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rdf:type |
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lifeskim:mentions |
umls-concept:C0007004,
umls-concept:C0031308,
umls-concept:C0043393,
umls-concept:C0086418,
umls-concept:C0439064,
umls-concept:C1257857,
umls-concept:C1417249,
umls-concept:C1514562,
umls-concept:C1521991,
umls-concept:C1880022,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
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pubmed:issue |
6
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pubmed:dateCreated |
1991-1-31
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pubmed:abstractText |
The macrophage mannose receptor is an integral membrane protein expressed on the surface of tissue macrophages. After ligation of mannose-rich glycoconjugates or pathogens, the receptor mediates endocytosis and phagocytosis of the bound ligands by macrophages. The cDNA-derived primary structure of the mannose receptor predicts a cysteine-rich NH2-terminal domain, followed by a fibronectin type II region. The remainder of the ectodomain is comprised of eight carbohydrate recognition-like domains, followed by a transmembrane region, and a cytoplasmic tail. Transfection of the mannose receptor cDNA into Cos-I cells is necessary for receptor-mediated endocytosis of mannose-rich glycoconjugate as well as phagocytosis of yeasts. Deletion of the cytoplasmic tail results in a mutant receptor that is able to bind but not ingest the ligated pathogens, suggesting that the signal for phagocytosis is contained in the cytoplasmic tail.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/2258707-1968060,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2258707-1968349,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2258707-2200126,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2258707-2300204,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2258707-2466335,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2258707-2466574,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2258707-2477486,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2258707-2529342,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2258707-2534350,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2258707-2568890,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2258707-2579146,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2258707-2590164,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2258707-2647302,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2258707-271968,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2258707-2818558,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2258707-2909656,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2258707-2911749,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2258707-2934410,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2258707-2972794,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2258707-2978536,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2258707-2992939,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2258707-3009480,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2258707-3077136,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2258707-332066,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2258707-3611070,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2258707-3891904,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2258707-6120989,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2258707-6188151,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2258707-6287227,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2258707-6298248,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2258707-6319531,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2258707-6766809,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2258707-963012
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0022-1007
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
172
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1785-94
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:2258707-Amino Acid Sequence,
pubmed-meshheading:2258707-Animals,
pubmed-meshheading:2258707-Cell Line,
pubmed-meshheading:2258707-Endocytosis,
pubmed-meshheading:2258707-Female,
pubmed-meshheading:2258707-Gene Expression,
pubmed-meshheading:2258707-Gene Library,
pubmed-meshheading:2258707-Humans,
pubmed-meshheading:2258707-Lectins, C-Type,
pubmed-meshheading:2258707-Mannose,
pubmed-meshheading:2258707-Mannose-Binding Lectins,
pubmed-meshheading:2258707-Molecular Sequence Data,
pubmed-meshheading:2258707-Phagocytosis,
pubmed-meshheading:2258707-Placenta,
pubmed-meshheading:2258707-Pregnancy,
pubmed-meshheading:2258707-Receptors, Cell Surface,
pubmed-meshheading:2258707-Receptors, Immunologic,
pubmed-meshheading:2258707-Saccharomyces cerevisiae,
pubmed-meshheading:2258707-Sequence Homology, Nucleic Acid,
pubmed-meshheading:2258707-Transfection
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pubmed:year |
1990
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pubmed:articleTitle |
Molecular characterization of the human macrophage mannose receptor: demonstration of multiple carbohydrate recognition-like domains and phagocytosis of yeasts in Cos-1 cells.
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pubmed:affiliation |
Division of Hematology/Oncology, Children's Hospital, Dana-Farber Cancer Institute, Boston, Massachusetts.
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pubmed:publicationType |
Journal Article,
Comparative Study
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