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    Ptprb protein tyrosine phosphatase receptor type B [ Mus musculus (house mouse) ]

    Gene ID: 19263, updated on 28-Oct-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Heterogeneity of endothelial VE-PTP downstream polarization, Tie2 activation, junctional claudin-5, and permeability in the aorta and vena cava.

    Heterogeneity of endothelial VE-PTP downstream polarization, Tie2 activation, junctional claudin-5, and permeability in the aorta and vena cava.
    Baluk P, Shirakura K, Vestweber D, McDonald DM., Free PMC Article

    01/11/2024
    Shear stress control of vascular leaks and atheromas through Tie2 activation by VE-PTP sequestration.

    Shear stress control of vascular leaks and atheromas through Tie2 activation by VE-PTP sequestration.
    Shirakura K, Baluk P, Nottebaum AF, Ipe U, Peters KG, McDonald DM, Vestweber D., Free PMC Article

    04/14/2023
    The Tyrosine Phosphatase hPTPRbeta Controls the Early Signals and Dopaminergic Cells Viability via the P2X7 Receptor.

    The Tyrosine Phosphatase hPTPRβ Controls the Early Signals and Dopaminergic Cells Viability via the P2X(7) Receptor.
    Bernal FL, Luque Montoro M, Arrazola Sastre A, Lacerda HM, Zugaza JL., Free PMC Article

    01/15/2022
    The study provides evidence that PTPRB is an important regulator of TEK signaling in the aqueous humor outflow pathway, and it identifies a new therapeutic target for treatment of glaucoma.

    Targeting the vascular-specific phosphatase PTPRB protects against retinal ganglion cell loss in a pre-clinical model of glaucoma.
    Thomson BR, Carota IA, Souma T, Soman S, Vestweber D, Quaggin SE., Free PMC Article

    05/9/2020
    This study provides the evidence to support a model whereby VE-PTP is a driver of diabetic nephropathy and shows that VE-PTP inhibition is a promising vasculoprotective strategy for the kidney in diabetes.

    Targeting VE-PTP phosphatase protects the kidney from diabetic injury.
    Carota IA, Kenig-Kozlovsky Y, Onay T, Scott R, Thomson BR, Souma T, Bartlett CS, Li Y, Procissi D, Ramirez V, Yamaguchi S, Tarjus A, Tanna CE, Li C, Eremina V, Vestweber D, Oladipupo SS, Breyer MD, Quaggin SE., Free PMC Article

    05/9/2020
    VEPTP (vascular endothelial protein tyrosine phosphatase) determines TIE2 response to ANGPT2. VEPTP is absent from lymphatic endothelium in mouse in vivo, permitting ANGPT2/TIE2-mediated lymphangiogenesis.

    Context-dependent functions of angiopoietin 2 are determined by the endothelial phosphatase VEPTP.
    Souma T, Thomson BR, Heinen S, Carota IA, Yamaguchi S, Onay T, Liu P, Ghosh AK, Li C, Eremina V, Hong YK, Economides AN, Vestweber D, Peters KG, Jin J, Quaggin SE., Free PMC Article

    08/4/2018
    PTPRB regulates branching morphogenesis in the mammary epithelium by modulating the response of the FGFR signalling pathway to FGF stimulation

    The receptor protein tyrosine phosphatase PTPRB negatively regulates FGF2-dependent branching morphogenesis.
    Soady KJ, Tornillo G, Kendrick H, Meniel V, Olijnyk-Dallis D, Morris JS, Stein T, Gusterson BA, Isacke CM, Smalley MJ., Free PMC Article

    11/11/2017
    STIM1-induced Ca(2+) signaling activates Pyk2 to inhibit the interaction of VE-PTP and VE-cadherin and hence increase endothelial permeability.

    Pyk2 phosphorylation of VE-PTP downstream of STIM1-induced Ca(2+) entry regulates disassembly of adherens junctions.
    Soni D, Regmi SC, Wang DM, DebRoy A, Zhao YY, Vogel SM, Malik AB, Tiruppathi C., Free PMC Article

    08/5/2017
    In the absence of Tie-2, VE-PTP inhibition destabilizes endothelial barrier integrity in agreement with the VE-cadherin-supportive effect of VE-PTP.

    Interfering with VE-PTP stabilizes endothelial junctions in vivo via Tie-2 in the absence of VE-cadherin.
    Frye M, Dierkes M, Küppers V, Vockel M, Tomm J, Zeuschner D, Rossaint J, Zarbock A, Koh GY, Peters K, Nottebaum AF, Vestweber D., Free PMC Article

    05/28/2016
    The Lewis X epitope is mainly expressed on phosphacan/receptor protein tyrosine phosphatase beta (RPTPbeta) in the developing mouse brain.

    Major glycan structure underlying expression of the Lewis X epitope in the developing brain is O-mannose-linked glycans on phosphacan/RPTPβ.
    Yaji S, Manya H, Nakagawa N, Takematsu H, Endo T, Kannagi R, Yoshihara T, Asano M, Oka S.

