Lo W K, Mills A, Kuck J F
Department of Anatomy, Morehouse School of Medicine, Atlanta, GA 30310.
Exp Eye Res. 1994 Feb;58(2):189-96. doi: 10.1006/exer.1994.1007.
A unique association between actin filament bundles and gap junctions in cortical fiber cells of human and monkey lenses was studied with thin-section electron microscopy and immunocytochemistry. Thin-section electron microscopy showed that distinct layers of filament bundles (approximately 55 nm thick) were consistently associated with fiber gap junctions (approximately 16 nm thick) from intermediate to deep cortical regions in both species studied. The filament bundle was composed of 6-8 nm microfilaments which lay along both cytoplasmic surfaces of the junction. Fluorescence microscopy revealed a patchy pattern of F-actin labeling along the fiber cell membranes in the intermediate and deep cortical regions of the lens. The size and distribution pattern of F-actin labeling appear to correlate well with those of filament bundles/gap junctions seen in thin-section electron microscopy. By immunoelectron microscopy, the anti-actin antibody was shown to be localized to filament bundles/gap junctions in the intermediate cortical fibers of human lens, indicating that filament bundles are F-actin in nature. The identical filament bundle/gap junction association was not found in other species examined, including rodent, bird and fish, by the same procedure, suggesting that an association between actin bundles and gap junctions has a special functional role in the primate lens. It is proposed that gap junction-associated actin bundles may provide added structural stability for the primate lens.
利用超薄切片电子显微镜和免疫细胞化学技术,研究了人类和猴子晶状体皮质纤维细胞中肌动蛋白丝束与缝隙连接之间的独特关联。超薄切片电子显微镜显示,在研究的两个物种中,从中间皮质区域到深层皮质区域,不同层的丝束(约55纳米厚)始终与纤维缝隙连接(约16纳米厚)相关联。丝束由6 - 8纳米的微丝组成,这些微丝沿着连接的两个细胞质表面排列。荧光显微镜显示,在晶状体中间和深层皮质区域的纤维细胞膜上,F - 肌动蛋白标记呈斑点状分布。F - 肌动蛋白标记的大小和分布模式似乎与超薄切片电子显微镜中看到的丝束/缝隙连接的大小和分布模式密切相关。通过免疫电子显微镜观察,抗肌动蛋白抗体显示定位于人类晶状体中间皮质纤维中的丝束/缝隙连接,表明丝束本质上是F - 肌动蛋白。通过相同的程序,在包括啮齿动物、鸟类和鱼类在内的其他被检查物种中未发现相同的丝束/缝隙连接关联,这表明肌动蛋白束与缝隙连接之间的关联在灵长类晶状体中具有特殊的功能作用。有人提出,与缝隙连接相关的肌动蛋白束可能为灵长类晶状体提供额外的结构稳定性。