| Literature DB >> 18848522 |
Tomoharu Takeuchi1, Remi Sennari, Ken-ichi Sugiura, Hiroaki Tateno, Jun Hirabayashi, Ken-ichi Kasai.
Abstract
C-type lectins are a family of proteins with an affinity to carbohydrates in the presence of Ca(2+). In the genome of Caenorhabditis elegans, almost 300 genes encoding proteins containing C-type lectin-like domains (CTLDs) have been assigned. However, none of their products has ever been shown to have carbohydrate-binding activity. In the present study, we selected 6 potential C-type lectin genes and prepared corresponding recombinant proteins. One of them encoded by clec-79 was found to have sugar-binding activity by using a newly developed glycoconjugate microarray based on evanescent-field excited fluorescence. CLEC-79 exhibited affinity to sugars containing galactose at the non-reducing terminal, especially to the Galbeta1-3GalNAc structure, in the presence of Ca(2+). Combined with structural information of the glycans of C. elegans, these results suggest that CLEC-79 preferentially binds to O-glycans in vivo.Entities:
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Year: 2008 PMID: 18848522 DOI: 10.1016/j.bbrc.2008.10.001
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN: 0006-291X Impact factor: 3.575