Selected article for: "biological role and diverse biological role"
Author: Lechowicz, Urszula; Rudzinski, Stefan; Jezela-Stanek, Aleksandra; Janciauskiene, Sabina; Chorostowska-Wynimko, Joanna
Title: Post-Translational Modifications of Circulating Alpha-1-Antitrypsin Protein
  • Cord-id: q96vk3t8
  • Document date: 2020_12_2
    • ID: q96vk3t8
    Snippet: Alpha-1-antitrypsin (AAT), an acute-phase protein encoded by the SERPINA1 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 bi
    Document: Alpha-1-antitrypsin (AAT), an acute-phase protein encoded by the SERPINA1 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.

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