rdf:type |
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lifeskim:mentions |
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pubmed:issue |
11
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pubmed:dateCreated |
1990-7-12
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pubmed:abstractText |
The Friend spleen focus-forming virus envelope glycoprotein, gp55, binds to the murine erythropoietin receptor (EPO-R) and triggers growth activation in the absence of EPO. Interleukin 3-dependent lymphoid cell lines that have been stably transfected with the EPO-R cDNA grow in the presence of EPO or interleukin 3. In these cells, the EPO-R is synthesized as a minor 62-kDa unglycosylated form and a major 64-kDa form carrying one high-mannose N-linked oligosaccharide. A fraction of the 64-kDa form is processed to a 66-kDa species with complex-type sugars. Very little of the EPO-R is expressed on the cell surface and all three forms of EPO-R are degraded rapidly. Cells transfected with both EPO-R and gp55 cDNAs grow in the absence of EPO. Most of the EPO-R associated with gp55 is endoglycosidase H-sensitive, suggesting that the interactions between these proteins occur in the endoplasmic reticulum. Furthermore, the endoglycosidase H-sensitive EPO-R is more stable than in the absence of gp55, a result suggesting that interaction of gp55 with the EPO-R causes it to remain within the rough endoplasmic reticulum. It is possible that gp55 EPO-R complexes within this compartment send a growth-promoting signal to the cell.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/2161534-13416470,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2161534-2154268,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2161534-2154592,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2161534-2154701,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2161534-2404337,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2161534-2476441,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2161534-2539263,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2161534-2550142,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2161534-2551043,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2161534-2554298,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2161534-2688704,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2161534-2789432,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2161534-2934137,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2161534-2990034,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2161534-2999422,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2161534-3032937,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2161534-3040719,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2161534-3143116,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2161534-3292055,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2161534-3308876,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2161534-3924414,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2161534-6250721,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2161534-6262795,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2161534-6308644,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2161534-6606682,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2161534-6936081,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2161534-6955026,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2161534-6955527,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2161534-723932,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2161534-7420541
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidase K,
http://linkedlifedata.com/resource/pubmed/chemical/Erythropoietin,
http://linkedlifedata.com/resource/pubmed/chemical/Gene Products, env,
http://linkedlifedata.com/resource/pubmed/chemical/Hexosaminidases,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Erythropoietin,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Serine Endopeptidases
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
87
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4139-43
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:2161534-Animals,
pubmed-meshheading:2161534-Cell Compartmentation,
pubmed-meshheading:2161534-Cell Division,
pubmed-meshheading:2161534-Endopeptidase K,
pubmed-meshheading:2161534-Endoplasmic Reticulum,
pubmed-meshheading:2161534-Erythropoietin,
pubmed-meshheading:2161534-Gene Products, env,
pubmed-meshheading:2161534-Hexosaminidases,
pubmed-meshheading:2161534-Membrane Glycoproteins,
pubmed-meshheading:2161534-Mice,
pubmed-meshheading:2161534-Molecular Weight,
pubmed-meshheading:2161534-Protein Processing, Post-Translational,
pubmed-meshheading:2161534-Receptors, Cell Surface,
pubmed-meshheading:2161534-Receptors, Erythropoietin,
pubmed-meshheading:2161534-Recombinant Proteins,
pubmed-meshheading:2161534-Serine Endopeptidases
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pubmed:year |
1990
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pubmed:articleTitle |
Friend spleen focus-forming virus glycoprotein gp55 interacts with the erythropoietin receptor in the endoplasmic reticulum and affects receptor metabolism.
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pubmed:affiliation |
Whitehead Institute for Biomedical Research, Nine Cambridge Center, MA 02142.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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