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Potential Role of Kringle-Integrin Interaction in Plasmin and uPA Actions (A Hypothesis)
Author
Source
Journal of Biomedicine and Biotechnology
Issue
Vol. 2012, Issue 2012 (31 Dec. 2012), pp.1-8, 8 p.
Publisher
Hindawi Publishing Corporation
Publication Date
2012-10-16
Country of Publication
Egypt
No. of Pages
8
Main Subjects
Abstract EN
We previously showed that the kringle domains of plasmin and angiostatin, the N-terminal four kringles (K1–4) of plasminogen, directly bind to integrins.
Angiostatin blocks tumor-mediated angiogenesis and has great therapeutic potential.
Angiostatin binding to integrins may be related to the antiinflammatory action of angiostatin.
We reported that plasmin induces signals through protease-activated receptor (PAR-1), and plasmin-integrin interaction may be required for enhancing plasmin concentration on the cell surface, and enhances its signaling function.
Angiostatin binding to integrin does not seem to induce proliferative signals.
One possible mechanism of angiostatin's inhibitory action is that angiostatin suppresses plasmin-induced PAR-1 activation by competing with plasmin for binding to integrins.
Interestingly, plasminogen did not interact with αvβ3, suggesting that the αvβ3-binding sites in the kringle domains of plasminogen are cryptic.
The kringle domain of urokinase-type plasminogen activator (uPA) also binds to integrins.
The uPA-integrin interaction enhances uPA concentrations on the cell surface and enhances plasminogen activation on the cell surface.
It is likely that integrins bind to the kringle domain, and uPAR binds to the growth factor-like domain (GFD) of uPA simultaneously, making the uPAR-uPA-integrin ternary complex.
We present a docking model of the ternary complex.
American Psychological Association (APA)
Takada, Yoshikazu. 2012. Potential Role of Kringle-Integrin Interaction in Plasmin and uPA Actions (A Hypothesis). Journal of Biomedicine and Biotechnology،Vol. 2012, no. 2012, pp.1-8.
https://search.emarefa.net/detail/BIM-448560
Modern Language Association (MLA)
Takada, Yoshikazu. Potential Role of Kringle-Integrin Interaction in Plasmin and uPA Actions (A Hypothesis). Journal of Biomedicine and Biotechnology No. 2012 (2012), pp.1-8.
https://search.emarefa.net/detail/BIM-448560
American Medical Association (AMA)
Takada, Yoshikazu. Potential Role of Kringle-Integrin Interaction in Plasmin and uPA Actions (A Hypothesis). Journal of Biomedicine and Biotechnology. 2012. Vol. 2012, no. 2012, pp.1-8.
https://search.emarefa.net/detail/BIM-448560
Data Type
Journal Articles
Language
English
Notes
Includes bibliographical references
Record ID
BIM-448560