Cytotoxicity and glycan-binding properties of an 18 kDa lectin isolated from the marine sponge Halichondria okadai

Ryo Matsumoto; Yuki Fujii; Sarkar M.A. Kawsar; Robert A. Kanaly; Hidetaro Yasumitsu; Yasuhiro Koide; Imtiaj Hasan; Chihiro Iwahara; Yukiko Ogawa; Chang Hun Im; Shigeki Sugawara; Masahiro Hosono; Kazuo Nitta; Jiharu Hamako; Taei Matsui; Yasuhiro Ozeki

doi:10.3390/toxins4050323

Cytotoxicity and glycan-binding properties of an 18 kDa lectin isolated from the marine sponge Halichondria okadai

Ryo Matsumoto, Yuki Fujii, Sarkar M.A. Kawsar, Robert A. Kanaly, Hidetaro Yasumitsu, Yasuhiro Koide, Imtiaj Hasan, Chihiro Iwahara, Yukiko Ogawa, Chang Hun Im, Shigeki Sugawara, Masahiro Hosono, Kazuo Nitta, Jiharu Hamako, Taei Matsui, Yasuhiro Ozeki

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33 Citations (Scopus)

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.

Original language	English
Pages (from-to)	323-338
Number of pages	16
Journal	Toxins
Volume	4
Issue number	5
DOIs	https://doi.org/10.3390/toxins4050323
Publication status	Published - 05-2012

All Science Journal Classification (ASJC) codes

Toxicology
Health, Toxicology and Mutagenesis

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.3390/toxins4050323

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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. (2012). Cytotoxicity and glycan-binding properties of an 18 kDa lectin isolated from the marine sponge Halichondria okadai. Toxins, 4(5), 323-338. https://doi.org/10.3390/toxins4050323

@article{6c63ebb270064121b58b2c329ffbca2e,

title = "Cytotoxicity and glycan-binding properties of an 18 kDa lectin isolated from the marine sponge Halichondria okadai",

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.",

author = "Ryo Matsumoto and Yuki Fujii and Kawsar, {Sarkar M.A.} and Kanaly, {Robert A.} and Hidetaro Yasumitsu and Yasuhiro Koide and Imtiaj Hasan and Chihiro Iwahara and Yukiko Ogawa and Im, {Chang Hun} and Shigeki Sugawara and Masahiro Hosono and Kazuo Nitta and Jiharu Hamako and Taei Matsui and Yasuhiro Ozeki",

year = "2012",

month = may,

doi = "10.3390/toxins4050323",

language = "English",

volume = "4",

pages = "323--338",

journal = "Toxins",

issn = "2072-6651",

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}

Matsumoto, R, Fujii, Y, Kawsar, SMA, Kanaly, RA, Yasumitsu, H, Koide, Y, Hasan, I, Iwahara, C, Ogawa, Y, Im, CH, Sugawara, S, Hosono, M, Nitta, K, Hamako, J, Matsui, T & Ozeki, Y 2012, 'Cytotoxicity and glycan-binding properties of an 18 kDa lectin isolated from the marine sponge Halichondria okadai', Toxins, vol. 4, no. 5, pp. 323-338. https://doi.org/10.3390/toxins4050323

TY - JOUR

T1 - Cytotoxicity and glycan-binding properties of an 18 kDa lectin isolated from the marine sponge Halichondria okadai

AU - Matsumoto, Ryo

AU - Fujii, Yuki

AU - Kawsar, Sarkar M.A.

AU - Kanaly, Robert A.

AU - Yasumitsu, Hidetaro

AU - Koide, Yasuhiro

AU - Hasan, Imtiaj

AU - Iwahara, Chihiro

AU - Ogawa, Yukiko

AU - Im, Chang Hun

AU - Sugawara, Shigeki

AU - Hosono, Masahiro

AU - Nitta, Kazuo

AU - Hamako, Jiharu

AU - Matsui, Taei

AU - Ozeki, Yasuhiro

PY - 2012/5

Y1 - 2012/5

N2 - 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.

AB - 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.

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JO - Toxins

JF - Toxins

IS - 5

ER -

Cytotoxicity and glycan-binding properties of an 18 kDa lectin isolated from the marine sponge Halichondria okadai

Abstract

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