Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
4
|
| pubmed:dateCreated |
1998-8-27
|
| pubmed:abstractText |
IL-1R antagonist (IL-1Ra) exists in two well-characterized forms, 17-kDa secretory IL-1Ra (sIL-1Ra) and 18-kDa intracellular IL-1Ra (icIL-1Ra), that arise by alternative transcription of the same IL-1Ra gene. A third, lower molecular mass form (approximately 16 kDa) was detected by immunoblot within lysates of a variety of cells, including human monocytes and myelomonocytic cell lines. The 16-kDa isoform was designated icIL-1RaII, and the previously established 18-kDa form was designated icIL-1RaI. Intracellular IL-1RaII bound type I IL-1R up to fivefold less avidly than did sIL-1Ra and icIL-1RaI. Microsequencing of cyanogen bromide fragments of purified icIL-1RaII provided evidence consistent with initiation of protein translation at the second start site in either IL-1Ra mRNA. The results of site-directed mutation experiments established that icIL-1RaII could be derived by alternative translation initiation. In vitro transcription and translation of intact sIL-1Ra cDNA in rabbit reticulocyte lysates led to both pro-sIL-1Ra and icIL-1RaII proteins, whereas transcription and translation of icIL-1RaI cDNA produced both icIL-1RaI and icIL-1RaII proteins. Mutation of the first 5' ATG in sIL-1Ra cDNA led to translation of only icIL-1RaII, while only sIL-1Ra was observed after mutation of the second ATG. These results indicate that icIL-1RaII is a third member of the IL-1Ra family and is a 16-kDa, 143-amino acid intracellular protein derived by alternative translation initiation from either sIL-1Ra mRNA or icIL-1Ra mRNA. The role in biology of either intracellular form of IL-1Ra remains unknown.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
AIM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/IL1RN protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Il1rn protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin 1 Receptor Antagonist...,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Interleukin-1,
http://linkedlifedata.com/resource/pubmed/chemical/Sialoglycoproteins
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Aug
|
| pubmed:issn |
0022-1767
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
15
|
| pubmed:volume |
161
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
1997-2003
|
| pubmed:dateRevised |
2007-11-14
|
| pubmed:meshHeading |
pubmed-meshheading:9712072-Amino Acid Sequence,
pubmed-meshheading:9712072-Animals,
pubmed-meshheading:9712072-Base Sequence,
pubmed-meshheading:9712072-Humans,
pubmed-meshheading:9712072-Interleukin 1 Receptor Antagonist Protein,
pubmed-meshheading:9712072-Isomerism,
pubmed-meshheading:9712072-Lymphocyte Activation,
pubmed-meshheading:9712072-Mice,
pubmed-meshheading:9712072-Molecular Sequence Data,
pubmed-meshheading:9712072-Molecular Weight,
pubmed-meshheading:9712072-Mutagenesis, Site-Directed,
pubmed-meshheading:9712072-Protein Binding,
pubmed-meshheading:9712072-Protein Biosynthesis,
pubmed-meshheading:9712072-Rabbits,
pubmed-meshheading:9712072-Receptors, Interleukin-1,
pubmed-meshheading:9712072-Reticulocytes,
pubmed-meshheading:9712072-Sequence Analysis,
pubmed-meshheading:9712072-Sialoglycoproteins,
pubmed-meshheading:9712072-Transcription, Genetic,
pubmed-meshheading:9712072-Tumor Cells, Cultured
|
| pubmed:year |
1998
|
| pubmed:articleTitle |
Characterization of a low molecular weight isoform of IL-1 receptor antagonist.
|
| pubmed:affiliation |
Department of Medicine, University of Colorado Health Sciences Center, Denver 80262, USA.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|