Mata M, Fink D J
Neurology Research Laboratory, University of Michigan, Ann Arbor.
Brain Res. 1988 Dec 20;475(2):297-304. doi: 10.1016/0006-8993(88)90618-x.
We used electron microscopic immunocytochemistry to study the distribution of calmodulin in rat sciatic nerve. Calmodulin immunoreactivity was found throughout the axoplasmic matrix, but particularly along microtubules. Schwann cell cytoplasm and nuclei demonstrated immunoreactivity, while compact myelin did not. There was particularly intense immuno-gold deposition within Schmidt Lanterman clefts. At the nodes of Ranvier, calmodulin appeared preferentially in the paranodal region, along the apposition of the axolemma to the paranodal loops of myelin and extending into the paranodal loops. The presence of calmodulin immunoreactivity along microtubules supports biochemical and pharmacological evidence of calmodulin involvement in regulating the assembly and phosphorylation of microtubules, and in fast axonal transport along microtubules. The co-localization of paranodal calmodulin immunoreactivity with Ca-ATPase activity demonstrated cytochemically (Mata et al., Brain Research, in press) supports the notion that the paranodal Ca-ATPase activity may be regulated by calmodulin, and agrees with the in vitro biochemical evidence for Ca-ATPase of other cells.
我们运用电子显微镜免疫细胞化学技术研究钙调蛋白在大鼠坐骨神经中的分布。在整个轴浆基质中均发现了钙调蛋白免疫反应性,尤其是沿着微管分布。施万细胞的细胞质和细胞核呈现免疫反应性,而致密髓鞘则无。在施密特-兰特尔曼切迹内有特别强烈的免疫金沉积。在郎飞结处,钙调蛋白优先出现在结旁区域,沿着轴膜与髓鞘结旁环的附着处并延伸至结旁环。沿着微管存在钙调蛋白免疫反应性,这支持了钙调蛋白参与调节微管组装和磷酸化以及沿着微管进行快速轴突运输的生化和药理学证据。结旁钙调蛋白免疫反应性与通过细胞化学方法证实的钙-ATP酶活性(Mata等人,《脑研究》,即将发表)的共定位支持了结旁钙-ATP酶活性可能受钙调蛋白调节的观点,并且与其他细胞的钙-ATP酶的体外生化证据相符。