Intracellular transport and tyrosine sulfation of procollagens V.
Intracellular transport and tyrosine sulfation of procollagens V.
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前胶原 V 的细胞内运输和酪氨酸硫酸化。
DOI：
10.1111/j.1432-1033.1986.tb09784.x
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发表时间：
1986
期刊：
影响因子：
--
通讯作者：
Fessler,JH
中科院分区：
文献类型：
--
作者：
Fessler,LI;Chapin,S;Brosh,S;Fessler,JH
细胞外 p-胶原蛋白 V 和胶原蛋白 V 的几个酪氨酸残基被硫酸化 [Fessler, L. I., Brosh, S., Chapin, S. 和 Fessler, J. H. (1986)J.生物。化学。 261, 5034–5040]。在这里，研究了它们的细胞内前体，前胶原 V 的硫酸化。鸡胚肌腱富含高尔基体的亚细胞部分催化内源性和添加的未硫酸化前胶原 V 中酪氨酸残基与硫酸盐供体 3'-磷酸腺苷 5'-[35S]磷酸硫酸盐的硫酸化。根据前胶原 V 的 N 连接碳水化合物从内切糖苷酶 H 敏感到耐药的变化来判断，原胶原 V 的细胞内酪氨酸硫酸化发生在高尔基体隔室远端的点。通过将肌腱与 3 H 标记的氨基酸和[ 35 S]硫酸盐一起孵育来测定原胶原 V 的细胞内修饰的时间过程。 proα(V) 链在大约 10 分钟内合成，然后组装成未硫酸化的前胶原 V 分子。酪氨酸硫酸化发生在多肽合成完成后50分钟，并且分子按照它们合成的顺序连续硫酸化。抗微管药物诺考达唑会破坏高尔基体的空间组织，缩短前胶原 V 合成和硫酸化之间的时间间隔。硫酸化原胶原 V 很快被分泌并切割成硫酸化 p-胶原 V。硫酸化 proα1(V) 链比硫酸化 proα1'(V) 链切割得更快。讨论了连续蛋白质修饰与空间细胞组织的关系。
Several tyrosine residues of the extracellular p‐collagens V and collagens V are sulfated [Fessler, L. I., Brosh, S., Chapin, S. and Fessler, J. H. (1986)J. Biol. Chem. 261, 5034–5040]. Here, the sulfation of their intracellular precursors, the procollagens V, was studied. A Golgi‐enriched subcellular fraction of chick embryo tendon catalyzed the sulfation of tyrosine residues in both endogenous and added, unsulfated procollagens V with the sulfate donor 3′‐phosphoadenosine 5′‐[35S]phosphosulfate. Intracellular tyrosine sulfation of procollagen V occurred at a point distal to thecisGolgi compartment as judged by change of the N‐linked carbohydrate of procollagen V from being endoglycosidase‐H‐sensitive to being resistant. The time course of the intracellular modifications of procollagen V was determined by incubating tendons with3H‐labeled amino acids and with [35S]sulfate. The proα(V) chains were synthesised in about 10 min and then assembled into unsulfated procollagen V molecules. Tyrosine sulfation occurred 50 min after completion of polypeptide synthesis and the molecules were successively sulfated in the order in which they had been synthesized. The antimicrotubular drug Nocodazole, which disrupts the spatial organization of the Golgi, decreased the time interval between synthesis of procollagens V and sulfation. The sulfated procollagens V were soon secreted and cut to sulfated p‐collagens V. Sulfated proα1(V) chains were cleaved faster than sulfated proα1′(V) chains. The relationship of sequential protein modification to spatial cellular organization is discussed.