Source:http://linkedlifedata.com/resource/pubmed/id/16622020
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
9
|
pubmed:dateCreated |
2006-4-19
|
pubmed:abstractText |
Dectin-1 is a specific receptor for beta-glucans and a major receptor for fungal particles on macrophages (Mphi). It is a type II membrane receptor that has a C-terminal, NK-like, C-type lectin-like domain separated from the cell membrane by a short stalk region and a cytoplasmic immunoreceptor tyrosine-based activation-like motif. We observed functional differences in dectin-1-dependent recognition of fungal particles by Mphi from different mouse strains. RT-PCR analysis revealed that mice have at least two splice forms of dectin-1, generated by differential usage of exon 3, encoding the full-length dectin-1A and a stalkless Mphi dectin-1B. Mphi from BALB/c mice and genetically related mice expressed both isoforms in similar amounts, whereas Mphi from C57BL/6 and related mice mainly expressed the smaller isoform. NIH-3T3 fibroblast and RAW264.7 macrophage cell lines stably expressing either isoform were able to bind and phagocytose zymosan at 37 degrees C. However, binding by the smaller dectin-1B isoform was significantly affected at lower temperatures. These properties were shared by the equivalent human isoforms. The relative ability of each of the isoforms to induce TNF-alpha production in RAW264.7 Mphi was also found to be different. These results are the first evidence that dectin-1 isoforms are functionally distinct and indicate that differential isoform usage may represent a mechanism of regulating cellular responses to beta-glucans.
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
AIM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Isoforms,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Necrosis Factor-alpha,
http://linkedlifedata.com/resource/pubmed/chemical/Zymosan,
http://linkedlifedata.com/resource/pubmed/chemical/dectin 1
|
pubmed:status |
MEDLINE
|
pubmed:month |
May
|
pubmed:issn |
0022-1767
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
1
|
pubmed:volume |
176
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
5513-8
|
pubmed:dateRevised |
2007-11-14
|
pubmed:meshHeading |
pubmed-meshheading:16622020-Animals,
pubmed-meshheading:16622020-Cell Line,
pubmed-meshheading:16622020-Gene Expression Regulation,
pubmed-meshheading:16622020-Humans,
pubmed-meshheading:16622020-Macrophages,
pubmed-meshheading:16622020-Membrane Proteins,
pubmed-meshheading:16622020-Mice,
pubmed-meshheading:16622020-Nerve Tissue Proteins,
pubmed-meshheading:16622020-Protein Isoforms,
pubmed-meshheading:16622020-Temperature,
pubmed-meshheading:16622020-Tumor Necrosis Factor-alpha,
pubmed-meshheading:16622020-Zymosan
|
pubmed:year |
2006
|
pubmed:articleTitle |
Expression of functionally different dectin-1 isoforms by murine macrophages.
|
pubmed:affiliation |
Sir William Dunn School of Pathology, University of Oxford, Oxford, United Kingdom.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
|