Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
1990-7-12
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.
pubmed:grant
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
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:volume
87
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4139-43
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Friend spleen focus-forming virus glycoprotein gp55 interacts with the erythropoietin receptor in the endoplasmic reticulum and affects receptor metabolism.
pubmed:affiliation
Whitehead Institute for Biomedical Research, Nine Cambridge Center, MA 02142.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't