Inhibition of kinesin-driven microtubule motility by monoclonal antibodies to kinesin heavy chains.
Inhibition of kinesin-driven microtubule motility by monoclonal antibodies to kinesin heavy chains.
复制标题
抑制驱动蛋白重链的单克隆抗体对运动蛋白驱动的微管运动。
DOI：
10.1083/jcb.107.6.2657
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发表时间：
1988-12
期刊：
影响因子：
--
通讯作者：
Scholey JM
中科院分区：
文献类型：
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作者：
Ingold AL;Cohn SA;Scholey JM
我们制备并鉴定了7株抗海胆卵动蛋白130-kD重链的小鼠单抗(Suk1-7)。在免疫印迹上，Suk3和Suk4与果蝇胚胎116kD的重链发生交叉反应，Suk4、Suk5、Suk6和Suk7与120kD的牛脑激肽重链结合。7种单抗中的3种(Suk 4、Suk 6和Suk 7)对海胆卵动蛋白诱导的微管移位有剂量依赖性的抑制作用，而其他4种单抗对这种运动无明显影响。抑制性单抗(Suk 4、Suk 6和Suk 7)似乎与ATP敏感的微管结合130-kD重链的45-kD糜溶片段上的空间相关部位结合，而Suk 2与空间上不同的部位结合。单抗激动素均不能抑制微管激活的激动素的镁ATPase活性，提示Suk 4、Suk 6和Suk 7使该酶的活性从运动中解偶联。
We have prepared and characterized seven mouse monoclonal antibodies (SUK 1-7) to the 130-kD heavy chain of sea urchin egg kinesin. On immunoblots, SUK 3 and SUK 4 cross-reacted with Drosophila embryo 116- kD heavy chains, and SUK 4, SUK 5, SUK 6, and SUK 7 bound to the 120-kD heavy chains of bovine brain kinesin. Three out of seven monoclonal antikinesins (SUK 4, SUK 6, and SUK 7) caused a dose-dependent inhibition of sea urchin egg kinesin-induced microtubule translocation, whereas the other four monoclonal antibodies had no detectable effect on this motility. The inhibitory monoclonal antibodies (SUK 4, SUK 6, and SUK 7) appear to bind to spatially related sites on an ATP- sensitive microtubule binding 45-kD chymotryptic fragment of the 130-kD heavy chain, whereas SUK 2 binds to a spatially distinct site. None of the monoclonal antikinesins inhibited the microtubule activated MgATPase activity of kinesin, suggesting that SUK 4, SUK 6, and SUK 7 uncouple this MgATPase activity from motility.