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    UCHL1, a deubiquitinating enzyme, regulates lung endothelial cell permeability in vitro and in vivo

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    Name:
    UCHL1 paper-AJPLung-9Oct20-FOR ...
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    Author
    Mitra, Sumegha
    Epshtein, Yulia
    Sammani, Saad
    Quijada, Hector
    Chen, Weiguo
    Bandela, Mounica
    Desai, Ankit A
    Garcia, Joe G N
    Jacobson, Jeffrey R
    Affiliation
    Department of Medicine, Arizona Health Sciences Center, University of Arizona
    Issue Date
    2021-01-13
    Keywords
    UCHL1
    VE-cadherin
    adherens junction
    claudin-5
    endothelial cells
    lung vascular permeability
    Tight Junction
    
    Metadata
    Show full item record
    Publisher
    American Physiological Society
    Citation
    Mitra, S., Epshtein, Y., Sammani, S., Quijada, H., Chen, W., Bandela, M., ... & Jacobson, J. R. (2021). UCHL1, a deubiquitinating enzyme, regulates lung endothelial cell permeability in vitro and in vivo. American Journal of Physiology-Lung Cellular and Molecular Physiology, 320(4), L497-L507.
    Journal
    American journal of physiology. Lung cellular and molecular physiology
    Rights
    Copyright © 2021 the American Physiological Society.
    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
    Increasing evidence suggests an important role for deubiquitinating enzymes (DUBs) in modulating a variety of biological functions and diseases. We previously identified the upregulation of the DUB ubiquitin carboxyl terminal hydrolase 1 (UCHL1) in murine ventilator-induced lung injury (VILI). However, the role of UCHL1 in modulating vascular permeability, a cardinal feature of acute lung injury (ALI) in general, remains unclear. We investigated the role of UCHL1 in pulmonary endothelial cell (EC) barrier function in vitro and in vivo and examined the effects of UCHL1 on VE-cadherin and claudin-5 regulation, important adherens and tight junctional components, respectively. Measurements of transendothelial electrical resistance confirmed decreased barrier enhancement induced by hepatocyte growth factor (HGF) and increased thrombin-induced permeability in both UCHL1-silenced ECs and in ECs pretreated with LDN-57444 (LDN), a pharmacological UCHL1 inhibitor. In addition, UCHL1 knockdown (siRNA) was associated with decreased expression of VE-cadherin and claudin-5, whereas silencing of the transcription factor FoxO1 restored claudin-5 levels. Finally, UCHL1 inhibition in vivo via LDN was associated with increased VILI in a murine model. These findings support a prominent functional role of UCHL1 in regulating lung vascular permeability via alterations in adherens and tight junctions and implicate UCHL1 as an important mediator of ALI.
    Note
    12 month embargo; published online 31 March 2021
    EISSN
    1522-1504
    PubMed ID
    33438509
    DOI
    10.1152/ajplung.00492.2020
    Version
    Final accepted manuscript
    ae974a485f413a2113503eed53cd6c53
    10.1152/ajplung.00492.2020
    Scopus Count
    Collections
    UA Faculty Publications

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