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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
23
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pubmed:dateCreated |
1997-6-26
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pubmed:abstractText |
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 Man-BSA. Monosaccharides that inhibit binding of Man-BSA by the Man-R enhance binding by the S4GGnM-R. Oligosaccharides terminating with S4GGnM and those terminating with Man are bound at independent sites on the S4GGnM-R. The S4GGnM-R present in hepatic endothelial cells may account for clearance of glycoproteins bearing oligosaccharides terminating with S4GGnM and glycoproteins bearing oligosaccharides terminating with either mannose, fucose, or N-acetylglucosamine.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Indicators and Reagents,
http://linkedlifedata.com/resource/pubmed/chemical/Oligosaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
6
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pubmed:volume |
272
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
14629-37
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:9169424-Amino Acid Sequence,
pubmed-meshheading:9169424-Animals,
pubmed-meshheading:9169424-Carbohydrate Sequence,
pubmed-meshheading:9169424-Chromatography, Affinity,
pubmed-meshheading:9169424-Glycoproteins,
pubmed-meshheading:9169424-Indicators and Reagents,
pubmed-meshheading:9169424-Kinetics,
pubmed-meshheading:9169424-Liver,
pubmed-meshheading:9169424-Molecular Sequence Data,
pubmed-meshheading:9169424-Molecular Weight,
pubmed-meshheading:9169424-Oligosaccharides,
pubmed-meshheading:9169424-Peptide Fragments,
pubmed-meshheading:9169424-Peptide Mapping,
pubmed-meshheading:9169424-Radioimmunoassay,
pubmed-meshheading:9169424-Rats,
pubmed-meshheading:9169424-Rats, Sprague-Dawley,
pubmed-meshheading:9169424-Receptors, Cell Surface
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pubmed:year |
1997
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pubmed:articleTitle |
Isolation of the SO4-4-GalNAcbeta1,4GlcNAcbeta1,2Manalpha-specific receptor from rat liver.
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pubmed:affiliation |
Department of Pathology, Washington University School of Medicine, St. Louis, Missouri 63110, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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