scholarly journals Augmented cystine-glutamate exchange by pituitary adenylate cyclase-activating polypeptide signaling via the VPAC1 receptor

Synapse ◽  
2014 ◽  
Vol 68 (12) ◽  
pp. 604-612 ◽  
Author(s):  
Jon M. Resch ◽  
Rebecca Albano ◽  
Xiaoqian Liu ◽  
Julie Hjelmhaug ◽  
Doug Lobner ◽  
...  
Keyword(s):  
Adenylate Cyclase ◽  
Vpac1 Receptor ◽  
Pituitary Adenylate Cyclase

scholarly journals Evidence for a direct interaction between the Thr11 residue of vasoactive intestinal polypeptide and Tyr184 located in the first extracellular loop of the VPAC2 receptor

2003 ◽  
Vol 370 (3) ◽  
pp. 1003-1009 ◽  
Author(s):  
Ingrid NACHTERGAEL ◽  
Pascale VERTONGEN ◽  
Ingrid LANGER ◽  
Jason PERRET ◽  
Patrick ROBBERECHT ◽  
...  
Keyword(s):  
Hydrogen Bond ◽  
Adenylate Cyclase ◽  
Hydroxy Group ◽  
Direct Interaction ◽  
Side Chain ◽  
Extracellular Loop ◽  
Vpac1 Receptor ◽  
Pituitary Adenylate Cyclase ◽  
Selective Ligands ◽  
Natural Peptide

We developed previously VPAC1 [vasoactive intestinal peptide (VIP)/pituitary adenylate cyclase-activating peptide (PACAP) receptor]>VPAC2 receptor selective ligands. Replacement of the VIP-Thr11 by an Arg11 in these ligands contributed to their selectivity: Arg11-VIP had a 200-fold lower affinity when compared with VIP at VPAC2 receptors as opposed to 3- to 5-fold higher affinity at VPAC1 receptors. Comparison of the binding and functional properties of related VIP analogues suggested that the VPAC1 selectivity of Arg11-VIP was due to the loss of a hydrogen bond between the hydroxy group of Thr residue and the VPAC2 receptor, steric hindrance between the Arg side chain and the VPAC2 receptor and charge attraction by the VPAC1 receptor. Comparison of the ability of VIP analogues to activate adenylate cyclase through chimaeric VPAC1/VPAC2 and VPAC2/VPAC1 receptors indicated that the first extracellular receptor loop carried most of the VPAC2 receptors’ ability to discriminate VIP from Arg11-VIP. Based on results obtained for a truncated VPAC2 receptor and the closely related PACAP-preferring receptor (PAC1) and secretin receptors, we hypothesized that Thr11 interacted with the VPAC2 receptor Tyr184 (similar to the VPAC1 receptor Phe200 residue). The Y184F (Tyr184→Phe) VPAC2 mutant lost the ability to discriminate VIP from Val11-VIP, and the F200Y VPAC1 mutant acquired the ability to discriminate the natural peptide from Val11-VIP. These results support the hypothesis that the hydroxy group of the native VIP-Thr11 side chain can indeed form a hydrogen bond with the Tyr side chain in the VPAC2 receptor.

scholarly journals The human vasoactive intestinal peptide/pituitary adenylate cyclase-activating peptide receptor 1 (VPAC1) promoter: characterization and role in receptor expression during enterocytic differentiation of the colon cancer cell line Caco-2Cl.20

2000 ◽  
Vol 347 (3) ◽  
pp. 623-632 ◽  
Author(s):  
Alain COUVINEAU ◽  
Jean-José MAORET ◽  
Christiane ROUYER-FESSARD ◽  
Isabel CARRERO ◽  
Marc LABURTHE
Keyword(s):  
Colon Cancer ◽  
Adenylate Cyclase ◽  
Vasoactive Intestinal Peptide ◽  
Human Colon ◽  
Flanking Sequence ◽  
Human Colon Cancer ◽  
Peptide Receptor ◽  
Vpac1 Receptor ◽  
Pituitary Adenylate Cyclase ◽  
Enterocytic Differentiation

