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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred


IMPACT FACTOR 2018: 3.014
5-year IMPACT FACTOR: 3.162

CiteScore 2018: 3.09

SCImago Journal Rank (SJR) 2018: 1.482
Source Normalized Impact per Paper (SNIP) 2018: 0.820

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1437-4315
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Volume 385, Issue 9

Issues

Non-muscle α-actinin-4 interacts with plasminogen activator inhibitor type-1 (PAI-1)

Ulla Magdolen
  • Klinische Forschergruppe der Frauenklinik der Technischen Universität München, Klinikum rechts der Isar, Ismaninger str. 22, D-81675 München, Germany
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Florian Schroeck
  • Klinische Forschergruppe der Frauenklinik der Technischen Universität München, Klinikum rechts der Isar, Ismaninger str. 22, D-81675 München, Germany
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Sabine Creutzburg
  • Klinische Forschergruppe der Frauenklinik der Technischen Universität München, Klinikum rechts der Isar, Ismaninger str. 22, D-81675 München, Germany
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Manfred Schmitt
  • Klinische Forschergruppe der Frauenklinik der Technischen Universität München, Klinikum rechts der Isar, Ismaninger str. 22, D-81675 München, Germany
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Viktor Magdolen
  • Klinische Forschergruppe der Frauenklinik der Technischen Universität München, Klinikum rechts der Isar, Ismaninger str. 22, D-81675 München, Germany
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
Published Online: 2005-06-01 | DOI: https://doi.org/10.1515/BC.2004.105

Abstract

PAI-1 modulates many biological processes involving fibrinolysis, cell migration or tissue remodelling. In addition to inhibiting serine proteases (mainly tPA and uPA), PAI-1 interacts with vitronectin (Vn), fibrin or α(1)-acid glycoprotein, interactions which are important for PAI-1-mediated effects in inflammation, tumor invasion and metastasis. To further identify proteins interacting with PAI-1, the yeast two-hybrid strategy was employed. Screening of a human placenta cDNA library identified – in addition to the C-terminal region of cytokeratin 18 (CK18182-430) – a large C-terminal fragment of α-actinin-4 (Act-4) as a binding partner for PAI-1. Two different cDNA clones encoding Act-4287-911 and Act-4330-911, respectively, were isolated. An Act-4330-911/GST-fusion protein, but not GST alone, was immunoprecipitated together with active PAI-1. In solid phase binding assays, active wild-type PAI-1 as well as the PAI-1 variant Q123K (which does not interact with multimeric Vn) was found to bind to Act-4330-911/GST. Latent PAI-1, latent Q123K, and the inactive PAI-1 variant Q55P did not display any binding activity. Act-4 is mainly present intracellularly and is involved in cellular motility via interaction with the actin cytoskeleton, thus probably affecting the metastatic potential of tumor cells. However, an extracellular Act-4-derived fragment (mactinin) has previously been identified, which (i) is generated by proteolytic action of uPA, (ii) displays significant chemotactic activity for monocytes, and (iii) promotes monocyte/macrophage maturation. We suggest that PAI-1, via interaction with both Act-4 and uPA, may function as a modulator of this mononuclear phagocyte response, not only in inflammation but also in tumor invasion and metastasis.

Keywords: α-actinin; plasminogen activator inhibitor type 1; yeast two-hybrid system

About the article

Received: May 6, 2004

Accepted: July 5, 2004

Published Online: 2005-06-01

Published in Print: 2004-09-01


Citation Information: Biological Chemistry, Volume 385, Issue 9, Pages 801–808, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2004.105.

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