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

被引：28

作者：

Matsumoto, Ryo ^{[1
]}

Fujii, Yuki ^{[1
,2
,6
]}

Kawsar, Sarkar M. A. ^{[1
,3
]}

Kanaly, Robert A. ^{[1
]}

Yasumitsu, Hidetaro ^{[1
]}

Koide, Yasuhiro ^{[1
]}

Hasan, Imtiaj ^{[1
]}

Iwahara, Chihiro ^{[1
]}

Ogawa, Yukiko ^{[2
,6
]}

Im, Chang Hun ^{[4
]}

Sugawara, Shigeki ^{[4
]}

Hosono, Masahiro ^{[4
]}

Nitta, Kazuo ^{[4
]}

Hamako, Jiharu ^{[5
]}

Matsui, Taei ^{[5
]}

Ozeki, Yasuhiro ^{[1
]}

机构：

[1] Yokohama City Univ, Grad Sch NanoBio Sci, Dept Genome Syst Sci, Lab Glycobiol & Marine Biochem,Kanazawa Ku, Yokohama, Kanagawa 2360027, Japan

[2] Nagasaki Int Univ, Fac Pharmaceut Sci, Dept Pharm, Div Funct Morphol, Nagasaki 8593298, Japan

[3] Univ Chittagong, Fac Sci, Dept Chem, Lab Carbohydrate & Prot Chem, Chittagong 4221, Bangladesh

[4] Tohoku Pharmaceut Univ, Inst Mol Biomembrane & Glycobiol, Div Cell Recognit Study, Aoba Ku, Sendai, Miyagi 9818558, Japan

[5] Fujita Hlth Univ, Dept Biol, Toyoake, Aichi 4701192, Japan

[6] Nagasaki Int Univ, Div Microbiol, Dept Pharm, Fac Pharmaceut Sci, Nagasaki 8593298, Japan

来源：

TOXINS | 2012年 / 4卷 / 05期

基金：

日本学术振兴会;

关键词：

cytotoxicity; frontal affinity chromatography technology; glycoprotein Japanese black sponge (Halichondria okadai); lectin; PROTEIN; CELLS; OLIGOSACCHARIDE; SILICATEIN; ACID;

D O I：

10.3390/toxins4050323

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

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 (GlcNAc beta 1-4GlcNAc beta 1-4GlcNAc), fetuin and mucins from porcine stomach and bovine submaxillary gland. Lectin activity was stable at pH 4-12 and temperatures lower than 60 degrees 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.

引用

页码：323 / 338

页数：16

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