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Immunohistochemical study of cytoskeletal and extracellular matrix components in the notochord and notochordal sheath of amphioxus

机译:两栖动物脊索和脊索鞘细胞骨架和细胞外基质成分的免疫组织化学研究

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A major cytoskeletal and extracellular matrix proteins of the amphioxus notochordal cells and sheath were detected by immunohistochemical techniques. The three-layered amphioxus notochordal sheath strongly expressed fish collagen type I in its outer and middle layers, while in the innermost layer expression did not occur. The amphioxus notochordal sheath was reactive to applied anti-human antibodies for intermediate filament proteins such as cytokeratins, desmin and vimentin, as well as to microtubule components (?-tubulin), particularly in the area close to the epipharyngeal groove. Alpha-smooth muscle actin was expressed in some notochordal cells and in the area of the notochordal attachment to the sheath. Thus muscular nature of notochordal cells was shown by immunohistochemistry in tissue section. Our results confirm that genes encoding intermediate filament proteins, microtubules and microfilaments are highly conserved during evolution. Collagen type I was proven to be the key extracellular matrix protein that forms the amphioxus notochordal sheath.
机译:免疫组化技术检测到了两栖动物脊索细胞和鞘细胞的主要细胞骨架和细胞外基质蛋白。三层的两栖动物的脊索鞘在其外层和中层强烈表达I型鱼胶原蛋白,而在最内层不表达。两栖动物的脊索鞘对所应用的抗人抗体具有反应性,这些抗体适用于中间丝蛋白(例如细胞角蛋白,结蛋白和波形蛋白)以及微管成分(β-微管蛋白),特别是在靠近上咽沟的区域。 α-平滑肌肌动蛋白在一些脊索细胞中以及在与脊索的脊索附着区域表达。因此,通过组织切片的免疫组织化学显示了脊索细胞的肌肉性质。我们的结果证实,在进化过程中,编码中间丝蛋白,微管和微丝的基因高度保守。事实证明,I型胶原是形成两栖动物脊索鞘的关键细胞外基质蛋白。

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