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    The human CFTR protein expressed in CHO cells activates aquaporin-3 in a cAMP-dependent pathway: study by digital holographic microscopy

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    J Cell Sci-2014-Jourdain-546-56.pdf
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    Type
    Article
    Authors
    Jourdain, P.
    Becq, F.
    Lengacher, S.
    Boinot, C.
    Magistretti, Pierre J. cc
    Marquet, P.
    KAUST Department
    Biological and Environmental Sciences and Engineering (BESE) Division
    Bioscience Program
    Date
    2013-12-11
    Online Publication Date
    2013-12-11
    Print Publication Date
    2014-02-01
    Permanent link to this record
    http://hdl.handle.net/10754/555774
    
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    Abstract
    The transmembrane water movements during cellular processes and their relationship to ionic channel activity remain largely unknown. As an example, in epithelial cells it was proposed that the movement of water could be directly linked to cystic fibrosis transmembrane conductance regulator (CFTR) protein activity through a cAMP-stimulated aqueous pore, or be dependent on aquaporin. Here, we used digital holographic microscopy (DHM) an interferometric technique to quantify in situ the transmembrane water fluxes during the activity of the epithelial chloride channel, CFTR, measured by patch-clamp and iodide efflux techniques. We showed that the water transport measured by DHM is fully inhibited by the selective CFTR blocker CFTRinh172 and is absent in cells lacking CFTR. Of note, in cells expressing the mutated version of CFTR (F508del-CFTR), which mimics the most common genetic alteration encountered in cystic fibrosis, we also show that the water movement is profoundly altered but restored by pharmacological manipulation of F508del-CFTR-defective trafficking. Importantly, whereas activation of this endogenous water channel required a cAMP-dependent stimulation of CFTR, activation of CFTR or F508del-CFTR by two cAMP-independent CFTR activators, genistein and MPB91, failed to trigger water movements. Finally, using a specific small-interfering RNA against the endogenous aquaporin AQP3, the water transport accompanying CFTR activity decreased. We conclude that water fluxes accompanying CFTR activity are linked to AQP3 but not to a cAMP-stimulated aqueous pore in the CFTR protein.
    Citation
    The human CFTR protein expressed in CHO cells activates aquaporin-3 in a cAMP-dependent pathway: study by digital holographic microscopy 2013, 127 (3):546 Journal of Cell Science
    Publisher
    The Company of Biologists
    Journal
    Journal of Cell Science
    DOI
    10.1242/jcs.133629
    Additional Links
    http://jcs.biologists.org/cgi/doi/10.1242/jcs.133629
    ae974a485f413a2113503eed53cd6c53
    10.1242/jcs.133629
    Scopus Count
    Collections
    Articles; Biological and Environmental Science and Engineering (BESE) Division; Bioscience Program

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