Mannosamine, a novel inhibitor of glycosylphosphatidylinositol incorporation into proteins. Academic Article uri icon

Overview

abstract

  • Mannosamine (2-amino-2-deoxy D-mannose) is shown here to block the incorporation of glycosylphosphatidylinositol (GPI) into GPI-anchored proteins. The amino sugar drastically reduced the surface expression of a recombinant GPI-anchored protein in polarized MDCK cells, converted this apical membrane-bound protein to an unpolarized secretory product and blocked the expression of endogenous GPI-anchored proteins. Furthermore, it specifically inhibited the incorporation of [3H]ethanolamine (a GPI component) into mammalian and trypanosomal GPI-anchored proteins and into a well characterized GPI-lipid of Trypanosoma brucei. These results suggest that mannosamine converted an apical GPI-anchored protein to a non-polarized secretory product by depleting transfer competent GPI-precursor lipids. Our inhibitor studies provide new independent evidence for the apical targeting role of GPI in polarized epithelia and open the way towards a greater understanding of the functional role of GPI in membrane trafficking and cell regulation.

publication date

  • August 1, 1991

Research

keywords

  • Glycolipids
  • Hexosamines
  • Phosphatidylinositols
  • Protozoan Proteins

Identity

PubMed Central ID

  • PMC452876

Scopus Document Identifier

  • 0025895044

Digital Object Identifier (DOI)

  • 10.1002/j.1460-2075.1991.tb07726.x

PubMed ID

  • 1829673

Additional Document Info

volume

  • 10

issue

  • 8