scholarly journals The Pituitary Adenylate Cyclase Activating Polypeptide Type 1 Receptor (PAC1-R) Is Expressed on Gastric ECL Cells: Evidence by Immunocytochemistry and RT-PCR

1998 ◽  
Vol 865 (1 VIP, PACAP, A) ◽  
pp. 147-156 ◽  
Author(s):  
NINGXIN ZENG ◽  
TAO KANG ◽  
RONG-MING LYU ◽  
HELEN WONG ◽  
YI WEN ◽  
...  
Keyword(s):  
Adenylate Cyclase ◽  
Rt Pcr ◽  
Ecl Cells ◽  
Pituitary Adenylate Cyclase

scholarly journals Multiple splice variants of the pituitary adenylate cyclase-activating polypeptide type 1 receptor detected by RT-PCR in single rat pituitary cells

1998 ◽  
Vol 21 (2) ◽  
pp. 109-120 ◽  
Author(s):  
L Bresson-Bepoldin ◽  
MC Jacquot ◽  
W Schlegel ◽  
SR Rawlings
Keyword(s):  
Alternative Splicing ◽  
Adenylate Cyclase ◽  
Single Cell ◽  
Splice Variant ◽  
Cell Biology ◽  
Splice Variants ◽  
Pituitary Cells ◽  
Rt Pcr ◽  
Pituitary Adenylate Cyclase

Alternative splicing of the rat type 1 pituitary adenylate cyclase-activating polypeptide (PACAP) receptor (PVR1) produces variants that couple either to both adenylyl cyclase (AC) and phospholipase C (PLC) (PVR1 short, PVR1 hop, PVR1 hiphop), or to AC alone (PVR1 hip). We have previously shown that populations of clonal alphaT3-1 gonadotrophs express PVR1 hop and PVR1 short mRNAs, whereas clonal GH4C1 somatotrophs do not. Here we have used the single cell RT-PCR technique to investigate whether normal rat gonadotrophs and somatotrophs express PVR1 mRNA, whether a single cell co-expresses multiple splice variant forms, and whether differential PVR1 mRNA expression correlates with differences in PACAP-stimulated Ca2+ signalling. We found that individual rat gonadotrophs expressed mRNA either for PVR1 hop, for PVR1 short, or co-expressed the two forms. Although we found no differences between the splice variant(s) expressed and the characteristics of PACAP-stimulated Ca2+ responses, the expression of PVR1 mRNA is consistent with the known PACAP stimulation of the PLC system in gonadotrophs. Individual rat somatotrophs also expressed PVR1 hop or PVR1 short (but not PVR1 hip) mRNAs although these forms were never co-expressed. The expression of PVR1 mRNA in somatotrophs can explain in part the activation by PACAP of the AC system in such cells. In conclusion, the single cell RT-PCR technique was used to demonstrate expression of multiple PVR1 splice variants in single identified pituitary cells. These findings open up important questions on the role of alternative splicing in cell biology.

Expression, pharmacological, and functional evidence for PACAP/VIP receptors in human lung

1999 ◽  
Vol 277 (1) ◽  
pp. L42-L48 ◽  
Author(s):  
Rebeca Busto ◽  
Isabel Carrero ◽  
Luis G. Guijarro ◽  
Rosa M. Solano ◽  
José Zapatero ◽  
...  
Keyword(s):  
Adenylate Cyclase ◽  
Human Lung ◽  
Dissociation Constants ◽  
Binding Capacity ◽  
Rt Pcr ◽  
Vip Receptors ◽  
Pituitary Adenylate Cyclase ◽  
Maximum Binding Capacity ◽  
Specific Receptors

Pituitary adenylate cyclase-activating peptide (PACAP) type 1 (PAC1) and common PACAP/vasoactive intestinal peptide (VIP) type 1 and 2 (VPAC1 and VPAC2, respectively) receptors were detected in the human lung by RT-PCR. The proteins were identified by immunoblotting at 72, 67, and 68 kDa, respectively. One class of PACAP receptors was defined from125I-labeled PACAP-27 binding experiments (dissociation constant = 5.2 nM; maximum binding capacity = 5.2 pmol/mg protein) with a specificity: PACAP-27 ≈ VIP > helodermin ≈ peptide histidine-methionine (PHM) ≫ secretin. Two classes of VIP receptors were established with 125I-VIP (dissociation constants of 5.4 and 197 nM) with a specificity: VIP ≈ helodermin ≈ PACAP-27 ≫ PHM ≫ secretin. PACAP-27 and VIP were equipotent on adenylyl cyclase stimulation (EC50 = 1.6 nM), whereas other peptides showed lower potency (helodermin > PHM ≫ secretin). PACAP/VIP antagonists supported that PACAP-27 acts in the human lung through either specific receptors or common PACAP/VIP receptors. The present results are the first demonstration of the presence of PAC1 receptors and extend our knowledge of common PACAP/VIP receptors in the human lung.

