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This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Larrucea, S. Articles by Parrilla, R. Search for Related Content PubMed PubMed Citation Articles by Larrucea, S. Articles by Parrilla, R. Related Collections Hemostasis, Thrombosis, and Vascular Biology Signal Transduction Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  Blood, 15 April 2002, Vol. 99, No. 8, pp. 2819-2827 HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY Agonist-induced aggregation of Chinese hamster ovary cells coexpressing the human receptors for fibrinogen (integrin IIb3) and the platelet-activating factor: dissociation between adhesion and aggregation Susana Larrucea, Consuelo González-Manchón, Nora Butta, Elena G. Arias-Salgado, Linnan Shen, Matilde S. Ayuso, and Roberto Parrilla From the Department of Physiopathology and Human Molecular Genetics, Centro de Investigaciones Biológicas (CSIC), Madrid, Spain. This work reports the establishment of a Chinese hamster ovary (CHO) cell line stably coexpressing the human IIb3 integrin and the platelet-activating factor receptor (PAFR). These cells aggregate in response to PAF in a Ca++, IIb3, and soluble fibrinogen (Fg)-dependent manner that is prevented by PAF antagonists or IIb3 blockade. The aggregating response is accompanied by enhanced binding of fibrinogen and the activation-dependent IgM PAC1. This model has permitted us to identify, for the first time, intracellular signals distinctly associated with either IIb3-mediated adhesion or aggregation. Nonreceptor activation of protein kinase C (PKC) by phorbol ester produced cellular adhesion and spreading onto immobilized Fg, but it was not a sufficient signal to provoke cellular aggregation. Moreover, inhibition of PKC impeded the PAF stimulation of cellular adhesion, whereas the aggregation was not prevented. The PAF-induced cellular aggregation was distinctly associated with signaling events arising from the liganded Fg receptor and the agonist-induced stimulation of a calcium/calmodulin-dependent signaling pathway. Sustained tyrosine phosphorylation of both mitogen-activated protein kinase (MAPK) and an approximately 100-kd protein was associated with the PAF-induced aggregation, whereas phosphorylation of focal adhesion kinase (FAK) was preferably associated with cellular adherence and spreading onto immobilized Fg. © 2002 by The American Society of Hematology.   CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: C.-F. Hsieh, B.-J. Chang, C.-H. Pai, H.-Y. Chen, J.-W. Tsai, Y.-H. Yi, Y.-T. Chiang, D.-W. Wang, S. Chi, L. Hsu, et al. Stepped Changes of Monovalent Ligand-binding Force during Ligand-induced Clustering of Integrin {alpha}IIBbeta3 J. Biol. Chem., September 1, 2006; 281(35): 25466 - 25474. [Abstract] [Full Text] [PDF]

	Copyright © 2002 by American Society of Hematology         Online ISSN: 1528-0020