    12/5/2015
    VE-PTP activates TIE2 and stabilizes retinal and choroidal blood vessels

    Targeting VE-PTP activates TIE2 and stabilizes the ocular vasculature.
    Shen J, Frye M, Lee BL, Reinardy JL, McClung JM, Ding K, Kojima M, Xia H, Seidel C, Lima e Silva R, Dong A, Hackett SF, Wang J, Howard BW, Vestweber D, Kontos CD, Peters KG, Campochiaro PA., Free PMC Article

    02/14/2015
    We suggest that lymphocyte binding to vascular cell adhesion molecule 1 triggers a signaling process that enables a VE-PTP substrate to dissociate VE-PTP from VE-cadherin, thereby facilitating efficient transmigration.

    How T cells trigger the dissociation of the endothelial receptor phosphatase VE-PTP from VE-cadherin.
    Vockel M, Vestweber D.

    11/23/2013
    We conclude that the role of Tie2 in maintenance of vascular quiescence involves VE-PTP-dependent dephosphorylation of VEGF receptor-2, and that VEGF receptor-2 activity regulates VE-cadherin tyrosine phosphorylation, endothelial cell polarity

    VE-PTP regulates VEGFR2 activity in stalk cells to establish endothelial cell polarity and lumen formation.
    Hayashi M, Majumdar A, Li X, Adler J, Sun Z, Vertuani S, Hellberg C, Mellberg S, Koch S, Dimberg A, Koh GY, Dejana E, Belting HG, Affolter M, Thurston G, Holmgren L, Vestweber D, Claesson-Welsh L., Free PMC Article

    10/26/2013
    IGFBP-2 bound receptor protein tyrosine phosphatase beta, which led to its dimerization and inactivation. Analysis of aortas obtained from IGFBP-2(-/-) mice showed that receptor protein tyrosine phosphatase beta was activated.

    Insulin-like growth factor (IGF) binding protein 2 functions coordinately with receptor protein tyrosine phosphatase β and the IGF-I receptor to regulate IGF-I-stimulated signaling.
    Shen X, Xi G, Maile LA, Wai C, Rosen CJ, Clemmons DR., Free PMC Article

    01/5/2013
    Suggest that VE-PTP, in cooperation with integrins, regulates the spreading and migration of endothelial cells during angiogenesis.

    Promotion of cell spreading and migration by vascular endothelial-protein tyrosine phosphatase (VE-PTP) in cooperation with integrins.
    Mori M, Murata Y, Kotani T, Kusakari S, Ohnishi H, Saito Y, Okazawa H, Ishizuka T, Mori M, Matozaki T.

    05/31/2010
    Dissociation of VE-PTP from VE-cadherin triggers the activation of Tie-2, leading to enhanced endothelial cell proliferation and enlargement of vascular structures through activation of Erk1/2.

    VE-PTP controls blood vessel development by balancing Tie-2 activity.
    Winderlich M, Keller L, Cagna G, Broermann A, Kamenyeva O, Kiefer F, Deutsch U, Nottebaum AF, Vestweber D., Free PMC Article

    01/21/2010
    Data show that leukocytes interacting with endothelial cells rapidly dissociate VE-PTP from VE-cadherin, weakening endothelial cell contacts via a mechanism that requires plakoglobin but not beta-catenin.

    VE-PTP maintains the endothelial barrier via plakoglobin and becomes dissociated from VE-cadherin by leukocytes and by VEGF.
    Nottebaum AF, Cagna G, Winderlich M, Gamp AC, Linnepe R, Polaschegg C, Filippova K, Lyck R, Engelhardt B, Kamenyeva O, Bixel MG, Butz S, Vestweber D., Free PMC Article

    01/21/2010
    expression of Ptprb in mouse brain after chronic morphine treatment was found to be up-regulated in some brain regions

    Association of PTPRB gene polymorphism with drug addiction.
    Ishiguro H, Gong JP, Hall FS, Arinami T, Uhl GR.

    01/21/2010
    the activity of VE-PTP is not required for the initial formation of blood vessels, yet it is essential for their maintenance and remodeling.

    Vascular endothelial cell-specific phosphotyrosine phosphatase (VE-PTP) activity is required for blood vessel development.
    Bäumer S, Keller L, Holtmann A, Funke R, August B, Gamp A, Wolburg H, Wolburg-Buchholz K, Deutsch U, Vestweber D.

    01/21/2010
    Data show that vascular endothelial protein tyrosine phosphatase (VE-PTP) is a transmembrane binding partner of VE-cadherin that reduces the tyrosine phosphorylation of VE-cadherin and cell layer permeability.

    VE-PTP and VE-cadherin ectodomains interact to facilitate regulation of phosphorylation and cell contacts.
    Nawroth R, Poell G, Ranft A, Kloep S, Samulowitz U, Fachinger G, Golding M, Shima DT, Deutsch U, Vestweber D., Free PMC Article

    01/21/2010
    Vascular endothelial tyrosine phosphatase (VE-PTP)-null mice undergo vasculogenesis but die embryonically because of defects in angiogenesis.

    Vascular endothelial tyrosine phosphatase (VE-PTP)-null mice undergo vasculogenesis but die embryonically because of defects in angiogenesis.
    Dominguez MG, Hughes VC, Pan L, Simmons M, Daly C, Anderson K, Noguera-Troise I, Murphy AJ, Valenzuela DM, Davis S, Thurston G, Yancopoulos GD, Gale NW., Free PMC Article

    01/21/2010
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