Proteolytic processing of the Aplysia egg-laying hormone prohormone
Proteolytic processing of the Aplysia egg-laying hormone prohormone
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DOI：
10.1073/pnas.95.7.3972
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发表时间：
1998-03-31
影响因子：
11.1
通讯作者：
Sweedler, JV
中科院分区：
文献类型：
--
作者：
Garden, RW;Shippy, SA;Sweedler, JV
通过使用基质辅助激光解吸/电离飞行时间质谱，单个肽能神经元的测定，从Aaplasia，一个半定量的方法，通过使用光谱归一化比较单细胞配置文件，和肽定位到特定的细胞质谱细胞映射。除了所有先前鉴定的产蛋激素（ELH）基因的产物之外，其它肽由ELH和酸性肽（AP）内的Leu-Leu残基的蛋白水解形成，AP表现出进一步加工以产生AP（1-20）和AP（9-27）。这些肽似乎与ELH共定位在囊泡中，运输到特定的神经元靶点，并以Ca 2+依赖的方式释放。在特定靶细胞处观察到差异肽分布，并且在单个动物中检测到AP的低频变异，[Thr（21）]AP。
By using matrix-assisted laser desorption/ionization time-of-flight MS, individual peptidergic neurons from Aplysia are assayed, A semiquantitative method is developed for comparing single-cell profiles by using spectral normalization, and peptides are localized to specific cells by mass spectrometric cell mapping. In addition to all previously identified products of the egg-laying hormone (ELH) gene, other peptides are formed from proteolytic hydrolysis of Leu-Leu residues within ELH and acidic peptide (AP), AP exhibits further processing to yield AP(1-20) and AP(9-27). These peptides appear to be colocalized in vesicles with ELH, transported to specific neuronal targets, and released in a Ca2+ dependent manner. A differential peptide distribution is observed at a specific target cell, and a low-frequency variation of AP, [Thr(21)]AP, is detected in a single animal.