |
| title |
Post-Translational Modifications of Circulating Alpha-1-Antitrypsin Protein |
| title_short |
Post-Translational Modifications of Circulating Alpha-1-Antitrypsin Protein |
| title_full |
Post-Translational Modifications of Circulating Alpha-1-Antitrypsin Protein |
| title_fullStr |
Post-Translational Modifications of Circulating Alpha-1-Antitrypsin Protein |
| title_full_unstemmed |
Post-Translational Modifications of Circulating Alpha-1-Antitrypsin Protein |
| title_sort |
post-translational modifications of circulating alpha-1-antitrypsin protein |
| publisher |
MDPI AG |
| series |
International Journal of Molecular Sciences |
| issn |
1661-6596 1422-0067 |
| publishDate |
2020-12-01 |
| description |
Alpha-1-antitrypsin (AAT), an acute-phase protein encoded by the <i>SERPINA1</i> gene, is a member of the serine protease inhibitor (SERPIN) superfamily. Its primary function is to protect tissues from enzymes released during inflammation, such as neutrophil elastase and proteinase 3. In addition to its antiprotease activity, AAT interacts with numerous other substances and has various functions, mainly arising from the conformational flexibility of normal variants of AAT. Therefore, AAT has diverse biological functions and plays a role in various pathophysiological processes. This review discusses major molecular forms of AAT, including complex, cleaved, glycosylated, oxidized, and S-nitrosylated forms, in terms of their origin and function. |
| topic |
alpha-1-antitrypsin AAT <i>SERPINA1</i> chronic obstructive pulmonary disease protease inhibitor S-nitrosylation |
| url |
https://www.mdpi.com/1422-0067/21/23/9187 |
| work_keys_str_mv |
AT urszulalechowicz posttranslationalmodificationsofcirculatingalpha1antitrypsinprotein AT stefanrudzinski posttranslationalmodificationsofcirculatingalpha1antitrypsinprotein AT aleksandrajezelastanek posttranslationalmodificationsofcirculatingalpha1antitrypsinprotein AT sabinajanciauskiene posttranslationalmodificationsofcirculatingalpha1antitrypsinprotein AT joannachorostowskawynimko posttranslationalmodificationsofcirculatingalpha1antitrypsinprotein |
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