Specific inhibition of binding of antistasin and [A103,106,108] antistasin 93–119 to sulfatide (Gal(3‐SO4)β1‐1Cer) by glycosaminoglycans

FEBS Letters

Manley, George D.¹  Brankamp, Robert G.¹  Cardin, Alan D.¹  Krstenansky, John L.²  Owen, Thomas J.¹ 

[1] Marion Merrell Dow Research Institute, 2110 East Galbraith Rd, Cincinnati, OH 45215, USA;Syntex Research, 3401 Hillview Ave., Palo Alto, CA 94303, USA

关键词: Antistasin;    Ghilanten;    Haementeria;    Sulfatide;    Glycosaminoglycans;    Leech;   

DOI  :  10.1016/0014-5793(92)80366-O

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Leech-derived antistasin is a potent anticoagulant and antimetastatic protein that binds sulfatide (Gal(3-SO4)β1-1Cer)and sulfated polysaccharides. In this study, the synthetic fragment [A^103,106,108] antistasin 93–119, which corresponds to the carboxyl terminus, showed specific and saturable binding to sulfatide. Binding was competitively blocked by glycosaminoglycans (GAGs) in the order: dextran sulfate 5000 ≅ dextran sulfate 500 0OO > heparin > dermatan sulfate ⪢ chondroitin sulfates A and C. This rank order of inhibitory potency was identical to that observed with whole antistasin. We suggest that residues 93–119 of antistasin represent a critical domain for binding GAGs and sulfated glycolipids.

【 授权许可】

Unknown