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
Ryo Matsumoto 1,†, Yuki Fujii 1,2,†, Sarkar M. A. Kawsar 1,3, Robert A. Kanaly 1, Hidetaro Yasumitsu 1, Yasuhiro Koide 1, Imtiaj Hasan 1
, Chihiro Iwahara 1, Yukiko Ogawa 2, Chang Hun Im 4, Shigeki Sugawara 4, Masahiro Hosono 4, Kazuo Nitta 4, Jiharu Hamako 5, Taei Matsui 5 and Yasuhiro Ozeki 1,*
, Chihiro Iwahara 1, Yukiko Ogawa 2, Chang Hun Im 4, Shigeki Sugawara 4, Masahiro Hosono 4, Kazuo Nitta 4, Jiharu Hamako 5, Taei Matsui 5 and Yasuhiro Ozeki 1,*
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
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-TextKeywords:
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.