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Potent inhibition of dynein adenosinetriphosphatase and of the motility of cilia and sperm flagella by vanadate.钒酸盐对动力蛋白三磷酸腺苷酶以及纤毛和精子鞭毛运动的强力抑制作用。
Proc Natl Acad Sci U S A. 1978 May;75(5):2220-4. doi: 10.1073/pnas.75.5.2220.
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3
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Metabolism of trace amounts of vanadium 48 in rat organs and liver subcellular particles.
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Possible transition-state analogs for ribonuclease. The complexes of uridine with oxovanadium(IV) ion and vanadium(V) ion.核糖核酸酶可能的过渡态类似物。尿苷与氧钒(IV)离子和钒(V)离子的配合物。
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Letter: Transition metal ion inhibition of enzyme-catalyzed phosphate ester displacement reactions.信函:过渡金属离子对酶催化的磷酸酯置换反应的抑制作用。
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Some properties of bound and soluble dynein from sea urchin sperm flagella.海胆精子鞭毛中结合态与可溶性动力蛋白的一些特性
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Flagellar movement and adenosine triphosphatase activity in sea urchin sperm extracted with triton X-100.用曲拉通X-100提取的海胆精子中的鞭毛运动和三磷酸腺苷酶活性
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The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin.兔骨骼肌收缩的调节。I. 原肌球蛋白-肌钙蛋白复合物与肌动蛋白及肌球蛋白蛋白水解片段相互作用的生化研究。
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Calcium ion regulation of flagellar beat symmetry in reactivated sea urchin spermatozoa.钙离子对再活化海胆精子鞭毛摆动对称性的调节
Biochem Biophys Res Commun. 1974 Jun 4;58(3):795-800. doi: 10.1016/s0006-291x(74)80487-0.
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Vanadium ion inhibition of alkaline phosphatase-catalyzed phosphate ester hydrolysis.钒离子对碱性磷酸酶催化的磷酸酯水解的抑制作用。
Arch Biochem Biophys. 1976 Jul;175(1):31-8. doi: 10.1016/0003-9861(76)90482-3.
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Vanadate is a potent (Na,K)-ATPase inhibitor found in ATP derived from muscle.
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钒酸盐对动力蛋白三磷酸腺苷酶以及纤毛和精子鞭毛运动的强力抑制作用。

Potent inhibition of dynein adenosinetriphosphatase and of the motility of cilia and sperm flagella by vanadate.

作者信息

Gibbons I R, Cosson M P, Evans J A, Gibbons B H, Houck B, Martinson K H, Sale W S, Tang W J

出版信息

Proc Natl Acad Sci U S A. 1978 May;75(5):2220-4. doi: 10.1073/pnas.75.5.2220.

DOI:10.1073/pnas.75.5.2220
PMID:149986
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC392523/
Abstract

The motility of demembranated sea urchin sperm flagella and that of embryo cilia reactivated with 0.1 mM ATP are completely inhibited by 4 micron and 0.5 micron vanadium(V) [V(V), in vanadate], respectively. The Mg2+-activated ATPase activity (ATP phosphohydrolase, EC 3.6.1.3)of the latent form of dynein 1 is inhibited 50% by 0.5-1 micron V(V), while the Ca2+-activated ATPase activity is much less sensitive. The inhibition of flagellar beat frequency and of dynein 1 ATPase activity by V(V) appears not to be competitive with ATP. In agreement with other reports, the inhibition of (Na,K)-ATPase by V(V) shows a slow onset in the presence of ATP and is relatively rapid in its absence. With dynein, however, the inhibition occurs at a rapid rate whether or not ATP is present. Catechol at a concentration of 1 mM reverses the V(V) inhibition of reactivated sperm motility, dynein ATPase, and (Na, K)-ATPase. Myosin and actomyosin ATPases show no inhibition by concentrations of V(V) up to 500 micron. The inhibition by V(V) provides a possible technique for distinguishing between the actions of dynein and myosin in different forms of cell motility.

摘要

用0.1 mM ATP重新激活的去膜海胆精子鞭毛的运动性以及胚胎纤毛的运动性,分别被4微米和0.5微米的钒(V)[钒酸盐中的V(V)]完全抑制。动力蛋白1潜在形式的Mg2+激活的ATP酶活性(ATP磷酸水解酶,EC 3.6.1.3)被0.5 - 1微米的V(V)抑制50%,而Ca2+激活的ATP酶活性对其敏感性要低得多。V(V)对鞭毛摆动频率和动力蛋白1 ATP酶活性的抑制似乎与ATP不存在竞争性。与其他报道一致,V(V)对(Na,K)-ATP酶的抑制在有ATP存在时起效缓慢,而在无ATP时相对较快。然而,对于动力蛋白,无论是否存在ATP,抑制都快速发生。1 mM浓度的儿茶酚可逆转V(V)对重新激活的精子运动性、动力蛋白ATP酶和(Na,K)-ATP酶的抑制作用。肌球蛋白和肌动球蛋白ATP酶在高达500微米的V(V)浓度下未显示出抑制作用。V(V)的抑制作用为区分动力蛋白和肌球蛋白在不同形式细胞运动中的作用提供了一种可能的技术。