Go to JCI Insight
  • About
  • Editors
  • Consulting Editors
  • For authors
  • Publication ethics
  • Alerts
  • Advertising
  • Job board
  • Subscribe
  • Contact
  • Current issue
  • Past issues
  • By specialty
    • COVID-19
    • Cardiology
    • Gastroenterology
    • Immunology
    • Metabolism
    • Nephrology
    • Neuroscience
    • Oncology
    • Pulmonology
    • Vascular biology
    • All ...
  • Videos
    • Conversations with Giants in Medicine
    • Author's Takes
  • Reviews
    • View all reviews ...
    • Immune Environment in Glioblastoma (Feb 2023)
    • Korsmeyer Award 25th Anniversary Collection (Jan 2023)
    • Aging (Jul 2022)
    • Next-Generation Sequencing in Medicine (Jun 2022)
    • New Therapeutic Targets in Cardiovascular Diseases (Mar 2022)
    • Immunometabolism (Jan 2022)
    • Circadian Rhythm (Oct 2021)
    • View all review series ...
  • Viewpoint
  • Collections
    • In-Press Preview
    • Commentaries
    • Research letters
    • Letters to the editor
    • Editorials
    • Viewpoint
    • Top read articles
  • Clinical Medicine
  • JCI This Month
    • Current issue
    • Past issues

  • Current issue
  • Past issues
  • Specialties
  • Reviews
  • Review series
  • Conversations with Giants in Medicine
  • Author's Takes
  • In-Press Preview
  • Commentaries
  • Research letters
  • Letters to the editor
  • Editorials
  • Viewpoint
  • Top read articles
  • About
  • Editors
  • Consulting Editors
  • For authors
  • Publication ethics
  • Alerts
  • Advertising
  • Job board
  • Subscribe
  • Contact
Platelet glycoproteins Ia, Ic, and IIa are physicochemically indistinguishable from the very late activation antigens adhesion-related proteins of lymphocytes and other cell types.
K D Pischel, … , H G Bluestein, V L Woods Jr
K D Pischel, … , H G Bluestein, V L Woods Jr
Published February 1, 1988
Citation Information: J Clin Invest. 1988;81(2):505-513. https://doi.org/10.1172/JCI113348.
View: Text | PDF
Research Article

Platelet glycoproteins Ia, Ic, and IIa are physicochemically indistinguishable from the very late activation antigens adhesion-related proteins of lymphocytes and other cell types.

  • Text
  • PDF
Abstract

The very late activation antigens (VLA) are a subset of the superfamily of cell surface glycoproteins that serve as receptors from extracellular matrix proteins. One or more of the VLA heterodimers are present on T lymphocytes and most other cell types, including platelets. We have used VLA-specific monoclonal antibodies to isolate the reactive platelet membrane molecules. We have identified them as previously characterized platelet surface glycoproteins and have compared them with VLA molecules isolated from lymphocytes and other cells. Utilizing one-dimensional SDS-PAGE, two-dimensional O'Farrell gel electrophoresis, and nonreduced-reduced two-dimensional gel electrophoresis, we show that reduced VLA molecules of platelets are composed of three chains of molecular weights 165,000, 145,000, and 140,000 that possess the physicochemical properties of platelet glycoproteins GPIa, GPIc alpha, and GPIIa. GPIa corresponds to the VLA 165,000 alpha 2-chain, GPIIa corresponds to a 145,000 Mr VLA beta-chain, and GPIc alpha corresponds to a 140,000 Mr VLA alpha-chain. The polypeptide structure of VLA molecules on platelets and lymphocytes are very similar or identical. Platelet proteins GPIa and GPIIa exist as a mixed heterodimer in detergent lysates and correspond with the VLA-2 heterodimer found on activated T lymphocytes and other cell types. The platelet glycoproteins GPIIa and GPIc form a second mixed heterodimer. The mAb A-1A5, which binds to the VLA beta chain, binds to platelet GPIIa and precipitates both the GPIIa-GPIa and GPIIa-GPIc heterodimers, and binds to 4,926 +/- 740 sites per platelet. A VLA-2-specific mAb, 12F1, which binds to the VLA alpha 2-chain reacts with GPIa and immunoprecipitates only the GPIIa-GPIa heterodimer, and binds to 1,842 +/- 449 sites per platelet. The similarity of VLA chains and platelet GPIIa, GPIa, and GPIc molecules suggests that these molecules may have similar functions on various cell types.

Authors

K D Pischel, H G Bluestein, V L Woods Jr

×

Full Text PDF | Download (2.82 MB)


Copyright © 2023 American Society for Clinical Investigation
ISSN: 0021-9738 (print), 1558-8238 (online)

Sign up for email alerts