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.
Highlights
Lectins are carbohydrate-binding proteins that are present among various living organisms
Unique chemicals that have attractive activities such as okadaic acid and halichondrin B, which are known to act as a phosphatase inhibitor and as an anticancer agent, respectively, are produced by symbiotic microorganisms that are isolated from the Japanese black sponge Halichondria okadai [4,5]
Frontal affinity chromatography technology (FACT) is a method by which the glycan-binding specificity of lectins may be evaluated by using various types of pyridylamino group (PA)-labeled oligosaccharides on an affinity column whereby the delay in the elution of the lectin is indicative of its binding affinity [13,14]
Summary
Lectins are carbohydrate-binding proteins that are present among various living organisms. Frontal affinity chromatography technology (FACT) is a method by which the glycan-binding specificity of lectins may be evaluated by using various types of pyridylamino group (PA)-labeled oligosaccharides on an affinity column whereby the delay in the elution of the lectin is indicative of its binding affinity [13,14]. This information in regard to the binding property of the lectin will aid in the understanding of the novel characters of each lectin. The specific glycan-binding properties and glycan-dependent cytotoxicity of an 18 kDa lectin isolated from a Japanese black sponge were evaluated
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
