Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
12
|
| pubmed:dateCreated |
1989-6-2
|
| pubmed:abstractText |
Human interleukin 4 (IL-4) specifically induces the low affinity receptor for IgE (Fc epsilon R2/CD23) on the surface of the Burkitt lymphoma cell line Jijoye. At 4 degrees C 125I-IL-4 specifically binds to high affinity receptors (Kd = 4-10 x 10(-11) M; Bmax, 600-1,200 sites/cell). Following a rapid temperature shift from 4 to 37 degrees C, 80% of the receptor-bound 125I-IL-4 disappeared from the cell surface within 20 min (t1/2 = 8.9 min). For every two internalized molecules of IL-4 (t1/2 = 13 min), one molecule of IL-4 dissociated from the cell surface (t1/2 = 25 min). More than 90% of the internalized IL-4 was released in a degraded form into the medium following first order kinetics (t1/2 = 68 min). Internalization was inhibited by cytoskeletal disrupting and lysosomotropic agents. Incubating cells with 1 nM IL-4 resulted in a rapid down-regulation of IL-4 receptors (75% loss after 2 h); a reexpression of receptor to control level occurred after 20 h in spite of the presence of a large excess of IL-4. Reexpression was delayed by chloroquine and blocked by cycloheximide and actinomycin D. By using the cross-linking agent bis(sulfosuccinimidyl)suberate, three polypeptides of Mr 130,000, 80,000, and 70,000 were specifically labeled with 125I-IL-4. These three polypeptides coordinately disappeared and reappeared with the 125I-IL-4 binding sites. The induction of Fc epsilon R2/CD23 required prolonged incubation (greater than 8 h) with IL-4 and thus may be dependent on the reexpression of IL-4 receptor.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Differentiation...,
http://linkedlifedata.com/resource/pubmed/chemical/Azides,
http://linkedlifedata.com/resource/pubmed/chemical/Chloroquine,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochalasin B,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-4,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Fc,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, IgE,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Interleukin-4,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Mitogen
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Apr
|
| pubmed:issn |
0021-9258
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
25
|
| pubmed:volume |
264
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
6984-9
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:2523386-Antigens, Differentiation, B-Lymphocyte,
pubmed-meshheading:2523386-Azides,
pubmed-meshheading:2523386-Cell Line,
pubmed-meshheading:2523386-Chloroquine,
pubmed-meshheading:2523386-Cytochalasin B,
pubmed-meshheading:2523386-Endocytosis,
pubmed-meshheading:2523386-Gene Expression Regulation,
pubmed-meshheading:2523386-Humans,
pubmed-meshheading:2523386-Interleukin-4,
pubmed-meshheading:2523386-Interleukins,
pubmed-meshheading:2523386-Kinetics,
pubmed-meshheading:2523386-Lysosomes,
pubmed-meshheading:2523386-Receptors, Fc,
pubmed-meshheading:2523386-Receptors, IgE,
pubmed-meshheading:2523386-Receptors, Interleukin-4,
pubmed-meshheading:2523386-Receptors, Mitogen,
pubmed-meshheading:2523386-Temperature,
pubmed-meshheading:2523386-Time Factors,
pubmed-meshheading:2523386-Transcription, Genetic
|
| pubmed:year |
1989
|
| pubmed:articleTitle |
Internalization of human interleukin 4 and transient down-regulation of its receptor in the CD23-inducible Jijoye cells.
|
| pubmed:affiliation |
UNICET, Laboratory for Immunological Research, Dardilly, France.
|
| pubmed:publicationType |
Journal Article,
In Vitro
|