Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form
As of April 1st VIVO Scientific Profiles will no longer updated for faculty, and the link to VIVO will be removed from the library website. Faculty profile pages will continue to be updated via Interfolio. VIVO will continue being used behind the scenes to update graduate student profiles. Please contact helplib@scripps.edu if you have questions.
How to download citations from VIVO | Alternative profile options

A thy-1 negative lymphoma cell variant defective in the formation of glycosyl-phosphatidylinositol membrane-protein anchors

Academic Article
uri icon
  • Overview
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

authors

  • Teng, M. H.
  • Hedayati, S.
  • Alexander, A. A.
  • Barkin, R.
  • Basch, R. S.
  • Buxbaum, Joel

publication date

  • April 1989

journal

  • Molecular Immunology  Journal

abstract

  • Thy-1 is a glycoprotein present on the membrane of murine cells of the T-lineage. The mature Thy-1 is anchored to the membrane via a glycolipid, phosphatidylinositide. In order to study the regulation of the synthesis and membrane insertion of this protein, the biochemical properties of a Thy-1.2 negative variant T-lymphoma cell (RL male 1.4) were studied. It contains intracellular Thy-1 protein but fails to express it on the cell surface. While the wild type and the mutant show similar labelling of the intracellular Thy-1 glycoprotein with amino acids, no ethanolamine is incorporated into the Thy-1 molecule of RL male 1.4. A plasmid, pT1, containing the normal Thy-1.2 gene and bacterial gpt gene was transfected into RL male 1.4 and into the murine plasmacytoma cell, J558L. A transfected plasmacytoma, T1J2, synthesized a normal sized Thy-1 protein and displayed the antigen on the membrane. In contrast, the mycophenolic acid resistant RL male 1.4 transfectants did not display Thy-1.2 on the cell surface, despite the presence of substantial amounts of Thy-1 intracellularly. Two other antigens known to be anchored in the membrane by phospholipid, Ly-6e and Qa-2, were also examined in RL male 1.4. RL male 1.4 did not express Ly-6e after alpha interferon induction. In addition, the expression of Qa-2 antigen was greatly diminished in RL male 1.4 in comparison to RL male 1.3. Thus, the defect in RL male 1.4 is not restricted to Thy-1.2, but includes other similarly anchored glycoproteins as well. This implies that the addition of phospholipid to core proteins is similar, if not identical, for all these molecules and that the RL male 1.4 cell lacks the capacity to from the lipid glycoprotein linkage required for the expression of these proteins on the cell surface.

subject areas

  • Animals
  • Antigens, Surface
  • Antigens, Thy-1
  • Cell Line
  • Cloning, Molecular
  • Genes
  • Glycolipids
  • Glycosylphosphatidylinositols
  • Immunoblotting
  • Lymphoma
  • Membrane Proteins
  • Mice
  • Mice, Inbred BALB C
  • Phosphatidylinositols
  • Plasmids
  • T-Lymphocytes
  • Transfection
  • Tumor Cells, Cultured
scroll to property group menus

Identity

International Standard Serial Number (ISSN)

  • 0161-5890

PubMed ID

  • 2566113
scroll to property group menus

Additional Document Info

start page

  • 391

end page

  • 402

volume

  • 26

issue

  • 4

©2022 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support