help button home button Endocrine Society Endocrinology
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow Request Copyright Permission
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Braas, K. M.
Right arrow Articles by May, V.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Braas, K. M.
Right arrow Articles by May, V.

Endocrinology, Vol 134, 186-195, Copyright © 1994 by Endocrine Society


ARTICLES

Pituitary adenylate cyclase-activating polypeptide regulation of AtT- 20/D16v corticotrope cell proopiomelanocortin expression and secretion

KM Braas, CA Brandenburg and V May
Department of Anatomy and Neurobiology, University of Vermont College of Medicine, Burlington 05405.

The hypothalamic peptides pituitary adenylate cyclase-activating polypeptides (PACAPs) may play central roles in the regulation of anterior pituitary gland function. The two pro-PACAP-derived peptides, PACAP38 and PACAP27, are posttranslationally processed from a common precursor molecule and share amino acid sequence homology with vasoactive intestinal peptide (VIP). To further evaluate and compare the physiological roles of these peptides, we have examined the short and long term effects of PACAP38, PACAP27, and VIP on POMC-related peptide production in the mouse AtT-20/D16v corticotrope cell line. Short term (0.5- to 5-h) treatment of AtT-20/D16v cells with PACAP38, PACAP27, or VIP elicited similar concentration-dependent and biphasic stimulation of ACTH release. Half-maximal stimulation of the higher potency phase was attained with 1-2 nM peptide; maximal secretion was observed at peptide concentrations greater than 100 nM. Similar 2- to 3- fold maximal stimulation of ACTH secretion was elicited by all three bioactive peptides; linear sustained ACTH secretion was observed. Long term (12- to 72-h) treatment of AtT-20/D16v cultures with these peptides resulted in substantially decreased rates of cellular division, with a concomitant increase in cell size and formation of cell processes characteristic of cellular differentiation. These morphological changes coincided with a sustained 2-fold increase in AtT- 20 corticotrope intracellular hormone content and secretion. Northern blot analysis demonstrated a parallel induction of POMC mRNA expression by the PACAP38, PACAP27, and VIP peptides. These results suggest that AtT-20/D16v cells possess primarily the type II PACAP receptor subtype, which binds PACAP38, PACAP27, and VIP with apparent equal affinity. Furthermore, the long term effects of these peptides implicate a potentially significant role for PACAP and VIP peptides in the mediation of altered pituitary gland functions. In this vein, the PACAPs may prove to be unique regulators of neuroendocrine function and development.


This article has been cited by other articles:


Home page
Pharmacol. Rev.Home page
D. Vaudry, A. Falluel-Morel, S. Bourgault, M. Basille, D. Burel, O. Wurtz, A. Fournier, B. K. C. Chow, H. Hashimoto, L. Galas, et al.
Pituitary Adenylate Cyclase-Activating Polypeptide and Its Receptors: 20 Years after the Discovery
Pharmacol. Rev., September 1, 2009; 61(3): 283 - 357.
[Abstract] [Full Text] [PDF]


Home page
Pharmacol. Rev.Home page
D. Vaudry, B. J. Gonzalez, M. Basille, L. Yon, A. Fournier, and H. Vaudry
Pituitary Adenylate Cyclase-Activating Polypeptide and Its Receptors: From Structure to Functions
Pharmacol. Rev., June 1, 2000; 52(2): 269 - 324.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
K. M. Braas and V. May
Pituitary Adenylate Cyclase-activating Polypeptides Directly Stimulate Sympathetic Neuron Neuropeptide Y Release through PAC1 Receptor Isoform Activation of Specific Intracellular Signaling Pathways
J. Biol. Chem., September 24, 1999; 274(39): 27702 - 27710.
[Abstract] [Full Text] [PDF]


Home page
J. Neurosci.Home page
K. M. Braas, V. May, S. A. Harakall, J. C. Hardwick, and R. L. Parsons
Pituitary Adenylate Cyclase-Activating Polypeptide Expression and Modulation of Neuronal Excitability in Guinea Pig Cardiac Ganglia
J. Neurosci., December 1, 1998; 18(23): 9766 - 9779.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
A. P. Barrie, A. M. Clohessy, C. S. Buensuceso, M. V. Rogers, and J. M. Allen
Pituitary Adenylyl Cyclase-activating Peptide Stimulates Extracellular Signal-regulated Kinase 1 or 2 (ERK1/2) Activity in a Ras-independent, Mitogen-activated Protein Kinase/ERK Kinase 1 or 2-dependent Manner in PC12 Cells
J. Biol. Chem., August 8, 1997; 272(32): 19666 - 19671.
[Abstract] [Full Text] [PDF]


Home page
J. Neurosci.Home page
C. A. Brandenburg, V. May, and K. M. Braas
Identification of Endogenous Sympathetic Neuron Pituitary Adenylate Cyclase-Activating Polypeptide (PACAP): Depolarization Regulates Production and Secretion through Induction of Multiple Propeptide Transcripts
J. Neurosci., June 1, 1997; 17(11): 4045 - 4055.
[Abstract] [Full Text] [PDF]


Home page
EndocrinologyHome page
Y. Aoki, Y. Iwasaki, M. Katahira, Y. Oiso, and H. Saito
Regulation of the Rat Proopiomelanocortin Gene Expression in AtT-20 cells. II: Effects of the Pituitary Adenylate Cyclase-Activating Polypeptide and Vasoactive Intestinal Polypeptide
Endocrinology, May 1, 1997; 138(5): 1930 - 1934.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Endocrinology Endocrine Reviews J. Clin. End. & Metab.
Molecular Endocrinology Recent Prog. Horm. Res. All Endocrine Journals
Copyright © 1994 by The Endocrine Society