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Laboratory of Cellular and Molecular Biotechnology, Faculty of Science, Kochi University, Kochi 780-8520, Japan
* Present address: Biomolecular Engineering Department, National Institute of Bioscience and Human Technology, AIST, 1-1 Higashi, Tsukuba, Ibaragi 305-8566, Japan
Author for correspondence (e-mail: kazuk{at}cc.kochi-u.ac.jp)
Accepted June 6, 2001
We have isolated two Ca2+-dependent, galactose-binding polypeptides from the budding tunicate, Polyandrocarpa misakiensis. Based on their partial amino acid sequences, full-length cDNAs were cloned. One of them was identical with a tunicate C-type lectin (TC14-2) reported previously. The other was a novel C-type lectin, referred to as TC14-3. In living animals, they appeared to be coupled. This complex of lectins, when applied in vitro to tunicate multipotent cells of epithelial origin, blocked cell proliferation and induced cell aggregation. The aggregates expressed a homolog of the integrin
-chain and other differentiation markers specific for epithelial cells. Recombinant TC14-3 could reproduce all the activities of native lectins by itself, which was accelerated by recombinant TC14-2. The inhibitory activity of TC14-3 on cell growth was completely abolished by the addition of 50 µM D-galactose. Anti-TC14-3 monoclonal antibody showed that the antigen was expressed constitutively by the multipotent epithelial and mesenchymal cells. These results provide evidence that in P. misakiensis a C-type lectin plays a novel, cytostatic role in regulating cell growth, cell adhesion and cell differentiation during asexual reproduction.
Key words: Lectin,
-Integrin, Alkaline phosphatase, Recombinant protein, Cell growth, Multipotency, Budding, Tunicate, Polyandrocarpa misakiensis
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