%0 Journal Article
%T Cytotoxicity and Glycan-Binding Properties of an 18 kDa Lectin Isolated from the Marine Sponge Halichondria okadai
%A Ryo Matsumoto
%A Yuki Fujii
%A Sarkar M. A. Kawsar
%A Robert A. Kanaly
%A Hidetaro Yasumitsu
%A Yasuhiro Koide
%A Imtiaj Hasan
%A Chihiro Iwahara
%A Yukiko Ogawa
%A Chang Hun Im
%A Shigeki Sugawara
%A Masahiro Hosono
%A Kazuo Nitta
%A Jiharu Hamako
%A Taei Matsui
%A Yasuhiro Ozeki
%J Toxins
%D 2012
%I MDPI AG
%R 10.3390/toxins4050323
%X A divalent cation-independent lectin¡ªHOL-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¦Â1-4GlcNAc¦Â1-4GlcNAc), fetuin and mucins from porcine stomach and bovine submaxillary gland. Lectin activity was stable at pH 4¨C12 and temperatures lower than 60 ¡ãC. 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.
%K cytotoxicity
%K frontal affinity chromatography technology
%K glycoprotein
%K Japanese black sponge (Halichondria okadai)
%K lectin
%U http://www.mdpi.com/2072-6651/4/5/323