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    A Role for Calcium-Activated Adenylate Cyclase and Protein Kinase A in the Lens Src Family Kinase and Na,K-ATPase Response to Hyposmotic Stress

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    Author
    Shahidullah, Mohammad
    Mandal, Amritlal
    Delamere, Nicholas A.
    Affiliation
    Univ Arizona, Dept Physiol
    Univ Arizona, Dept Ophthalmol & Vision Sci
    Issue Date
    2017-09-01
    Keywords
    calcium-activated adenylyl cyclase
    cAMP
    lens
    Na
    K-ATPase
    Src family kinase
    
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    Publisher
    ASSOC RESEARCH VISION OPHTHALMOLOGY INC
    Citation
    A Role for Calcium-Activated Adenylate Cyclase and Protein Kinase A in the Lens Src Family Kinase and Na,K-ATPase Response to Hyposmotic Stress 2017, 58 (11):4447 Investigative Opthalmology & Visual Science
    Journal
    Investigative Opthalmology & Visual Science
    Rights
    Copyright © 2017 The Authors. This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.
    Collection Information
    This item from the UA Faculty Publications collection is made available by the University of Arizona with support from the University of Arizona Libraries. If you have questions, please contact us at repository@u.library.arizona.edu.
    Abstract
    PURPOSE. Na, K-ATPase activity in lens epithelium is subject to control by Src family tyrosine kinases (SFKs). Previously we showed hyposmotic solution causes an SFK-dependent increase in Na, K-ATPase activity in the epithelium. Here we explored the role of cAMP in the signaling mechanism responsible for the SFK and Na, K-ATPase response. METHODS. Intact porcine lenses were exposed to hyposmotic Krebs solution (200 mOsm) then the epithelium was assayed for cAMP, SFK phosphorylation (activation) or Na, K-ATPase activity. RESULTS. An increase of cAMP was observed in the epithelium of lenses exposed to hyposmotic solution. In lenses exposed to hyposmotic solution SFK phosphorylation in the epithelium approximately doubled as did Na, K-ATPase activity and both responses were prevented by H89, a protein kinase A inhibitor. The magnitude of the SFK response to hyposmotic solution was reduced by a TRPV4 antagonist HC067047 added to prevent TRPV4-mediated calcium entry, and by a cytoplasmic Ca2+ chelator BAPTA-AM. The Na, K-ATPase activity response in the epithelium of lenses exposed to hyposmotic solution was abolished by BAPTA-AM. As a direct test of cAMP-dependent SFK activation, intact lenses were exposed to 8-pCPT-cAMP, a cell-permeable cAMP analog. 8-pCPT-cAMP caused robust SFK activation. Using Western blot, two calcium-activated adenylyl cyclases, ADCY3 and ADCY8, were detected in lens epithelium. CONCLUSIONS. Calcium-activated adenylyl cyclases are expressed in the lens epithelium and SFK activation is linked to a rise of cAMP that occurs upon hyposmotic challenge. The findings point to cAMP as a link between TRPV4 channel-mediated calcium entry, SFK activation, and a subsequent increase of Na, K-ATPase activity.
    Note
    Open access journal.
    ISSN
    1552-5783
    PubMed ID
    28863406
    DOI
    10.1167/iovs.17-21600
    Version
    Final published version
    Sponsors
    National Institutes of Health [EY 006915]
    Additional Links
    http://iovs.arvojournals.org/article.aspx?doi=10.1167/iovs.17-21600
    ae974a485f413a2113503eed53cd6c53
    10.1167/iovs.17-21600
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