Cell type-specific sorting of neuropeptides: a mechanism to modulate peptide composition of large dense-core vesicles.

  • Klumperman J
  • Spijker S
  • van Minnen J
 et al. 
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The CNS of Lymnaea stagnalis contains two populations of egg-laying hormone (ELH)-producing neurons that differ in size and topology. In type I neurons, all peptides located C-terminally from the cleavage site Arg-Ser-Arg-Arg180-183 are sorted into secretory large dense-core vesicles (LDCV), whereas N-terminal-located peptides accumulate in a distinct type of vesicle, the large electrondense granule (LEG). Via immunoelectron microscopy, we now show that the second population of ELH-producing neurons, type II neurons, lack LEG and incorporate all proELH-derived peptides into LDCV. This finding provides the first example of a cell type-specific sorting of neuropeptides into LDCV. Furthermore, we provide evidence that LEG are formed through a differential condensation process in the trans-Golgi network and that these bodies are ultimately degraded. Analysis of the endoprotease composition of the two types of proELH-producing neurons suggests that the formation of LEG, and consequently the retention of N-terminal peptides from the secretory pathway, requires the action of a furin-like protein.

Author-supplied keywords

  • and are incorporated into
  • egg laying
  • furin
  • immu-
  • large
  • ldcv
  • lum
  • lymnaea
  • neuropeptides
  • neuropeptides are synthesized at
  • noelectron microscopy
  • processing
  • sorting
  • the rough endoplasmic reticu-
  • traverse the golgi complex

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  • SGR: 0029808688
  • PUI: 26405056
  • SCOPUS: 2-s2.0-0029808688
  • ISBN: 0270-6474
  • ISSN: 0270-6474
  • PMID: 8987821


  • J Klumperman

  • S Spijker

  • J van Minnen

  • H Sharp-Baker

  • a B Smit

  • W P Geraerts

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