pH-independent and -dependent cleavage of proinsulin in the same secretory vesicle.
pH-independent and -dependent cleavage of proinsulin in the same secretory vesicle.
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DOI：
10.1083/jcb.126.5.1149
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发表时间：
1994-09
期刊：
影响因子：
--
通讯作者：
Anderson RG
中科院分区：
文献类型：
--
作者：
Orci L;Halban P;Perrelet A;Amherdt M;Ravazzola M;Anderson RG
通过定量免疫电镜和高效液相色谱，我们研究了氯化铵破坏pH梯度对朗格汉斯胰岛胰岛素生成b细胞胰岛素原转化的影响。在连续的序列切片上交替用抗胰岛素原或抗二硝基酚（以显示pH敏感探针DAMP）抗体免疫染色，测定单个分泌囊泡的胰岛素原含量和pH。用高效液相色谱法对相同条件下胰岛提取物的放射性标记胰岛素原、胰岛素原裂解中间体和胰岛素进行定量分析。C-肽/ a链连接处的分裂对pH梯度破坏的敏感性明显低于b -链/C肽连接处，但单个囊泡中pH和胰岛素原含量的范围表明，这两种分裂发生在从TGN释放的同一个囊泡中。
By quantitative immunoelectron microscopy and HPLC, we have studied the effect of disrupting pH gradients, by ammonium chloride, on proinsulin conversion in the insulin-producing B-cells of the islets of langerhans. Proinsulin content and pH in single secretory vesicles were measured on consecutive serial sections immunostained alternately with anti-proinsulin or anti-dinitrophenol (to reveal the pH-sensitive probe DAMP) antibodies. Radioactivity labeled proinsulin, proinsulin cleavage intermediates, and insulin were quantitated by HPLC analysis of extracts of islets treated in the same conditions. Cleavage at the C- peptide/A-chain junction is significantly less sensitive to pH gradient disruption than that of the B-chain/C-peptide junction, but the range of pH and proinsulin content in individual vesicles indicate that both cleavages occur in the same vesicle released from the TGN.
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