Skip Navigation



Glycobiology Advance Access published online on May 4, 2007

Glycobiology, doi:10.1093/glycob/cwm049
This Article
Right arrow Advance Access manuscript (PDF) Freely available
Right arrow All Versions of this Article:
17/8/838    most recent
cwm049v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrowRequest Permissions
Right arrow Disclaimer
Google Scholar
Right arrow Articles by Angata, T.
Right arrow Articles by Nakamura, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Angata, T.
Right arrow Articles by Nakamura, M.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© The Author 2007. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

Siglec-15: An immune system Siglec that is conserved throughout vertebrate evolution

Takashi Angata1, Yukako Tabuchi, Kazunori Nakamura and Mitsuru Nakamura

Research Center for Medical Glycoscience, National Institute of Advanced Industrial Science and Technology, 1-1-1 Umezono, Tsukuba, Ibaraki 305-8568, JAPAN


1 To whom correspondence should be addressed: Phone: +81-29-861-9460; Fax: +81-29-861-3191; E-mail: takashi-angata{at}aist.go.jp

Received on February 2, 2007; revised on March 27, 2007; accepted on April 23, 2007

Siglecs are vertebrate cell-surface receptors that recognize sialylated glycans. Here we have identified and characterized a novel Siglec, named Siglec-15. Siglec-15 is a type-I transmembrane protein consisting of two immunoglobulin-like domains, a transmembrane domain containing a lysine residue, and a short cytoplasmic tail. Siglec-15 is expressed on macrophages and/or dendritic cells of human spleen and lymph nodes. We show that the extracellular domain of Siglec-15 preferentially recognizes the sialyl Tn structure. Siglec-15 associates with the activating adaptor proteins DAP12 and DAP10 via its lysine residue in the transmembrane domain, implying that it functions as an activating signaling molecule. Siglec-15 is the second human Siglec identified to have an activating signaling potential; unlike the first example Siglec-14, however, it does not have an inhibitory counterpart. Orthologs of Siglec-15 are present not only in mammals but also in other branches of vertebrates; by contrast, no other known Siglec expressed in the immune system has been conserved throughout the vertebrate evolution. Thus, Siglec-15 probably plays a conserved regulatory role in the immune system of vertebrates.

Key words: DAP12 / dendritic cells / macrophages / sialyl Tn / Siglec


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?




Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.