Bolanos S H, Zamora D O, García D M, Koke J R
Department of Biology, Southwest Texas State University, San Marcos 78666, USA.
Cytobios. 1998;94(375):39-61.
The G.3.5 antigen (named for the monoclonal antibody which recognizes it) has been characterized as an intermediate filament-associated protein found in a variety of tissue types, including human and rat astrocytes, rat skeletal and cardiac myocytes, fibroblasts, rat hepatocytes, and chicken and fish retinal tissues. Sequencing of proteolytic fragments indicated a high degree of similarity to alpha-actinin. Comparison of the G.3.5 antigen to alpha-actinin revealed that alpha-actinin and the G.3.5 antigen migrated similarly in reducing and non-reducing environments and had similar molecular masses (approximately 100,000). Overlay-immunoblotting assays indicated that the G.3.5 antigen and alpha-actinin could bind filamentous actin and desmin simultaneously. In contrast, immunocytochemistry indicated the G.3.5 antigen and alpha-actinin were immunologically distinct in tissue sections. The results of this study suggest that the G.3.5 antigen is an isoform of alpha-actinin which may serve to cross-link intermediate filaments to microfilaments, and that other isoforms of alpha-actinin may also share this property.
G.3.5抗原(因其被识别的单克隆抗体而得名)已被鉴定为一种中间丝相关蛋白,存在于多种组织类型中,包括人和大鼠星形胶质细胞、大鼠骨骼肌和心肌细胞、成纤维细胞、大鼠肝细胞以及鸡和鱼的视网膜组织。蛋白水解片段的测序表明其与α-辅肌动蛋白高度相似。将G.3.5抗原与α-辅肌动蛋白进行比较发现,α-辅肌动蛋白和G.3.5抗原在还原和非还原环境中迁移情况相似且分子量相近(约100,000)。覆盖免疫印迹分析表明,G.3.5抗原和α-辅肌动蛋白能够同时结合丝状肌动蛋白和结蛋白。相比之下,免疫细胞化学表明,在组织切片中G.3.5抗原和α-辅肌动蛋白在免疫上是不同的。这项研究的结果表明,G.3.5抗原是α-辅肌动蛋白的一种异构体,可能有助于将中间丝与微丝交联,并且α-辅肌动蛋白的其他异构体也可能具有此特性。