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J. Biol. Chem., Vol. 279, Issue 32, 33379-33389, August 6, 2004

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Unique Catabolic Pathway of Glycosphingolipids in a Hydrozoan, Hydra magnipapillata, Involving Endoglycoceramidase^*

Yasuhiro Horibata, Keishi Sakaguchi, Nozomu Okino, Hiroshi Iida, Masanori Inagaki¶, Toshitaka Fujisawa||, Yoichiro Hama**, and Makoto Ito

From the Department of Bioscience and Biotechnology, Graduate School of Bioresource and Bioenvironmental Sciences, Kyushu University, 6-10-1 Hakozaki, Higashi-ku, Fukuoka 812-8581, the Department of Applied Genetics and Pest Management, Graduate School of Bioresource and Bioenvironmental Sciences, Kyushu University, 6-10-1 Hakozaki, Higashi-ku, Fukuoka 812-8581, the ^¶Faculty of Pharmaceutical Sciences, Graduate School Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka 812-8582, the ^||Department of Developmental Genetics, National Institute of Genetics, 1,111 Yata, Mishima, Shizuoka 411-8540, and the ^**Department of Applied Biological Sciences, Faculty of Agriculture, Saga University, 1 Honjo, Saga 840-8502, Japan

Endoglycoceramidase (EGCase; EC 3.2.1.123) is an enzyme capable of cleaving the glycosidic linkage between oligosaccharides and ceramides of various glycosphingolipids. We detected strong EGCase activity in animals belonging to Cnidaria, Mollusca, and Annelida and cloned the enzyme from a hydra, Hydra magnipapillata. The hydra EGCase, consisting of 517 amino acid residues, showed 19.2% and 50.2% identity to the Rhodococcus and jellyfish EGCases, respectively. The recombinant hydra enzyme, expressed in CHOP (Chinese hamster ovary cells expressing polyoma LT antigen) cells, hydrolyzed [¹⁴C]GM1a to produce [¹⁴C]ceramide with a pH optimum at 3.0-3.5. Whole mount in situ hybridization and immunocytochemical analysis revealed that EGCase was widely expressed in the endodermal layer, especially in digestive cells. GM1a injected into the gastric cavity was incorporated and then directly catabolized by EGCase to produce GM1a-oligosaccharide and ceramide, which were further degraded by exoglycosidases and ceramidase, respectively. However, hydra exoglycosidases did not hydrolyze GM1a directly. These results indicate that the EGCase is indispensable for the catabolic processing of dietary glycosphingolipids in hydra, demonstrating the unique catabolic pathway for glycosphingolipids in the animal.

Received for publication, February 10, 2004 , and in revised form, May 18, 2004.

The nucleotide sequence(s) reported in this paper has been submitted to the DDBJ/GenBank^TM/EBI Data Bank with accession number(s) AB179748.

^* This work was supported in part by a Grant-in-aid for Scientific Research on Priority Areas 12140204 and Research (B) 15380073 from the Ministry of Education, Science and Culture of Japan, and Takeda Science Foundation. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed. Tel.: 81-92-642-2898; Fax: 81-92-642-2907; E-mail: makotoi{at}agr.kyushu-u.ac.jp.

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