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    The abnormal accumulation 1 of heparan sulfate in patients with mucopolysaccharidosis prevents the elastolytic activity of cathepsin V

    Author
    Chazeirat, T.; Denamur, S.; Bojarski, K.K.; Andrault, P.-M.; Sizaret, D.; Zhang, F.; Saidi, A.; Tardieu, M.; Linhardt, Robert J.; Labarthe, F.; Brömme, D.; Samsonov, S.A.; Lalmanach, G.; Lecaille, F.
    ORCID
    https://orcid.org/0000-0003-2219-5833
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    Other Contributors
    Date Issued
    2020
    Subject
    Biology; Chemistry and chemical biology; Chemical and biological engineering; Biomedical engineering
    Degree
    Terms of Use
    In Copyright : this Item is protected by copyright and/or related rights. You are free to use this Item in any way that is permitted by the copyright and related rights legislation that applies to your use. For other uses you need to obtain permission from the rights-holder(s). https://rightsstatements.org/page/InC/1.0/;
    Full Citation
    The abnormal accumulation 1 of heparan sulfate in patients with mucopolysaccharidosis prevents the elastolytic activity of cathepsin V, T. Chazeirat, S. Denamur, K. K. Bojarski, P.-M. Andrault, D. Sizaret, F. Zhang, A. Saidi, M. Tardieu, R. J. Linhardt, F. Labarthe, D. Brömme, S. A. Samsonov, G. Lalmanach, F. Lecaille, Carbohydrate Polymers, 253, 117261, 2020.
    Metadata
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    URI
    https://doi.org/10.1016/j.carbpol.2020.117261; https://hdl.handle.net/20.500.13015/5478
    Abstract
    Mucopolysaccharidosis (MPS) are rare inherited diseases characterized by accumulation of lysosomal glycosaminoglycans, including heparan sulfate (HS). Patients exhibit progressive multi-visceral dysfunction and shortened lifespan mainly due to a severe cardiac/respiratory decline. Cathepsin V (CatV) is a potent elastolytic protease implicated in extracellular matrix (ECM) remodeling. Whether CatV is inactivated by HS in lungs from MPS patients remained unknown. Herein, CatV colocalized with HS in MPS bronchial epithelial cells. HS level correlated positively with the severity of respiratory symptoms and negatively to the overall endopeptidase activity of cysteine cathepsins. HS bound tightly to CatV and impaired its activity. Withdrawal of HS by glycosidases preserved exogenous CatV activity, while addition of Surfen, a HS antagonist, restored elastolytic CatV-like activity in MPS samples. Our data suggest that the pathophysiological accumulation of HS may be deleterious for CatV-mediated ECM remodeling and for lung tissue homeostasis, thus contributing to respiratory disorders associated to MPS diseases.;
    Description
    Carbohydrate Polymers, 253, 117261; Note : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
    Department
    The Linhardt Research Labs.; The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS);
    Relationships
    The Linhardt Research Labs Online Collection; Rensselaer Polytechnic Institute, Troy, NY; https://harc.rpi.edu/;
    Access
    https://login.libproxy.rpi.edu/login?url=https://doi.org/10.1016/j.carbpol.2020.117261;
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