Fisher J M, Sossin W, Newcomb R, Scheller R H
Department of Biological Sciences, Stanford University, California 94305.
Cell. 1988 Sep 9;54(6):813-22. doi: 10.1016/s0092-8674(88)91131-2.
The ELH prohormone is proteolytically processed into at least nine peptides which govern egg-laying behavior in Aplysia. Quantitative immunocytochemistry demonstrates that peptides derived from the prohormone are packaged into distinct vesicle classes. Further experiments suggest the segregation occurs via a rapid initial proteolytic cleavage of the prohormone followed by sorting at the trans Golgi. Egg-laying hormone (ELH) immunoreactivity is localized to the cell body and processes, while bag cell peptide (BCP) immunoreactivity is greater in the cell body. Steady state levels of the amino-terminal set of peptides including the BCPs are 3- to 8-fold lower than the carboxy-terminal cleavage products, such as ELH. Thus, intracellular packaging and routing of the peptides cleaved from a single prohormone regulate their localization and levels in these neurons.
ELH前激素经蛋白水解加工成至少九种肽，这些肽控制着海兔的产卵行为。定量免疫细胞化学表明，源自前激素的肽被包装到不同的囊泡类别中。进一步的实验表明，这种分离是通过前激素的快速初始蛋白水解切割，然后在反式高尔基体中进行分选实现的。产卵激素（ELH）免疫反应定位于细胞体和突起，而袋状细胞肽（BCP）免疫反应在细胞体中更强。包括BCP在内的氨基末端肽组的稳态水平比羧基末端切割产物（如ELH）低3至8倍。因此，从单一前激素切割而来的肽的细胞内包装和运输调节了它们在这些神经元中的定位和水平。
