Mechanisms involved in α6β1-integrin-mediated Ca signalling |
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| Authors: | Hella Sch ttelndreier, Barry V.L. Potter, Georg W. Mayr,Andreas H. Guse |
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| Affiliation: | a Institute for Medical Biochemistry and Molecular Biology, Division of Cellular Signal Transduction, University of Hamburg, University Hospital Eppendorf, Martinistr. 52, D-20246 Hamburg, Germany;b Wolfson Laboratory of Medicinal Chemistry, Department of Pharmacy and Pharmacology, University of Bath, Claverton Down, Bath BA2 7AY, UK |
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| Abstract: | Contact of Jurkat T-lymphocytes with the extracellular matrix (ECM) protein laminin resulted in long-lasting α6β1-integrin-mediated Ca2+ signalling. Both Ca2+ release from thapsigargin-sensitive Ca2+ stores and capacitative Ca2+ entry via Ca2+ channels sensitive to SKF 96365 constitute important parts of this process. Inhibition of α6β1-integrin-mediated Ca2+ signalling by (1) the src kinase inhibitor PP2, (2) the PLC inhibitor U73122, and (3) the cyclic adenosine diphosphoribose (cADPR) antagonist 7-deaza-8-Br-cADPR indicate the involvement of src tyrosine kinases and the Ca2+-releasing second messengers d-myo-inositol 1,4,5-trisphosphate (InsP3) and cADPR. |
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| Keywords: | Integrin Extracellular matrix Ca2+ signalling Inositol 1,4,5-trisphosphate Cyclic ADP-ribose Capacitative Ca2+ entry SKF 96365 |
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