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Originally published In Press as doi:10.1074/jbc.M011723200 on March 20, 2001

J. Biol. Chem., Vol. 276, Issue 23, 19959-19965, June 8, 2001
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Cloning and Characterization of Novel Ficolins from the Solitary Ascidian, Halocynthia roretzi*

Akira Kenjo, Minoru Takahashi, Misao Matsushita, Yuichi Endo, Munehiro NakataDagger , Tsuguo MizuochiDagger , and Teizo Fujita§

From the Department of Biochemistry, Fukushima Medical University, School of Medicine, 1-Hikariga-oka, Fukushima 960-1295, Japan and the Dagger  Laboratory of Biomedical Chemistry, Department of Applied Chemistry, Tokai University, Hiratsuka, Kanagawa 259-1292, Japan

Ficolins are animal lectins with collagen-like and fibrinogen-like domains. They are involved in the first line of host defense against pathogens. Human ficolin/P35 as well as mannose-binding lectin (MBL) activates the complement lectin pathway in association with MBL-associated serine proteases. To elucidate the origin and evolution of ficolins, we separated ~40 kDa (p40) and ~50 kDa (p50) N-acetylglucosamine-binding lectins from hemolymph plasma of the solitary ascidian. Binding assays revealed that p40 recognizes N-acetyl groups in association with a pyranose ring and that p50 recognizes N-acetylglucosamine alone. Based on the amino acid sequences of the proteins, we isolated two clones each of p40 and p50 from the ascidian hepatopancreas cDNA and determined the entire coding sequences of these clones. Because all of the clones contained both collagen-like and fibrinogen-like domains, we concluded that these were homologs of the mammalian ficolin family and designated ascidian ficolins (AsFCNs). The fibrinogen-like domain of the AsFCNs shows 45.4-52.4% amino acid sequence identity with the mammalian ficolin family. A phylogenetic tree of the fibrinogen-like sequences shows that all the fibrinogen-like domains may have evolved from a common ancestor that branched off an authentic fibrinogen. These results suggest that AsFCNs play an important role with respect to ascidian hemolymph lectin activity and the correlation of different functions with binding specificity.

* This work was supported by grants-in-aid for scientific research from the Japan Society for the Promotion of Science.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequences reported in this paper have been submitted to the DDBJ/GenBankTM/EBI Data Bank with accession numbers AB049619, AB049620, AB049621, and AB049622.

§ To whom correspondence should be addressed. Tel.: 81-24-548-2111, Ext. 2230; Fax: 81-24-548-6760; E-mail: tfujita@fmu.ac.jp.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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Copyright © 2001 by the American Society for Biochemistry and Molecular Biology.