Booth A G, Kenny J
J Cell Sci. 1976 Aug;21(3):449-63. doi: 10.1242/jcs.21.3.449.
The vesiculation of kidney proximal tubule microvilli has been examined in tissue slices, isolated brush borders and isolated microvilli. Vesiculation could be induced in tissue slices by 2,4-dinitrophenol and anoxia. Cycloheximide and fluoride had no effect. In brush borders and microvilli, the vesiculation was found to be essentially temperature-dependent. Whilst an osmotic swelling could be produced by hypo-osmolar media, the temperature-dependent vesiculation could not be prevented in hyper-osmolar media. Of a wide variety of reagents tested, only glutaraldehyde, mercuric chloride and mersalyl were effective in arresting the vesiculation. Electron micrographs show that vesiculation involves a collapse of the internal structure of the microvillus. However, the collapse was not associated with depolymerization of the microvillus actin filaments. Rather it appeared to be due to the parting of cross-bridges between the membrane and the actin filaments. The nature of these cross-bridges is discussed: it is suggested that alpha-actinin possesses the characteristics for the cross-bridging protein and that vesiculation might be explained by the displacement of alpha-actinin by tropomyosin.
已在组织切片、分离的刷状缘和分离的微绒毛中对肾近端小管微绒毛的小泡形成进行了研究。2,4-二硝基苯酚和缺氧可在组织切片中诱导小泡形成。环己酰亚胺和氟化物无作用。在刷状缘和微绒毛中,发现小泡形成基本上与温度有关。虽然低渗介质可产生渗透性肿胀,但在高渗介质中不能阻止温度依赖性小泡形成。在测试的多种试剂中,只有戊二醛、氯化汞和汞撒利能有效阻止小泡形成。电子显微镜照片显示,小泡形成涉及微绒毛内部结构的塌陷。然而,这种塌陷与微绒毛肌动蛋白丝的解聚无关。相反,它似乎是由于膜与肌动蛋白丝之间的交叉桥分离所致。讨论了这些交叉桥的性质:有人提出α-辅肌动蛋白具有交叉桥蛋白的特征,小泡形成可能是由原肌球蛋白取代α-辅肌动蛋白来解释的。