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

Research output: Contribution to journalArticlepeer-review

20 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 languageEnglish
Pages (from-to)323-338
Number of pages16
JournalToxins
Volume4
Issue number5
DOIs
Publication statusPublished - 05-2012

All Science Journal Classification (ASJC) codes

  • Toxicology
  • Health, Toxicology and Mutagenesis

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