Distinct Roles for Dectin-1 and Dectin-2 in Skin Wound Healing and Neutrophilic Inflammatory Responses
Kenji YamaguchiEmi KannoHiromasa TannoAyako SasakiYuki KitaiTakayuki MiuraNaoyuki TakagiM. ShojiJun KasamatsuKo SatoYuka SatoMomoko NiiyamaY GotoKeiko IshiiY ImaiShinobu SaijoYoichiro IwakuraMasahiro TachiKazuyoshi Kawakami
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The Dolichos biflorus seed lectin contains two structurally related subunits. A cDNA library was constructed using RNA isolated from D. biflorus seeds actively synthesizing the seed lectin. The library was expressed in Escherichia coli using a lambda Charon 16 vector, and lectin‐specific antiserum was used to isolate a seed lectin cDNA. Hybridization of the D. biflorus seed lectin cDNA to RNA isolated from seeds actively producing both lectin subunits identifies a single‐size RNA of 1100 bases. An oligodeoxyribonucleotide probe, constructed from an amino acid sequence common to both lectin subunits, detects the same size RNA. Translation of seed mRNA in vitro and immunoprecipitation of translation products using a lectin‐specific antiserum yields a single polypeptide of slightly higher molecular mass than the largest seed lectin subunit. This seed lectin precursor is indistinguishable from a polypeptide synthesized from mRNA hybrid selected by the seed lectin cDNA. These data support the existence of a single polypeptide precursor for both subunit types of the D. biflorus seed lectin and suggest that differences between the subunit types arise by posttranslational processing.
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Journal Article A Chimeric Lectin Formed from Bauhinia purpurea Lectin and Lens culinaris Lectin Recognizes a Unique Carbohydrate Structure Get access Kazuo Yamamoto, Kazuo Yamamoto 2 Laboratory of Molecular Medicine, Department of Integrated Biosciences, Graduate School of Frontier Sciences, The University of Tokyo7–3–1 Hongo, Bunkyo-ku, Tokyo 113–0033 2 To whom correspondence should be addressed. Tel +81-3-5841-4776, 8843, Fax: +81-03-5841-8923, E-mail:yamamoto@k.u-tokyo.ac.jp Search for other works by this author on: Oxford Academic PubMed Google Scholar Yukiko Konami, Yukiko Konami Laboratory of Molecular Medicine, Department of Integrated Biosciences, Graduate School of Frontier Sciences, The University of Tokyo7–3–1 Hongo, Bunkyo-ku, Tokyo 113–0033 Search for other works by this author on: Oxford Academic PubMed Google Scholar Toshiaki Osawa Toshiaki Osawa Laboratory of Molecular Medicine, Department of Integrated Biosciences, Graduate School of Frontier Sciences, The University of Tokyo7–3–1 Hongo, Bunkyo-ku, Tokyo 113–0033 Search for other works by this author on: Oxford Academic PubMed Google Scholar The Journal of Biochemistry, Volume 127, Issue 1, January 2000, Pages 129–135, https://doi.org/10.1093/oxfordjournals.jbchem.a022573 Published: 01 January 2000 Article history Received: 02 September 1999 Accepted: 25 October 1999 Published: 01 January 2000
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Pinctada fucata
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Abstract The crystal structures of an L‐type lectin domain from Methanocaldococcus jannaschii in apo and mannose‐bound forms have been determined. A thorough investigation of L‐type lectin domains from several organisms provides insight into the differences in these domains from different kingdoms of life. While the overall fold of the L‐type lectin domain is conserved, differences in the lengths of the carbohydrate‐binding loops and significant variations in the Mn 2+ ‐binding site compared to the Ca 2+ ‐binding site are observed. Furthermore, the sequence and phylogenetic analyses suggest that the archaeal L‐type lectin domain is evolutionarily closer to the plant legume lectins than to its bacterial or animal counterparts. This is the first report of the biochemical, structural, sequence, and phylogenetic analyses of an L‐type lectin domain from archaea and serves to enhance our understanding of the species‐specific differences and evolution of L‐type lectin domains.
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Vibrio alginolyticus
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