Bridgman Paul C
Dept. of Anatomy and Neurobiology, Washington University School of Medicine, St. Louis, Missouri 63110, USA.
Cell Motil Cytoskeleton. 2002 Jun;52(2):91-6. doi: 10.1002/cm.10038.
Nonmuscle myosin II is among the most abundant forms of myosin in nerve growth cones. At least two isoforms of myosin II (A and B) that have overlapping but distinct distributions are found in growth cones. It appears that both myosin IIA and IIB may be necessary for normal nerve outgrowth and motility, but the molecular interactions responsible for their activity remain unclear. For instance, it is unknown if these myosin II isoforms produce bipolar "minifilaments" in growth cones similar to those observed in other nonmuscle cells. To determine if minifilaments are present in growth cones, we modified the electron microscopy preparative procedures used to detect minifilaments in other cell types. We found structures that appeared very similar to bipolar minifilaments found in noneuronal cells. They also labeled with antibodies to either myosin IIA or IIB. Thus, the activity of myosin II in growth cones is likely to be similar to that in other nonmuscle cells. Bipolar filaments interacting with oppositely oriented actin filaments will produce localized contractions or exert tension on actin networks. This activity will be responsible for the myosin II dependent motility in growth cones.
非肌肉肌球蛋白II是神经生长锥中最丰富的肌球蛋白形式之一。在生长锥中发现了至少两种分布重叠但又不同的肌球蛋白II同工型(A和B)。似乎肌球蛋白IIA和IIB对于正常的神经生长和运动可能都是必需的,但其活性所涉及的分子相互作用仍不清楚。例如,尚不清楚这些肌球蛋白II同工型在生长锥中是否会产生类似于在其他非肌肉细胞中观察到的双极“微丝”。为了确定生长锥中是否存在微丝,我们改进了用于检测其他细胞类型中微丝的电子显微镜制备程序。我们发现了与非神经元细胞中发现的双极微丝非常相似的结构。它们也能用抗肌球蛋白IIA或IIB的抗体进行标记。因此,生长锥中肌球蛋白II的活性可能与其他非肌肉细胞中的相似。与相反方向的肌动蛋白丝相互作用的双极丝将产生局部收缩或对肌动蛋白网络施加张力。这种活性将导致生长锥中依赖于肌球蛋白II的运动。