Isolation of the SO4-4-GalNAcbeta1,4GlcNAcbeta1,2Manalpha-specific receptor from rat liver.

The Journal of Biological Chemistry
D Fiete, J U Baenziger

Abstract

Glycoproteins, such as the glycoprotein hormone lutropin (LH), bear oligosaccharides terminating with the sequence SO4-4GalNAcbeta1, 4GlcNAcbeta1,2Manalpha (S4GGnM) and are rapidly removed from the circulation by a receptor present in hepatic endothelial cells and Kupffer cells. Rapid removal from the circulation is essential for attaining maximal hormone activity in vivo. We have isolated a protein from rat liver which has the properties expected for the S4GGnM-specific receptor (S4GGnM-R). The S4GGnM-R is closely related to the macrophage mannose receptor (Man-R) both antigenically and structurally. At least 12 peptides prepared from the S4GGnM-R have amino acid sequences that are identical to those of the Man-R. Nonetheless, the ligand binding properties of the S4GGnM-R and the Man-R differ in a number of respects. The S4GGnM-R binds to immobilized LH but not to immobilized mannose, whereas the Man-R binds to immobilized mannose but not to immobilized LH. When analyzed using a binding assay that precipitates receptor ligand complexes with polyethylene glycol, the S4GGnM-R is able to bind S4GGnM-bovine serum albumin (S4GGnM-BSA) conjugates whereas the Man-R is not. In contrast both the S4GGnM-R and the Man-R are able to bind ...Continue Reading

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Citations

Apr 16, 1998·Proceedings of the National Academy of Sciences of the United States of America·D J FieteJ U Baenziger
Aug 16, 2000·Proceedings of the National Academy of Sciences of the United States of America·D S Roseman, J U Baenziger
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Jun 29, 2005·The Journal of Biological Chemistry·Yunpeng SuLuisa Martinez-Pomares
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