Kloog Y, Ambar I, Sokolovsky M, Kochva E, Wollberg Z, Bdolah A
Department of Biochemistry, George S. Wise Faculty of Life Sciences, Tel Aviv University, Israel.
Science. 1988 Oct 14;242(4876):268-70. doi: 10.1126/science.2845579.
Sarafotoxins, a group of 21-residue cardiotoxic peptides from snake venom that induce coronary vasoconstriction, show high-affinity binding to rat atrial and brain membranes and activate the hydrolysis of phosphoinositides. Neither their binding nor their activity is affected by blockers or activators of known receptors and ion channels, suggesting that sarafotoxins act either directly on the phosphoinositide phosphodiesterase system or on a novel receptor. Their amino acid sequence shows a high degree of homology with that of endothelin, a recently described 21-residue vasoconstrictor peptide found in porcine aortic endothelium. This is remarkable, since endothelin is a natural compound of the mammalian vascular system while sarafotoxins are highly toxic components of snake venom.
沙巴毒素是一组来自蛇毒的由21个氨基酸残基组成的心脏毒性肽，可诱导冠状动脉收缩，它与大鼠心房和脑膜具有高亲和力结合，并激活磷酸肌醇的水解。它们的结合和活性均不受已知受体和离子通道的阻断剂或激活剂的影响，这表明沙巴毒素要么直接作用于磷酸肌醇磷酸二酯酶系统，要么作用于一种新型受体。它们的氨基酸序列与内皮素的氨基酸序列具有高度同源性，内皮素是最近在猪主动脉内皮中发现的一种由21个氨基酸残基组成的血管收缩肽。这很引人注目，因为内皮素是哺乳动物血管系统的天然化合物，而沙巴毒素是蛇毒的剧毒成分。
