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

客員教員

研究成果: ジャーナルへの寄稿 › 学術論文 › 査読

43 被引用数 (Scopus)

抄録

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.

本文言語	英語
ページ（範囲）	323-338
ページ数	16
ジャーナル	Toxins
巻	4
号	5
DOI	https://doi.org/10.3390/toxins4050323
出版ステータス	出版済み - 05-2012

UN SDG

この成果は、次の持続可能な開発目標に貢献しています

SDG 14 海の豊かさを守ろう

All Science Journal Classification (ASJC) codes

毒物学
健康、毒物学および変異誘発

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10.3390/toxins4050323

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引用スタイル

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.",

keywords = "Cytotoxicity, Frontal affinity chromatography technology, Glycoprotein, Japanese black sponge (Halichondria okadai), Lectin",

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.

KW - Cytotoxicity

KW - Frontal affinity chromatography technology

KW - Glycoprotein

KW - Japanese black sponge (Halichondria okadai)

KW - Lectin

UR - https://www.scopus.com/pages/publications/84861523786

UR - https://www.scopus.com/pages/publications/84861523786#tab=citedBy

U2 - 10.3390/toxins4050323

DO - 10.3390/toxins4050323

M3 - Article

C2 - 22778903

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

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