A cysteine-rich domain of the "mannose" receptor mediates Ga1NAc-4-SO4 binding

A critical element of lutropin bioactivity in vivo is its rapid removal from the blood by a receptor, located in hepatic endothelial cells, that recognizes the terminal sulfated carbohydrate structure SO4-4-GalNACbeta1,4Glc-NAcbeta1,2Manalpha(S4GGnM). We have previously shown that the macrophage man...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1998-03, Vol.95 (5), p.2089
Main Authors: Fiete, Dorothy J, Beranek, Mary C, Baenziger, Jacques U
Format: Article
Language:English
Subjects:
Biochemistry
Blood
Carbohydrates
Cells
Deoxyribonucleic acid
DNA
Proteins
Online Access:Get full text
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Summary:A critical element of lutropin bioactivity in vivo is its rapid removal from the blood by a receptor, located in hepatic endothelial cells, that recognizes the terminal sulfated carbohydrate structure SO4-4-GalNACbeta1,4Glc-NAcbeta1,2Manalpha(S4GGnM). We have previously shown that the macrophage mannose (Man)-receptor cDNA directs the synthesis of a protein that binds oligosaccharides with either terminal S4GGnM or terminal Man, at independent sites.
ISSN:0027-8424
1091-6490