Cloning and characterization of novel snake venom proteins that block smooth muscle contraction

被引:126
作者
Yamazaki, Y
Koike, H
Sugiyama, Y
Motoyoshi, K
Wada, T
Hishinuma, S
Mita, M
Morita, T
机构
[1] Meiji Pharmaceut Univ, Dept Biochem, Tokyo 2048588, Japan
[2] Meiji Pharmaceut Univ, Dept Pharmacodynam, Tokyo 2048588, Japan
来源
EUROPEAN JOURNAL OF BIOCHEMISTRY | 2002年 / 269卷 / 11期
关键词
snake venom; neurotoxin; helothermine; cysteine-rich secretory proteins; ablomin;
D O I
10.1046/j.1432-1033.2002.02940.x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
In this study, we isolated a 25-kDa novel snake venom protein, designated ablomin, from the venom of the Japanese Mamushi snake (Agkistrodon blomhoffi ). The amino-acid sequence of this protein was determined by peptide sequencing and cDNA cloning. The deduced sequence showed high similarity to helothermine from the Mexican beaded lizard (Heloderma horridum horridum ), which blocks voltage-gated calcium and potassium channels, and ryanodine receptors. Ablomin blocked contraction of rat tail arterial smooth muscle elicited by high K+ -induced depolarization in the 0.1-1 mum range, but did not block caffeine-stimulated contraction. Furthermore, we isolated three other proteins from snake venoms that are homologous to ablomin and cloned the corresponding cDNAs. Two of these homologous proteins, triflin and latisemin, also inhibited high K+ -induced contraction of the artery. These results indicate that several snake venoms contain novel proteins with neurotoxin-like activity.
引用
收藏
页码:2708 / 2715
页数:8
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