The basic organization of the human vasoactive intestinal peptide/pituitary adenylate cyclase-activating peptide receptor (VPAC) 1 promoter was investigated after cloning the 5ʹ-flanking region (1.4 kb) of the VPAC1 gene from a human genomic library. Subsequent functional analysis of various deletions of the 5ʹ-flanking sequence, subcloned upstream of a luciferase reporter gene, was carried out in HT-29 cells. The minimal promoter region identified encompasses the -205/+76 sequence and contains a crucial CCAAT box (-182/-178) and a GC-rich sequence. Moreover a region (-1348/-933) containing a silencer element was identified. We previously showed that the expression of the VPAC1 receptor binding site is strictly dependent upon the enterocytic differentiation of human colon cancer Caco-2 cells [Laburthe, Rousset, Rouyer-Fessard, Couvineau, Chantret, Chevalier and Zweibaum (1987) J. Biol. Chem. 262, 10180-10184]. In the present study we show that VPAC1 mRNA increases dramatically when Caco-2Cl.20 cells differentiate, as measured by RNase protection assays and reverse transcriptase-PCR. A single transcript species of 3 kb is detected in differentiated cells by Northern-blot analysis. Accumulation of VPAC1 receptor mRNA is due to a 5-fold increase of transcription rate (run-on assay) without a change in mRNA half-life (9 h). Stable transfections of various constructs in Caco-2Cl.20 cells and subsequent analysis of reporter gene expression, during the enterocytic differentiation process over 25 days of culture, further indicated that the -254/+76 5ʹ-flanking sequence is endowed with the regulatory element(s) necessary for transcriptional regulation of VPAC1 during differentiation. Altogether, these observations provide the first characterization of the basic organization of the human VPAC1 gene promoter and unravel the crucial role of a short promoter sequence in the strict transcriptional control of VPAC1 expression during differentiation of human colon cancer Caco-2 cells.

Pituitary Adenylate Cyclase Activating Polypeptide: A Potential Neuroprotective Peptide

2004 ◽  
Vol 10 (23) ◽  
pp. 2861-2889 ◽  
Author(s):  
Aniko Somogyvari-Vigh ◽  
Dora Reglodi
Keyword(s):  
Adenylate Cyclase ◽  
Pituitary Adenylate Cyclase

EFFECT OF PITUITARY ADENYLATE CYCLASE-ACTIVATING POLYPEPTIDE (PACAP) ON PRODUCTION OF PROGESTERONE IN CULTURED LUTEAL CELLS FROM RAT OVARY

1997 ◽  
Vol 18 (5) ◽  
pp. 335-341 ◽  
Author(s):  
ERI KOTANI ◽  
SATOSHI USUKI ◽  
TAKESHI KUBO
Keyword(s):  
Adenylate Cyclase ◽  
Luteal Cells ◽  
Pituitary Adenylate Cyclase

scholarly journals Pituitary Adenylate Cyclase-Activating Polypeptide Receptors Mediating Insulin Secretion in Rodent Pancreatic Islets Are Coupled to Adenylate Cyclase But Not to PLC

Endocrinology ◽  
2002 ◽  
Vol 143 (4) ◽  
pp. 1253-1259 ◽  
Author(s):  
Francoise Jamen ◽  
Raymond Puech ◽  
Joel Bockaert ◽  
Philippe Brabet ◽  
Gyslaine Bertrand
Keyword(s):  
Insulin Secretion ◽  
Adenylate Cyclase ◽  
Pancreatic Islets ◽  
Pituitary Adenylate Cyclase

scholarly journals Purification and characterization of the receptor for pituitary adenylate cyclase-activating polypeptide.

1993 ◽  
Vol 268 (35) ◽  
pp. 26650-26657
Author(s):  
T Ohtaki ◽  
Y Masuda ◽  
Y Ishibashi ◽  
C Kitada ◽  
A Arimura ◽  
...  
Keyword(s):  
Adenylate Cyclase ◽  
Purification And Characterization ◽  
Pituitary Adenylate Cyclase

scholarly journals Pituitary adenylate cyclase activating polypeptide is an extraordinarily potent intra-pancreatic regulator of insulin secretion from islet beta-cells.

1994 ◽  
Vol 269 (2) ◽  
pp. 1290-1293
Author(s):  
T. Yada ◽  
M. Sakurada ◽  
K. Ihida ◽  
M. Nakata ◽  
F. Murata ◽  
...  
Keyword(s):  
Insulin Secretion ◽  
Adenylate Cyclase ◽  
Beta Cells ◽  
Islet Beta Cells ◽  
Pituitary Adenylate Cyclase
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