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M401460200v1
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Papers In Press, published online ahead of print May 19, 2004
J. Biol. Chem, 10.1074/jbc.M401460200
Submitted on February 10, 2004
Revised on May 18, 2004
Accepted on May 19, 2004

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

Department of Bioscience and Biotechnology, Graduate School of Kyushu University, Fukuoka, Fukuoka 812-8581

Corresponding Author: makotoi{at}agr.kyushu-u.ac.jp

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 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 GSLs in the animal.


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