These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Molecular mechanisms of fibrin gel clot retraction by platelets and cultured tumor cells.
    Author: Tanoue K, Katagiri Y, Suzuki H.
    Journal: Pol J Pharmacol; 1996; 48(3):341-3. PubMed ID: 9112674.
    Abstract:
    Using a new quantitative method, we compared the involvement of platelet alpha IIb beta 3 integrin in clot retraction with that in aggregation, and identified a receptor for fibrin gels on the cell surface in the nuclear cell-induced clot retraction. The platelets pretreated with thrombin in the presence of 4 mM EDTA at 37 degrees C completely lost aggregability in response to any agonist, while they were still able to retract clot, though to a less extent than controls. The clot retractions by these pretreated platelets as well as control platelets were inhibited by a monoclonal anti-beta 3 (T74) that also inhibits aggregation. These results suggest that a domain in alpha IIb beta 3 integrin involved in clot retraction is not exactly the same site involved in aggregation (the fibrinogen-binding site). C32TG cells expressing integrin alpha v beta 3 but not alpha IIb beta 3 complex showed an efficient clot retraction, which was inhibited by an anti-alpha v beta 3 antibody but not by Ro-43-5054, a potent inhibitor specific to platelet alpha IIb beta 3. When cDNA of beta 3 was transfected into 293 cells which otherwise lacked beta 3 and a retractile activity, the transfectants retracted significantly fibrin gels, which was specifically inhibited by the anti-beta 3 T74. These findings indicate that alpha v beta 3 is involved in mediating the clot retraction by tumor cells.
    [Abstract] [Full Text] [Related] [New Search]