Expression of functionally different dectin-1 isoforms by murine macrophages.
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 tyro...
| Main Authors: | , , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
2006
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| _version_ | 1797051744764559360 |
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| author | Heinsbroek, SE Taylor, P Rosas, M Willment, J Williams, D Gordon, S Brown, G |
| author_facet | Heinsbroek, SE Taylor, P Rosas, M Willment, J Williams, D Gordon, S Brown, G |
| author_sort | Heinsbroek, SE |
| collection | OXFORD |
| description | 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. |
| first_indexed | 2024-03-06T18:23:51Z |
| format | Journal article |
| id | oxford-uuid:073f0818-af6f-4337-9398-cd25709dd192 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T18:23:51Z |
| publishDate | 2006 |
| record_format | dspace |
| spelling | oxford-uuid:073f0818-af6f-4337-9398-cd25709dd1922022-03-26T09:06:37ZExpression of functionally different dectin-1 isoforms by murine macrophages.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:073f0818-af6f-4337-9398-cd25709dd192EnglishSymplectic Elements at Oxford2006Heinsbroek, SETaylor, PRosas, MWillment, JWilliams, DGordon, SBrown, GDectin-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. |
| spellingShingle | Heinsbroek, SE Taylor, P Rosas, M Willment, J Williams, D Gordon, S Brown, G Expression of functionally different dectin-1 isoforms by murine macrophages. |
| title | Expression of functionally different dectin-1 isoforms by murine macrophages. |
| title_full | Expression of functionally different dectin-1 isoforms by murine macrophages. |
| title_fullStr | Expression of functionally different dectin-1 isoforms by murine macrophages. |
| title_full_unstemmed | Expression of functionally different dectin-1 isoforms by murine macrophages. |
| title_short | Expression of functionally different dectin-1 isoforms by murine macrophages. |
| title_sort | expression of functionally different dectin 1 isoforms by murine macrophages |
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