Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
5
|
| pubmed:dateCreated |
1999-2-23
|
| pubmed:abstractText |
To investigate IL-1-dependent interactions of IL-1 type I (IL-1 RI) receptors on intact cells, lateral and rotational mobilities and detergent insolubility were investigated. Lateral mobility was measured by fluorescence photobleaching recovery, using a Cy3-modified, noncompetitive mAb specific for IL-1RI (M5) bound to wild-type IL-1 RI or mutant IL-1 RI with a truncated cytoplasmic tail. Addition of IL-1 causes significant reduction in the mobile fraction of wild-type IL-1 RI for two different transfected cell lines. For the mutant IL-1 RI, no significant decrease in response to IL-1 is observed, indicating that the missing cytoplasmic segment is involved in IL-1-dependent interactions of IL-1 RI that lead to reduced lateral mobility on the cell surface. The rotational mobility of IL-1 RI was assessed with phosphorescence anisotropy decay measurements using erythrosin-labeled M5. IL-1 decreases the rotational mobility of cell surface IL-1 RI on the microsecond time scale and also increases the initial anisotropy, indicating loss in segmental motion. Measurements of resistance to solubilization by Triton X-100 showed that IL-1 binding increases the fraction of IL-1 RI sedimenting with cytoskeletal residues. The IL-1 receptor antagonist protein (IL-1ra) causes partial effects in reducing rotational mobility and increasing detergent insolubility of M5-lableled IL-1 RI, indicating that this ligand causes structural changes in the presence of the dimerizing M5 mAb. These ligand-dependent physical interactions of IL-1 RI on the cell surface may be related to signal initiation by this receptor.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Detergents,
http://linkedlifedata.com/resource/pubmed/chemical/Erythrosine,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-1,
http://linkedlifedata.com/resource/pubmed/chemical/Isothiocyanates,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Interleukin-1,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Interleukin-1 Type I,
http://linkedlifedata.com/resource/pubmed/chemical/erythrosine isothiocyanate
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Feb
|
| pubmed:issn |
0006-2960
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
2
|
| pubmed:volume |
38
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
1618-25
|
| pubmed:dateRevised |
2011-11-17
|
| pubmed:meshHeading |
pubmed-meshheading:9931029-Animals,
pubmed-meshheading:9931029-Antibodies, Monoclonal,
pubmed-meshheading:9931029-Binding Sites, Antibody,
pubmed-meshheading:9931029-CHO Cells,
pubmed-meshheading:9931029-Cricetinae,
pubmed-meshheading:9931029-Detergents,
pubmed-meshheading:9931029-Erythrosine,
pubmed-meshheading:9931029-Fluorescence Polarization,
pubmed-meshheading:9931029-Interleukin-1,
pubmed-meshheading:9931029-Isothiocyanates,
pubmed-meshheading:9931029-Luminescent Measurements,
pubmed-meshheading:9931029-Mice,
pubmed-meshheading:9931029-Receptor Aggregation,
pubmed-meshheading:9931029-Receptors, Interleukin-1,
pubmed-meshheading:9931029-Receptors, Interleukin-1 Type I,
pubmed-meshheading:9931029-Solubility,
pubmed-meshheading:9931029-Spectrometry, Fluorescence,
pubmed-meshheading:9931029-Tumor Cells, Cultured
|
| pubmed:year |
1999
|
| pubmed:articleTitle |
Interleukin 1 (IL-1) causes changes in lateral and rotational mobilities of IL-1 type I receptors.
|
| pubmed:affiliation |
Department of Chemistry and Chemical Biology, Baker Laboratory, Cornell University, Ithaca, New York 14853-1301, USA.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
|