Shaw G, Weber K
Nature. 1982 Jul 15;298(5871):277-9. doi: 10.1038/298277a0.
Axonal transport studies and biochemical fractionation have led to the concept that the three 'triplet' proteins [approximate molecular weights 200,000 (200K), 145,000 (145K) and 68,000 (68K)] are the essential components of mammalian neurofilaments. Using a correlated biochemical and immunological approach, we have now shown that the 200K protein is under separate developmental control during rat brain differentiation and that the time of its expression differs in different regions. We were unable to detect 200K protein by immunofluorescence or in total brain filament preparations from prenatal rat brain, although the 145K and 68K proteins are both present in an apparently identical distribution. During development, progressively more 145K- and 68K-positive neurofilamentous bundles can be stained with 200K antibodies, paralleling the increasing quantities of this protein detected biochemically in brain filament preparations. We conclude that 200K protein probably has a more specialized role in neurofilament architecture and function than the other two triplet proteins.
轴突运输研究和生化分级分离引出了这样一个概念，即三种“三联体”蛋白[近似分子量分别为200,000（200K）、145,000（145K）和68,000（68K）]是哺乳动物神经丝的基本组成成分。运用生化与免疫学相结合的方法，我们现已表明，在大鼠脑分化过程中，200K蛋白受独立的发育调控，且其表达时间在不同脑区有所不同。尽管145K和68K蛋白在产前大鼠脑的分布明显相同，但通过免疫荧光法或从产前大鼠脑的全脑丝体制备物中，我们均未能检测到200K蛋白。在发育过程中，越来越多的145K和68K阳性神经丝束能用200K抗体染色，这与在脑丝体制备物中生化检测到的该蛋白数量增加情况相一致。我们得出结论，与其他两种三联体蛋白相比，200K蛋白在神经丝结构和功能中可能具有更特殊的作用。
