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Toxins 2012, 4(5), 323-338; https://doi.org/10.3390/toxins4050323

Cytotoxicity and Glycan-Binding Properties of an 18 kDa Lectin Isolated from the Marine Sponge Halichondria okadai

1
Laboratory of Glycobiology and Marine Biochemistry, Department of Genome System Science, Graduate School of NanoBio Sciences, Yokohama City University, 22-2 Seto, Kanazawa-ku, Yokohama 236-0027, Japan
2
Divisions of Functional Morphology and Microbiology, Department of Pharmacy, Faculty of Pharmaceutical Science, Nagasaki International University, 2825-7 Huis Ten Bosch, Sasebo, Nagasaki 859-3298, Japan
3
Laboratory of Carbohydrate and Protein Chemistry, Department of Chemistry, Faculty of Science, University of Chittagong, Chittagong-4221, Bangladesh
4
Division of Cell Recognition Study, Institute of Molecular Biomembrane and Glycobiology, Tohoku Pharmaceutical University, 4-4-1 Komatsusima, Aoba-ku, Sendai 981-8558, Japan
5
Department of Biology, Fujita Health University, Toyoake, Aichi 470-1192, Japan
These authors contributed equally to this work.
*
Author to whom correspondence should be addressed.
Received: 7 February 2012 / Revised: 31 March 2012 / Accepted: 5 April 2012 / Published: 30 April 2012
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Abstract

A divalent cation-independent lectin—HOL-18, with cytotoxic activity against leukemia cells, was purified from a demosponge, Halichondria okadai. HOL-18 is a 72 kDa tetrameric lectin that consists of four non-covalently bonded 18 kDa subunits. Hemagglutination activity of the lectin was strongly inhibited by chitotriose (GlcNAcβ1-4GlcNAcβ1-4GlcNAc), fetuin and mucins from porcine stomach and bovine submaxillary gland. Lectin activity was stable at pH 4–12 and temperatures lower than 60 °C. Frontal affinity chromatography with 16 types of pyridylaminated oligosaccharides indicated that the lectin had an affinity for N-linked complex-type and sphingolipid-type oligosaccharides with N-acetylated hexosamines and neuramic acid at the non-reducing termini. The lectin killed Jurkat leukemia T cells and K562 erythroleukemia cells in a dose- and carbohydrate-dependent manner. View Full-Text
Keywords: cytotoxicity; frontal affinity chromatography technology; glycoprotein; Japanese black sponge (Halichondria okadai); lectin cytotoxicity; frontal affinity chromatography technology; glycoprotein; Japanese black sponge (Halichondria okadai); lectin
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Matsumoto, R.; Fujii, Y.; Kawsar, S.M.A.; Kanaly, R.A.; Yasumitsu, H.; Koide, Y.; Hasan, I.; Iwahara, C.; Ogawa, Y.; Im, C.H.; Sugawara, S.; Hosono, M.; Nitta, K.; Hamako, J.; Matsui, T.; Ozeki, Y. Cytotoxicity and Glycan-Binding Properties of an 18 kDa Lectin Isolated from the Marine Sponge Halichondria okadai. Toxins 2012, 4, 323-338.

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