Biological and Pharmaceutical Bulletin
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Natural Killer Group 2A (NKG2A) and Natural Killer Group 2C (NKG2C) Bind to Sulfated Glycans and α2,3-NeuAc-containing Glycoproteins
Xin XinKoji HigaiYuzo ImaizumiChiho SuzukiKenichiro ItoAyumi ItohSayo MatsumotoYutaro AzumaKojiro Matsumoto
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2011 Volume 34 Issue 4 Pages 480-485

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Abstract

Killer lectin-like receptors on natural killer (NK) cells mediate cytotoxicity through glycans on target cells. We prepared recombinant glutathione S-transferase-fused extracellular lectin-like domains (AA 94-231) of natural killer group 2A (NKG2A) (rGST-NKG2A) and NKG2C (rGST-NKG2C) and determined the binding of these receptors to plates coated with heparin-conjugated bovine serum albumin (heparin-BSA) and glycoproteins. rGST-NKG2A and rGST-NKG2C directly bound to heparin-BSA with Kd values of 20 and 40 nM, respectively. Binding of rGST-NKG2A and rGST-NKG2C to heparin-BSA was suppressed in the presence of soluble heparin, heparan sulfate, fucoidan, λ-carrageenan, and dextran sulfate. 2-O-Sulfate residues in heparin were essential for the binding of rGST-NKG2A and rGST-NKG2C. Moreover, rGST-NKG2A and rGST-NKG2C bound to multimeric sialyl Lewis X expressing transferrin secreted by HepG2 cells with Kd values of 80 and 114 nM, respectively. This is the first report showing that NKG2A and NKG2C bind to heparin and α2,3-NeuAc-containing glycoproteins.

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© 2011 The Pharmaceutical Society of Japan
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