Human platelet glycoprotein V

Its role in enhancing expression of the glycoprotein Ib receptor

David Calverley, M. Yagi, S. M. Stray, G. J. Roth

    Research output: Contribution to journalArticle

    37 Citations (Scopus)

    Abstract

    Platelet adhesion to an injured blood vessel well is a critical initiating step in hemostasis mediated by a four member receptor complex (glycoprotein Ib/V/IX) interacting with plasma von Willebrand factor (vWF). The function of the GPV subunit within this complex is presently undefined. To study the role of glycoprotein (GP) V within the GPIb receptor complex, we transfected the GPV subunit gene into a hematopoietic cell line that constitutively expresses the other three subunits (human erythroleukemia [HEL] cells). Using flow cytometry, we found transfected GPV was surface expressed in HEL cells; this, in turn, led to increased surface expression of the ligand-binding GPIbα and GPIX subunits. Radioligand binding assays showed that GPV-transfected HEL cells bound more vWF than their non- or mock-transfected counterparts. We employed confocal microscopy of GPV-transfected HEL cells to show that GPV colocalizes with GPIbα on the cell surface. These findings suggest that the GPV subunit plays a role within the GPIb receptor complex by enhancing Ibα surface expression.

    Original languageEnglish (US)
    Pages (from-to)1361-1367
    Number of pages7
    JournalBlood
    Volume86
    Issue number4
    StatePublished - 1995

    Fingerprint

    Platelet Glycoprotein GPIb-IX Complex
    Platelet Membrane Glycoproteins
    Leukemia, Erythroblastic, Acute
    von Willebrand Factor
    Flow cytometry
    Confocal microscopy
    Blood vessels
    Platelets
    Radioligand Assay
    Assays
    Glycoproteins
    Hemostasis
    Adhesion
    Confocal Microscopy
    Genes
    Cells
    Blood Vessels
    Ligands
    Flow Cytometry
    Plasmas

    ASJC Scopus subject areas

    • Hematology

    Cite this

    Calverley, D., Yagi, M., Stray, S. M., & Roth, G. J. (1995). Human platelet glycoprotein V: Its role in enhancing expression of the glycoprotein Ib receptor. Blood, 86(4), 1361-1367.

    Human platelet glycoprotein V : Its role in enhancing expression of the glycoprotein Ib receptor. / Calverley, David; Yagi, M.; Stray, S. M.; Roth, G. J.

    In: Blood, Vol. 86, No. 4, 1995, p. 1361-1367.

    Research output: Contribution to journalArticle

    Calverley, D, Yagi, M, Stray, SM & Roth, GJ 1995, 'Human platelet glycoprotein V: Its role in enhancing expression of the glycoprotein Ib receptor', Blood, vol. 86, no. 4, pp. 1361-1367.
    Calverley, David ; Yagi, M. ; Stray, S. M. ; Roth, G. J. / Human platelet glycoprotein V : Its role in enhancing expression of the glycoprotein Ib receptor. In: Blood. 1995 ; Vol. 86, No. 4. pp. 1361-1367.
    @article{f93ff5a725cd4b4faa97847e087f95b7,
    title = "Human platelet glycoprotein V: Its role in enhancing expression of the glycoprotein Ib receptor",
    abstract = "Platelet adhesion to an injured blood vessel well is a critical initiating step in hemostasis mediated by a four member receptor complex (glycoprotein Ib/V/IX) interacting with plasma von Willebrand factor (vWF). The function of the GPV subunit within this complex is presently undefined. To study the role of glycoprotein (GP) V within the GPIb receptor complex, we transfected the GPV subunit gene into a hematopoietic cell line that constitutively expresses the other three subunits (human erythroleukemia [HEL] cells). Using flow cytometry, we found transfected GPV was surface expressed in HEL cells; this, in turn, led to increased surface expression of the ligand-binding GPIbα and GPIX subunits. Radioligand binding assays showed that GPV-transfected HEL cells bound more vWF than their non- or mock-transfected counterparts. We employed confocal microscopy of GPV-transfected HEL cells to show that GPV colocalizes with GPIbα on the cell surface. These findings suggest that the GPV subunit plays a role within the GPIb receptor complex by enhancing Ibα surface expression.",
    author = "David Calverley and M. Yagi and Stray, {S. M.} and Roth, {G. J.}",
    year = "1995",
    language = "English (US)",
    volume = "86",
    pages = "1361--1367",
    journal = "Blood",
    issn = "0006-4971",
    publisher = "American Society of Hematology",
    number = "4",

    }

    TY - JOUR

    T1 - Human platelet glycoprotein V

    T2 - Its role in enhancing expression of the glycoprotein Ib receptor

    AU - Calverley, David

    AU - Yagi, M.

    AU - Stray, S. M.

    AU - Roth, G. J.

    PY - 1995

    Y1 - 1995

    N2 - Platelet adhesion to an injured blood vessel well is a critical initiating step in hemostasis mediated by a four member receptor complex (glycoprotein Ib/V/IX) interacting with plasma von Willebrand factor (vWF). The function of the GPV subunit within this complex is presently undefined. To study the role of glycoprotein (GP) V within the GPIb receptor complex, we transfected the GPV subunit gene into a hematopoietic cell line that constitutively expresses the other three subunits (human erythroleukemia [HEL] cells). Using flow cytometry, we found transfected GPV was surface expressed in HEL cells; this, in turn, led to increased surface expression of the ligand-binding GPIbα and GPIX subunits. Radioligand binding assays showed that GPV-transfected HEL cells bound more vWF than their non- or mock-transfected counterparts. We employed confocal microscopy of GPV-transfected HEL cells to show that GPV colocalizes with GPIbα on the cell surface. These findings suggest that the GPV subunit plays a role within the GPIb receptor complex by enhancing Ibα surface expression.

    AB - Platelet adhesion to an injured blood vessel well is a critical initiating step in hemostasis mediated by a four member receptor complex (glycoprotein Ib/V/IX) interacting with plasma von Willebrand factor (vWF). The function of the GPV subunit within this complex is presently undefined. To study the role of glycoprotein (GP) V within the GPIb receptor complex, we transfected the GPV subunit gene into a hematopoietic cell line that constitutively expresses the other three subunits (human erythroleukemia [HEL] cells). Using flow cytometry, we found transfected GPV was surface expressed in HEL cells; this, in turn, led to increased surface expression of the ligand-binding GPIbα and GPIX subunits. Radioligand binding assays showed that GPV-transfected HEL cells bound more vWF than their non- or mock-transfected counterparts. We employed confocal microscopy of GPV-transfected HEL cells to show that GPV colocalizes with GPIbα on the cell surface. These findings suggest that the GPV subunit plays a role within the GPIb receptor complex by enhancing Ibα surface expression.

    UR - http://www.scopus.com/inward/record.url?scp=0029129219&partnerID=8YFLogxK

    UR - http://www.scopus.com/inward/citedby.url?scp=0029129219&partnerID=8YFLogxK

    M3 - Article

    VL - 86

    SP - 1361

    EP - 1367

    JO - Blood

    JF - Blood

    SN - 0006-4971

    IS - 4

    ER -