Drenckhahn D, Kaiser H W
Eur J Cell Biol. 1983 Sep;31(2):235-40.
Fluorescent staining with phalloidin, a specific probe for F-actin, and antibodies to non-muscle myosin from thymus was used to localize actin and myosin in brain neurons of the rat. Phalloidin and anti-myosin displayed a preferential affinity for synaptic formations in the cerebellum, the brain stem, the spinal cord and the retina. The conclusion that F-actin and myosin are concentrated in synaptic terminals was further established by simultaneous staining of isolated rat brain synaptosomes with phalloidin and anti-thymus myosin as well as by the demonstration of a selective affinity of anti-thymus myosin for a 200 000-Mr protein band in gel electrophoretograms of synaptic fractions. Apart from synaptic areas, phalloidin and anti-thymus myosin reacted also, albeit rather weakly, with a narrow circumferential layer located in the area of the plasma membrane of virtually all axons in the white matter and the spinal roots. The spatial coexistence of myosin and actin in brain synapses and axons is of particular interest in view of various dynamic functions that have been proposed for axonal and synaptic actin.
用鬼笔环肽（一种针对F-肌动蛋白的特异性探针）以及来自胸腺的非肌肉肌球蛋白抗体进行荧光染色，以定位大鼠脑神经元中的肌动蛋白和肌球蛋白。鬼笔环肽和抗肌球蛋白对小脑、脑干、脊髓和视网膜中的突触结构表现出优先亲和力。通过用鬼笔环肽和抗胸腺肌球蛋白同时对分离的大鼠脑突触体进行染色，以及通过在突触组分的凝胶电泳图中证明抗胸腺肌球蛋白对200 000道尔顿蛋白带的选择性亲和力，进一步证实了F-肌动蛋白和肌球蛋白集中在突触终末的结论。除了突触区域外，鬼笔环肽和抗胸腺肌球蛋白还与位于白质和脊髓神经根中几乎所有轴突质膜区域的狭窄圆周层发生反应，尽管反应相当微弱。鉴于已提出的轴突和突触肌动蛋白的各种动态功能，肌球蛋白和肌动蛋白在脑突触和轴突中的空间共存特别令人感兴趣。
