Glycosyl-Phosphatidylinositol Anchoring of Membrane Proteins

  • D. M. Lublin
Part of the Current Topics in Microbiology and Immunology book series (CT MICROBIOLOGY, volume 178)

Abstract

Three of the five complement regulatory proteins discussed in detail in other chapters of this volume are anchored to the plasma membrane through a glycosyl-phosphatidylinositol (GPI) structure; specifically, decay accelerating factor (DAF), membrane inhibitor of reactive lysis (MIRL), and homologous restriction factor (HRF). This GPI form of membrane anchoring has gone from being an unusual observation of the late 1970s relating to the release of a few hydrolytic enzymes (alkaline phosphatase, acetylcholinesterase, and 5´-nucleotidase) from plasma membranes by Pl-specific phospholipase C (PI-PLC) to recognition as a fairly common mode of membrane attachment (Low 1987). This is evidenced with almost every new issue of a journal and is reflected in the common use of this mode of attachment by cell membrane proteins, including complement regulatory proteins and other immunologically important molecules, e.g., Thy-1, one form of lymphocyte function-associated antigen 3 (LFA-3), and one form of IgG Fc receptor III.

Keywords

Arthritis Lymphoma Acetyl Oligosaccharide Galactose 

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Copyright information

© Springer-Verlag Berlin Heidelberg 1992

Authors and Affiliations

  • D. M. Lublin
    • 1
  1. 1.Division of Laboratory Medicine, Departments of Pathology and MedicineWashington University School of MedicineSt. LouisUSA

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