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Volume 16, Number 24, Issue of December 15, 1996 pp. 7930-7940
Copyright ©1996 Society for Neuroscience

Cell Type-Specific Sorting of Neuropeptides: A Mechanism to Modulate Peptide Composition of Large Dense-Core Vesicles

Received July 17, 1996; revised Sept. 24, 1996; accepted Oct. 1, 1996.

Judith Klumperman, Sabine Spijker, Jan van Minnen, Hilary Sharp-Baker, August B. Smit, and Wijnand P. M. Geraerts

Graduate School Neurosciences Amsterdam, Research Institute Neurosciences Vrije Universiteit, Faculty of Biology, 1081 HV Amsterdam, The Netherlands

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-Arg^180-183 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.

Key words: sorting; neuropeptides; LDCV; Lymnaea; immunoelectron microscopy; furin; egg laying; processing

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