The macrophage/endothelial cell mannose receptor cDNA encodes a protein that binds oligosaccharides terminating with SO4-4-GalNAcβ1,4GIcNAcaβ or Man at independent sites

Dorothy Fiete, Mary C. Beranek, Jacques U. Baenziger

Research output: Contribution to journalArticle

71 Scopus citations

Abstract

Lutropin (LH) and other glycoproteins bearing oligosaccharides with the terminal sequence SO4-4-GalNAcβ1,4GlcNAcβ1,4Man- (84GGnM) are rapidly removed from the circulation by an S4GGnM-specific receptor (84GGnM-R) expressed at the surface of hepatic endothelial cells. The 84GGnM-R isolated from rat liver is closely related to the macrophage mannose-specific receptor (Man-R) isolated from rat lung both antigenically and structurally. The 84GGnM-R and Man-R isolated from these tissues nonetheless differ in their ability to bind ligands bearing terminal GalNAc-4-SO4 or Man. In this paper, we have explored the structural relationship between the Man-R and the 84GGnM-R by examining the properties of the recombinant Man-R in the form of a transmembrane protein and a soluble chimeric fusion protein in which the transmembrane and cytosolic domains have been replaced by the Fc region of human IgG1. Like the S4GGnM-R isolated from liver, the chimeric fusion protein is able to bind ligands terminating with GalNAc-4-SO4 and Man at independent sites. When expressed in CHO cells the recombinant Man-R is able to mediate the uptake of ligands bearing either terminal Gal-NAc-4-SO4 or terminal Man. We propose that the Man-R be renamed the Man/S4GGnM receptor on the basis of its multiple and independent specificities.

Original languageEnglish
Pages (from-to)11256-11261
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume94
Issue number21
StatePublished - Oct 14 1997

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