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

visiting faculty

Research output: Contribution to journal › Article › peer-review

41 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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number = "5",

}

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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AN - SCOPUS:84861523786

SN - 2072-6651

VL - 4

SP - 323

EP - 338

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

All Science Journal Classification (ASJC) codes

UN SDGs

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