Takubo T, Hino M, Suzuki K, Tatsumi N
Department of Clinical and Laboratory Medicine, Osaka City University Medical School, Japan.
Eur J Histochem. 1999;43(1):71-7.
The characteristic amoeboid movement of human leucocytes uses mechanical energy derived from the hydrolysis of adenosine triphosphate through a mechanochemical system of the contractile proteins myosin, actin, and the actin-associated protein alpha-actinin. We observed the relative distribution of myosin, actin, and alpha-actinin in adherent monocytes during movement by a double-fluorescence staining procedure. The results indicate that myosin and alpha-actinin are closely associated with the actin cable network, and that alpha-actinin is in close association with the plasma membrane and anchors filamentous actin (F-actin) beneath the plasma membrane; F-actin and alpha-actinin play an important role at the leading edge during the formation of lamellipodia. These findings should be helpful in clarifying the mechanism of leucocyte movement from a morphologic standpoint.
人类白细胞特有的阿米巴样运动利用的机械能源自三磷酸腺苷的水解,该过程通过收缩蛋白肌球蛋白、肌动蛋白以及与肌动蛋白相关的蛋白质α-辅肌动蛋白组成的机械化学系统来实现。我们通过双荧光染色程序观察了贴壁单核细胞运动过程中肌球蛋白、肌动蛋白和α-辅肌动蛋白的相对分布。结果表明,肌球蛋白和α-辅肌动蛋白与肌动蛋白丝网络紧密相关,且α-辅肌动蛋白与质膜紧密相连,并将丝状肌动蛋白(F-肌动蛋白)锚定在质膜下方;在片状伪足形成过程中,F-肌动蛋白和α-辅肌动蛋白在前沿发挥着重要作用。这些发现应有助于从形态学角度阐明白细胞运动的机制。