@article{255,
  keywords = {Acetonitriles, Acute-Phase Reaction, alpha 1-Antitrypsin, Citrate (si)-Synthase, Hot Temperature, Humans, L-Lactate Dehydrogenase, Molecular Chaperones, Protein Folding, Proteins, Serine Proteinase Inhibitors},
  author = {Ferenc Zsila},
  title = {Inhibition of heat- and chemical-induced aggregation of various proteins reveals chaperone-like activity of the acute-phase component and serine protease inhibitor human α1-antitrypsin},
  abstract = {<p>In vitro chaperone-like activity of the serpin family member and plasma acute-phase component human alpha(1)-antitrypsin (AAT) has been shown for the first time. Results of light-scattering experiments demonstrated that AAT efficiently inhibits both heat- and chemical-induced aggregation of various test proteins including alcohol dehydrogenase, aldolase, carbonic anhydrase, catalase, citrate synthase, enolase, glutathione S-transferase, l-lactate dehydrogenase, and beta(L)-crystallin. The results suggest that the unique metastable serpin architecture enables dual function, protease inhibiton as well as chaperone activity and highlight the serpin superfamily as a possible source of additional intra- and extracellular chaperones (e.g. alpha(1)-antichymotrypsin). The present finding is surprising in the light of the well-known role of mutated forms of AAT and other serpins in the pathogenesis of diseases called serpinopathies that featured with aberrant conformational transitions and consequent self-aggregation of serpin proteins.</p>},
  year = {2010},
  journal = {Biochem Biophys Res Commun},
  volume = {393},
  pages = {242-7},
  month = {2010 Mar 5},
  issn = {1090-2104},
  doi = {10.1016/j.bbrc.2010.01.110},
}