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Characterization of rat β‐glucan receptor dectin‐1
Author(s) -
Kato Yuya,
Adachi Yoshiyuki,
Ohno Naohito
Publication year - 2008
Publication title -
microbiology and immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.664
H-Index - 70
eISSN - 1348-0421
pISSN - 0385-5600
DOI - 10.1111/j.1348-0421.2008.00055.x
Subject(s) - biology , gene isoform , syk , receptor , peptide sequence , alternative splicing , signal transduction , glucan , rna splicing , microbiology and biotechnology , biochemistry , gene , rna , tyrosine kinase
Dectin‐1 is a small C‐type lectin receptor for fungal cell wall β‐glucan. Its homologues in some species, including mouse and human, have been characterized, and their importance in antifungal immunity has also been clarified. However, its homologue in the rat has not yet been identified. In this study, DNA/amino acid sequences of rat dectin‐1 were analyzed by rapid amplification of cDNA ends. The sequence of rat dectin‐1 was found to be highly homologous to that of the mouse. It possesses essential motifs for the recognition of β‐glucan and signal transduction. However, the position of the start codon in the detected sequence was not conserved, and its cytoplasmic tail was shorter than that observed in other species. Similar to mouse dectin‐1, two major isoforms of rat dectin‐1 that were generated by alternative splicing were identified: a full‐length isoform and a shorter isoform deficient in the stalk domain. It was also demonstrated that rat dectin‐1 is capable of binding fungal β‐glucan and activating nuclear factor‐kappa B via Syk and the CARD9/Bcl10‐mediated pathway. These results suggest that rat dectin‐1 also plays essential roles in immune responses against fungi.