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dc.rights.licenseCC BY — Creative Commons Attribution
dc.contributor.authorBhattacharyya, S.
dc.contributor.authorFeferman, L.
dc.contributor.authorHan, X.
dc.contributor.authorOuya, Y.
dc.contributor.authorZhang, F.
dc.contributor.authorLinhardt, Robert J.
dc.contributor.authorTobacman, J.K.
dc.date2018
dc.date.accessioned2022-06-21T16:48:58Z
dc.date.available2022-06-21T16:48:58Z
dc.date.issued2018
dc.identifier.citationDecline in arylsulfatase B (N-acetylgalactosamine-4-sulfatase) leads to increased EGFR expression due to SHP2 inhibition and JNK activation in prostate, S. Bhattacharyya, L. Feferman, X. Han, Y. Ouya, F. Zhang, R. J. Linhardt, J. K. Tobacman, Journal of Biological Chemistry, 293, 11076–11087, 2018.
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5073
dc.identifier.urihttps://doi.org/10.1074/jbc.RA117.001244
dc.descriptionJournal of Biological Chemistry, 293, 11076–11087
dc.descriptionNote : 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.
dc.description.abstractEpidermal growth factor receptor (EGFR) has a crucial role in cell differentiation and proliferation and cancer, and its expression appears to be up-regulated when arylsulfatase B (ARSB or GalNAc-4-sulfatase) is reduced. ARSB removes 4-sulfate groups from the nonreducing end of dermatan sulfate and chondroitin 4-sulfate (C4S), and its decreased expression has previously been reported to inhibit the activity of the ubiquitous protein-tyrosine phosphatase, nonreceptor type 11 (SHP2 or PTPN11). However, the mechanism by which decline in ARSB leads to decline in SHP2 activity is unclear. Here, we show that SHP2 binds preferentially C4S, rather than chondroitin 6-sulfate, and confirm that SHP2 activity declines when ARSB is silenced. The reduction in ARSB activity, and the resultant increase in C4S, increased the expression of EGFR (Her1/ErbB1) in human prostate stem and epithelial cells. The increased expression of EGFR occurred after 1) the decline in SHP2 activity, 2) enhanced c-Jun N-terminal kinase (JNK) activity, 3) increased nuclear DNA binding by c-Jun and c-Fos, and 4) EGFR promoter activation. In response to exogenous EGF, there was increased bromodeoxyuridine incorporation, consistent with enhanced cell proliferation. These findings indicated that ARSB and chondroitin 4-sulfation affect the activation of an important dual phosphorylation threonine–tyrosine kinase and the mRNA expression of a critical tyrosine kinase receptor in prostate cells. Restoration of ARSB activity with the associated reduction in C4S may provide a new therapeutic approach for managing malignancies in which EGFR-mediated tyrosine kinase signaling pathways are active.
dc.languageen_US
dc.language.isoENG
dc.publisherThe American Society for Biochemistry and Molecular Biology (ASBMB) and Elsevier
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.urihttps://harc.rpi.edu/
dc.rightsAttribution 3.0 United States*
dc.rights.urihttp://creativecommons.org/licenses/by/3.0/us/*
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleDecline in arylsulfatase B (N-acetylgalactosamine-4-sulfatase) leads to increased EGFR expression due to SHP2 inhibition and JNK activation in prostateen_US
dc.typeArticle
dcterms.accessRightsOpen Access
dcterms.accessRightsA full text version is available in DSpace@RPI
dcterms.isVersionOfhttps://doi.org/10.1074/jbc.RA117.001244
dc.rights.holderCC BY : this license allows reusers to distribute, remix, adapt, and build upon the material in any medium or format, so long as attribution is given to the creator. The license allows for commercial use. Credit must be given to the authors and the original work must be properly cited.
dc.creator.identifierhttps://orcid.org/0000-0003-2219-5833
dc.relation.departmentThe Linhardt Research Labs.
dc.relation.departmentThe Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)


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Except where otherwise noted, this item's license is described as CC BY — Creative Commons Attribution