Pituitary Adenylate Cyclase Activating Peptide (PACAP) Participates in Adipogenesis by Activating ERK Signaling Pathway
Author(s) -
Tatjana Arsenijevic,
Françoise Grégoire,
Jeanne Chiadak,
Elodie Courtequisse,
Nargis Bolaky,
Jason Perret,
Christine Delporte
Publication year - 2013
Publication title -
plos one
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.99
H-Index - 332
ISSN - 1932-6203
DOI - 10.1371/journal.pone.0072607
Subject(s) - vasoactive intestinal peptide , adenylate kinase , receptor , cyclase , pituitary adenylate cyclase activating peptide , secretin , mapk/erk pathway , adipogenesis , endocrinology , chemistry , phosphorylation , medicine , biology , microbiology and biotechnology , neuropeptide , biochemistry , adipose tissue , secretion
Pituitary adenylate cyclase activating peptide (PACAP) belongs to the secretin/glucagon/vasoactive intestinal peptide (VIP) family. Its action can be mediated by three different receptor subtypes: PAC1, which has exclusive affinity for PACAP, and VPAC1 and VPAC2 which have equal affinity for PACAP and VIP. We showed that all three receptors are expressed in 3T3-L1 cells throughout their differentiation into adipocytes. We established the activity of these receptors by cAMP accumulation upon induction by PACAP. Together with insulin and dexamethasone, PACAP induced adipogenesis in 3T3-L1 cell line. PACAP increased cAMP production within 15 min upon stimulation and targeted the expression and phosphorylation of MAPK (ERK1/2), strengthened by the ERK1/2 phosphorylation being partially or completely abolished by different combinations of PACAP receptors antagonists. We therefore speculate that ERK1/2 activation is crucial for the activation of CCAAT/enhancer- binding protein β (C/EBPβ).
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