Regular Article
Expression of αIIbβ3 Integrin (GPIIb-IIIa) in Myeloid Cell Lines and Normal CD34+/CD33+ Bone Marrow Cells

https://doi.org/10.1006/bcmd.1997.0153Get rights and content

Abstract

ABSTRACT: Regulation of myeloid cell proliferation and differentiation in the bone marrow is mediated, in part, by the interaction of integrins on early myeloid cells with the extracellular matrix proteins secreted by stromal cells. To further define adhesive protein receptors of early myeloid cells, we examined the expression of the integrin GPIIb-IIIa (αIIbβ3) in leukemic cell lines KG-1a, KG-1, and HL-60, that represent early stages of myeloid differentiation. All three cell lines expressed surface GPIIb-IIIa as measured by flow cytometry and by binding of125I-anti-GPIIb-IIIa monoclonal antibody. Preincubation of cells with human AB serum or platelet releasate increased GPIIb-IIIa surface expression. GPIIb transcripts were identified in all three cell lines by Northern blot analysis. Furthermore, we readily detected GPIIb transcripts in fluorescence activated cell sorted (FACS) myeloid cells from normal human bone marrow by RT-PCR. Cloning and sequencing of the PCR products established the identity of GPIIb transcripts in the leukemic cell lines and CD34+/CD33+ normal bone marrow cells. Since the normal myeloid cells also demonstrated markers corresponding to the maturational stage of KG-1a/KG-1 cells, we propose that GPIIb-IIIa may serve as a myeloid differentiation antigen and as a key integrin of myeloid precursors.

References (60)

  • S Tsai et al.

    Differential binding of erythroid and myeloid progenitors to fibroblasts and fibronectin

    Blood

    (1987)
  • N Kieffer et al.

    Expression of platelet glycoprotein Ib in HEL cells

    J Biol Chem

    (1986)
  • M Poncz et al.

    Structure of the platelet membrane glycoprotein IIb: homology to the α subunits of the vitronectin and fibronectin membrane receptors

    J Biol Chem

    (1987)
  • DW Cleveland et al.

    Number and evolutionary conservation of α-and_β-tubulin and cytoplasmic β and γ-actin genes using specific cloned cDNA probes

    Cell

    (1980)
  • HP Koeffler et al.

    Human myeloid leukemia cell lines: A review

    Blood

    (1980)
  • HP Koeffler et al.

    An undifferentiated variant derived from human acute myelogenous leukemia cell line (KG-1)

    Blood

    (1980)
  • Y Bai et al.

    Monoclonal antibodies specific for platelet glycoproteins react with monocytes

    Blood

    (1984)
  • JJ Burckhardt et al.

    Human blood monocytes and platelets share a cell surface component

    Blood

    (1982)
  • TD Geppert et al.

    Regulatory role of microfilaments in the induction of T4 cell proliferation and interleukin 2 production

    Cell Immunol

    (1990)
  • J-P Rosa et al.

    Processing and assembly of the integrin, glycoprotein IIb-IIIa, in HEL cells

    J Biol Chem

    (1989)
  • JS Bennett et al.

    Exposure of platelet fibrinogen receptors by ADP and epinephrine

    J Clin Invest

    (1979)
  • ZM Ruggeri et al.

    Glanzmanns thrombasthenia: deficient binding of von Willebrand factor to thrombin-stimulated platelets

    Proc Natl Acad Sci USA

    (1982)
  • Fujimoto et al.

    Thrombin induced exposure and prostacyclin inhibition of the receptor for factor VIII/von Willebrand factor on human platelets

    J Clin Invest

    (1982)
  • R Pytela et al.

    Platelet membrane glycoprotein IIb/IIIa: Member of a family of arg-gly-asp-specific adhesion receptors

    Science

    (1986)
  • JD Wencel-Drake et al.

    Localization of internal pools of membrane glycoproteins involved in platelet adhesive responses

    Am J Pathol

    (1986)
  • GF Burns et al.

    The IIb-IIIa glycoprotein complex that mediates platelet aggregation is directly implicated in leukocyte adhesion

    Cell

    (1980)
  • JA Mourik et al.

    Vascular endothelial cells synthesize a plasma membrane indistinguishable from platelet membrane glycoprotein IIb

    J Biol Chem

    (1985)
  • IF Charo et al.

    Platelet glycoproteins IIb and IIIa: Evidence for a family of immunologically and structurally related glycoproteins in mammalian cells

    Proc Natl Acad Sci USA

    (1986)
  • ME Helmer et al.

    The VLA protein family. Characterization of five distinct cell surface heterodimers each with a common 130,000 molecular weight β subunit

    J Biol Chem

    (1987)
  • Cited by (5)

    • The role of β3-integrins in tumor angiogenesis: Context is everything

      2011, Current Opinion in Cell Biology
      Citation Excerpt :

      β3-integrins are not restricted to neo-vascular ECs. β3-integrin is, for example, expressed in BMDCs [42,43] (including megakaryocytes where it is coupled with αIIb-integrin [44,45]) and in many tumor cells [46] all of which contribute to angiogenesis. Based on global knockout and inhibition studies, a combination of pro-angiogenic and anti-angiogenic roles for β3-integrin has been reported [6••,7••,18••,47,48,49•,50••,51].

    09/23/97

    f1

    Reprint request to: Lisa K. Jennings, Ph.D., Department of Medicine, Room A303, 956 Court Avenue, Memphis, Tennessee 38163. phone (901)448-5067, fax (901)448-7181, email: [email protected]

    View full text