Glycobiology Advance Access published online on June 30, 2004
Glycobiology, doi:10.1093/glycob/cwh120
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1 Centre for Biomolecular Interactions Bremen, Department of Biology and Chemistry, University Bremen, 28334 Bremen, Germany
* To whom correspondence should be addressed. E-mail: flehmann{at}uni-bremen.de.
Siglecs are the largest family of sialic-acid recognizing lectins identified so far with eleven members in the human genome. Most of these siglecs are exclusively expressed by cells of the immune system. Comparison of different mammalian species has revealed differential and complex evolutionary paths for this protein family even within the primate lineage. To understand the evolution of siglecs, in particular the origin of this family, we investigated the occurrence of corresponding genes in bony fish. Interestingly, only unambiguous orthologues of mammalian Siglec-4, a cell adhesion molecule expressed exclusively in the nervous system, could be identified in the genomes of fugu and zebrafish, whereas no obvious orthologues of the other mammalian siglecs were found. As in mammals fish Siglec-4 expression is restricted to nervous tissues as demonstrated by Northern blot. Expressed as recombinant protein, fish Siglec-4 binds to sialic acids with a specificity similar to the mammalian orthologues. Relatively low sequence similarities in the cytoplasmic tail as well as an additional splice variant found in fish Siglec-4 suggest alternative signaling pathways compared to mammalian species. Our observations suggest that this siglec occurs at least in the nervous system of all vertebrates.
Revised June 15, 2004
Accepted June 28, 2004
ORIGINAL ARTICLES
Evolution of sialic acid-binding proteins: molecular cloning and expression of fish Siglec-4
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