许旺细胞和胶原合成在紫杉醇治疗的神经压迫。电子显微镜研究

Matias Röyttä , Juha Peltonen , Ville Vuorinen
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引用次数: 6

摘要

电镜观察了神经挤压对大鼠坐骨神经胶原合成的影响。粉碎的神经用紫杉醇处理,已知紫杉醇可以增加细胞质微管的数量,而损害其他细胞器,如粗内质网和高尔基复合物。将结果与未使用紫杉醇治疗的神经损伤进行比较。与完整对照组相比,损伤后两组损伤部位的胶原原纤维数量均有所增加。薄(直径30微米)的胶原纤维通常紧密排列在雪旺细胞表面,并在基底膜失去其典型完整性的区域与深部内陷相连。这表明了胶原蛋白可能分泌的部位,并进一步证明了成年损伤神经雪旺细胞能够合成纤维胶原。此外,在紫杉醇处理的神经中,约10 nm的细微原纤维与20-30 nm的细胶原原纤维之间出现端对端异常紧密的连接。微原纤维偶见胶原横带状结构。粗内质网和高尔基复合体在前胶原分子的翻译后修饰中起重要作用。紫杉醇诱导的细胞器(如高尔基复合体)的退化,也对蛋白质的分泌至关重要,因此可能导致胶原成熟缺陷,并可能部分解释胶原原纤维形成的改变。
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Schwann Cells and Collagen Synthesis in Taxol-Treated Nerve Crush. An Electron Microscopic Study

The effect of nerve crush on collagen synthesis in rat sciatic nerve was studied byelectron microscope. The crushed nerves were treated with taxol which is known to increase the amount of cytoplasmic microtubules at the expense of other cell organelles such as rough endoplasmic reticulum and Golgi complexes. The results were compared to those seen in crushed nerves without taxol treatment.

After the injury the amount of collagen fibrils increased at the site of the traumain both groups when compared to intact controls. Thin (30 mn in diameter) collagen firils were often arranged closely to the Schwann cell surface and were connected to deep invaginations in areas where the basal lamina had lost its typical integrity. This was concluded to indicate a probable site of collagen secretion and it provides further evidence that an adult injured nerve Schwann cell is capable of synthesizing fibrous collagen.

In taxol-treated nerves additional, abnormally close connection between thinmicrofibrils of about 10 nm and thin 20-30 nm collagen fibrils appeared in an end-to-end fashion. The microfibrils showed occasional collagenous transverse band like structures. The rough endoplasmic reticulum and Golgi complex play an important role in the posttranslational modifications of the procollagen molecule. Taxol-induced degeneration of cell organelles such as the Golgi complex, which is also essential in the secretion of proteins may thus lead to defective maturation of collagen and may explain partly the altered collagen fibril formation.

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