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首页> 外文期刊>The biochemical journal >The route of secretion of procollagen. The influence of αα′-bipyridyl, colchicine and antimycin A on the secretory process in embryonic-chick tendon and cartilage cells
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The route of secretion of procollagen. The influence of αα′-bipyridyl, colchicine and antimycin A on the secretory process in embryonic-chick tendon and cartilage cells

机译：Procollagen的分泌途径。 α'-双吡啶基，秋嘧啶和抗霉素A对胚胎肌腱和软骨细胞分泌过程的影响

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pI. Embryonic-chick tendon cells were pulse-labelled for 4 min with [14C]proline and the 14C-labelled polypeptides were chased with unlabelled proline for up to 30 min. Isolation of subcellular fractions during the chase period and their subsequent analysis for bacterial collagenase-susceptible 14C-labelled peptides demonstrated the transfer of procollagen polypeptides from rough to smooth microsomal fractions and thence to the extracellular medium. Parallel analyses of Golgi-enriched fractions indicated the involvement of this organelle in the secretory pathway of procollagen. Sodium dodecylsulphate/polyacrylamide-gel electrophoresis of the 14C-labelled polypeptides present in the Golgi-enriched fractions demonstrated that the procollagen polypeptides were all present as disulphide-linked pro-gamma components. 2. When similar kinetic studies of the intracellular transport of procollagen were conducted with embryonic-chick cartilage cells almost identical results were obtained, but the rate of translocation of cartilage procollagen was significantly slower than that observed for tendon procollagen. 3. When hydroxylation of procollagen polypeptides was inhibited by alphaalpha′-bipyridyl, the nascent polypeptides accumulated in the rough microsomal fraction. 4. When cells were pulse-labelled for 4min with [14C)proline and the label was chased in the presence of colchicine, secretion of procollagen was inhibited and an intracellular accumulation of procollagen 14C-labelled polypeptides was observed in the Golgi-enriched fractions. 5. The energy-dependence of the intracellular transport of procollagen was demonstrated in experiments in which antimycin A was found to inhibit the transfer of procollagen polypeptides from rough to smooth endoplasmic reticulum. 6. It is concluded that procollagen follows the classical route of secretion taken by other extracellular proteins./p
机译：> i。将胚胎肌腱细胞用[14C]脯氨酸脉冲标记4分钟，并将14℃标记的多肽用未标记的脯氨酸序列追加至30分钟。在追逐期间的亚细胞级分的分离及其随后的细菌胶原酶溶解的14C标记肽的分析证明了Procollagen多肽从粗糙到光滑的微薄馏分和该细胞外培养基的转移。富集的级分的平行分析表明了该细胞器在寄生虫分泌途径中的累积。在富含富硫级分的级分中存在的14℃标记多肽的十二烷基硫酸盐/聚丙烯酰胺 - 凝胶电泳表明，前胶原多肽全部存在为二硫化物连接的PROMMA组分。 2.当对胚胎软骨细胞进行胚胎的细胞内运输的类似动力学研究几乎获得了相同的结果，但软骨晶状体易位率明显慢于肌腱下常胶凝中观察到的速度。 3.当通过α-Bi丝吡啶抑制原胶拉拉格多肽的羟基化时，在粗略微粒体中累积的新生多肽。 4.当细胞用[14℃）脯氨酸脉冲标记4min时，在血清序列存在下追加标记，抑制了原胶原的分泌，并在富含富含富巯基的级分中观察到寄生虫14c标记多肽的细胞内积累。 5.在实验中对抗霉素A的实验证明了预胶凝中的细胞内传输的能量依赖性抑制粗霉素A从粗糙到光滑的内质网的转移。 6.得出结论，ProCollagen遵循其他细胞外蛋白的经典分泌途径。

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