HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Heinsbroek, S. E. M. Articles by Brown, G. D. Search for Related Content PubMed PubMed Citation Articles by Heinsbroek, S. E. M. Articles by Brown, G. D. Pubmed/NCBI databases Gene GEO Profiles HomoloGene UniGene Compound via MeSH Substance via MeSH

Expression of Functionally Different Dectin-1 Isoforms by Murine Macrophages¹

Sigrid E. M. Heinsbroek^*, Philip R. Taylor^*, Marcela Rosas^*, Janet A. Willment, David L. Williams, Siamon Gordon^2,* and Gordon D. Brown^2,3,

^* Sir William Dunn School of Pathology, University of Oxford, Oxford, United Kingdom; Institute of Infectious Disease and Molecular Medicine, University of Cape Town, Cape Town, South Africa; and Department of Surgery, James H. Quillen College of Medicine, East Tennessee State University, Johnson City, Tennessee 37614

Dectin-1 is a specific receptor for -glucans and a major receptor for fungal particles on macrophages (M). 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 M 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 M dectin-1B. M from BALB/c mice and genetically related mice expressed both isoforms in similar amounts, whereas M 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°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- production in RAW264.7 M 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 -glucans.

This article has been cited by other articles:

				M. Rosas, K. Liddiard, M. Kimberg, I. Faro-Trindade, J. U. McDonald, D. L. Williams, G. D. Brown, and P. R. Taylor The Induction of Inflammation by Dectin-1 In Vivo Is Dependent on Myeloid Cell Programming and the Progression of Phagocytosis J. Immunol., September 1, 2008; 181(5): 3549 - 3557. [Abstract] [Full Text] [PDF]

				A. T. Borchers, A. Krishnamurthy, C. L. Keen, F. J. Meyers, and M. E. Gershwin The Immunobiology of Mushrooms Experimental Biology and Medicine, March 1, 2008; 233(3): 259 - 276. [Abstract] [Full Text] [PDF]

				C. A. Rappleye, L. G. Eissenberg, and W. E. Goldman Histoplasma capsulatum {alpha}-(1,3)-glucan blocks innate immune recognition by the beta-glucan receptor PNAS, January 23, 2007; 104(4): 1366 - 1370. [Abstract] [Full Text] [PDF]

				F. Meyer-Wentrup, C. G. Figdor, M. Ansems, P. Brossart, M. D. Wright, G. J. Adema, and A. B. van Spriel Dectin-1 Interaction with Tetraspanin CD37 Inhibits IL-6 Production J. Immunol., January 1, 2007; 178(1): 154 - 162. [Abstract] [Full Text] [PDF]