Association of GPI-anchored glycoproteins with other components of the leucocyte membrane

Braz J Med Biol Res. 1994 Feb;27(2):255-62.


The leucocyte surface glycosylphosphatidylinositol (GPI)-anchored membrane proteins are localized within specific membrane microdomains which also contain specific (glyco)lipids and intracellular proteins including protein kinases. These "GPI-domains" are devoid of most abundant transmembrane proteins, but in T-cells they appear to contain small amounts of CD4 and CD8 and in B-cell lines, small amounts of CD10. The existence of these relatively detergent-resistant membrane microdomains explains the signal-transducing ability of GPI-anchored receptors. In addition to the "GPI-microdomains", several other types of analogous very large detergent-resistant complexes/domains appear to exist, such as those containing T-cell receptor, others containing CD45R molecules associated with a protein kinase, and still others composed mainly of several proteins of the tetraspan family. Therefore, we suggest that the leucocyte surface is a mosaic of microdomains of unique composition associated with specific signal-transducing molecules.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antigens, CD / analysis*
  • Antigens, CD / chemistry
  • Antigens, Surface / analysis*
  • Antigens, Surface / chemistry
  • B-Lymphocytes / chemistry
  • B-Lymphocytes / immunology
  • Glycosylphosphatidylinositols / biosynthesis
  • Glycosylphosphatidylinositols / chemistry*
  • Humans
  • Leukocytes / chemistry*
  • Leukocytes / immunology
  • Membrane Glycoproteins / analysis*
  • Membrane Glycoproteins / chemistry
  • T-Lymphocytes / chemistry
  • T-Lymphocytes / immunology


  • Antigens, CD
  • Antigens, Surface
  • Glycosylphosphatidylinositols
  • Membrane Glycoproteins