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

Cell. 1988 Sep 9;54(6):813-22. doi: 10.1016/s0092-8674(88)91131-2.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Aplysia / physiology*
  • Biological Transport
  • Cell Compartmentation
  • Cytoplasmic Granules / metabolism
  • Immunohistochemistry
  • Invertebrate Hormones / metabolism*
  • Microscopy, Electron
  • Neurons / metabolism
  • Protein Precursors / metabolism*
  • Protein Processing, Post-Translational*

Substances

  • Invertebrate Hormones
  • Protein Precursors
  • egg-laying hormone, Mollusca