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J Biol Chem, Vol. 273, Issue 31, 19685-19690, July 31, 1998
From the The growth rate of rodent embryonic
neuroblasts and human neuroblastoma cell lines is regulated in part by
autocrine or paracrine actions of neuropeptides of the family that
includes vasoactive intestinal peptide (VIP), peptide histidine
isoleucine (PHI), and pituitary adenylate cyclase-activating peptide
(PACAP). These peptides act via seven transmembrane G-protein-linked
receptors coupled to cAMP elevation, phospholipase C activation,
intracellular Ca2+ release, and/or of
mitogen-activated protein (MAP) kinase activation. Here we investigated
the action of these peptides on the mouse neuroblastoma cell line
Neuro2a. PHI and VIP inhibited proliferation at concentrations as low
as 10
Differential Effects of Peptide Histidine Isoleucine (PHI) and
Related Peptides on Stimulation and Suppression of Neuroblastoma
Cell Proliferation
A NOVEL VIP-INDEPENDENT ACTION OF PHI VIA MAP KINASE
,,,,
Department of Psychiatry, Mental Retardation
Research Center, UCLA, Neuropsychiatric Institute, Los Angeles, CA
90024 and the § CNRS UMR 6558, Laboratoire de Biologie des
Interactions Cellulaires, UFR Sciences, Universite de Poitiers, 40 avenue du Recteur PINEAU, 86022 Poitiers Cedex, France
13 M and 1010
M, respectively. In contrast, PACAP action was biphasic,
with stimulation occurring at subnanomolar doses and inhibition at higher doses. Peptide actions were studied further by measuring cAMP
and ERK1/2 MAP kinase activity and by assessing
3H-thymidine incorporation in conjunction with a panel of
signal transduction pathways inhibitors. The data obtained indicated that the PHI-inhibitory and PACAP-stimulatory activities were mediated
by corresponding changes in activity of the MAP kinase pathway and
independent of protein kinase A (PKA) or protein kinase C (PKC). In
contrast, the inhibitory actions of VIP and PACAP were specifically
blocked by antagonists of PKA. Northern blot analysis revealed gene
expression for only the PACAP-preferring (PAC1) receptor.
However, binding experiments using 125I-labeled PACAP27,
PHI, and VIP, demonstrated the presence of PACAP-preferring sites,
bivalent VIP/PACAP sites, and PHI-binding sites that did not interact
with VIP. The studies demonstrate potent regulatory actions of
PACAP, PHI, and VIP on neuroblastoma cell proliferation which appear to
be mediated by multiple subsets of receptors which differentially
couple to MAP kinase and PKA signaling pathways.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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