Multiple neuropeptides derived from a common precursor are differentially packaged and transported.

J M Fisher; W Sossin; R Newcomb; R H Scheller

doi:10.1016/s0092-8674(88)91131-2

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Multiple neuropeptides derived from a common precursor are differentially packaged and transported.

J M Fisher·W Sossin·R Newcomb·R H Scheller

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Abstract

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.

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Animals Aplysia Biological Transport Cell Compartmentation Cytoplasmic Granules Immunohistochemistry Invertebrate Hormones Microscopy, Electron Neurons Protein Precursors Protein Processing, Post-Translational Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

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J M Fisher, W Sossin, R Newcomb, R H Scheller. 1988-09-09. Multiple neuropeptides derived from a common precursor are differentially packaged and transported.. https://doi.org/10.1016/s0092-8674(88)91131-2

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