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

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.

journal_name

Cell

journal_title

Cell

authors

Fisher JM,Sossin W,Newcomb R,Scheller RH

doi

10.1016/s0092-8674(88)91131-2

subject

Has Abstract

pub_date

1988-09-09 00:00:00

pages

813-22

issue

6

eissn

0092-8674

issn

1097-4172

pii

S0092-8674(88)91131-2

journal_volume

54

pub_type

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