Design and biological assessment of membrane-tethering neuroprotective peptides derived from the pituitary adenylate cyclase-activating polypeptide type 1 receptor

2019 ◽  
Vol 1863 (11) ◽  
pp. 129398 ◽  
Author(s):  
Mathilde Poujol de Molliens ◽  
Priyanka Jamadagni ◽  
Myriam Létourneau ◽  
Dominic Devost ◽  
Terence E. Hébert ◽  
...  
Keyword(s):  
Adenylate Cyclase ◽  
Biological Assessment ◽  
Pituitary Adenylate Cyclase ◽  
Membrane Tethering

Mild deficits in mice lacking pituitary adenylate cyclase-activating polypeptide receptor type 1 (PAC1) performing on memory tasks

2000 ◽  
Vol 84 (1-2) ◽  
pp. 79-89 ◽  
Author(s):  
Magdalena Sauvage ◽  
Philippe Brabet ◽  
Florian Holsboer ◽  
Joel Bockaert ◽  
Thomas Steckler
Keyword(s):  
Adenylate Cyclase ◽  
Receptor Type ◽  
Pituitary Adenylate Cyclase

scholarly journals Pituitary Adenylate Cyclase-Activating Polypeptide (PACAP) and PACAP-Receptor Type 1 Expression in Rat and Human Placenta1

Endocrinology ◽  
2000 ◽  
Vol 141 (3) ◽  
pp. 1158-1167 ◽  
Author(s):  
Maria Lucia Scaldaferri ◽  
Andrea Modesti ◽  
Camilla Palumbo ◽  
Salvatore Ulisse ◽  
Andrea Fabbri ◽  
...  
Keyword(s):  
Adenylate Cyclase ◽  
Receptor Type ◽  
Pituitary Adenylate Cyclase

Identification of Binding Domains of Pituitary Adenylate Cyclase Activating Polypeptide (PACAP) for its Type 1 Receptor by Photoaffinity Labelinga

1998 ◽  
Vol 865 (1 VIP, PACAP, A) ◽  
pp. 82-91 ◽  
Author(s):  
YONG-JIANG CAO ◽  
ELZBIETA KOJRO ◽  
MAREK JASIONOWSKI ◽  
LESZEK LANKIEWICZ ◽  
ZBIGNIEW GRZONKA ◽  
...  
Keyword(s):  
Adenylate Cyclase ◽  
Binding Domains ◽  
Pituitary Adenylate Cyclase

Pituitary adenylate cyclase-activating polypeptide activates KATP current in rat atrial myocytes

2001 ◽  
Vol 280 (3) ◽  
pp. H1058-H1065 ◽  
Author(s):  
Anne Baron ◽  
Dominique Monnier ◽  
Angela Roatti ◽  
Alex J. Baertschi
Keyword(s):  
Protein Kinase ◽  
Adenylate Cyclase ◽  
Neonatal Rat ◽  
Atrial Myocytes ◽  
Camp Production ◽  
Rt Pcr ◽  
Kinase C ◽  
Pituitary Adenylate Cyclase ◽  
Inhibitor Peptide ◽  
Electrophysiological Effects

Because the electrophysiological effects of pituitary adenylate cyclase-activating polypeptide (PACAP) on the heart are little known, we studied the regulation of the atrial ATP-sensitive K+(KATP) current by PACAP on primary cultured neonatal rat atrial myocytes. PACAP-38 stimulates cAMP production with EC50 = 0.28 nmol/l ( r = 0.92, P < 0.02). PACAP-38 and PACAP-27 (10 nmol/l) have similar maximal effects, whereas 100 nmol/l vasoactive intestinal polypeptide (VIP) is 2.7 times less effective ( P < 0.05). RT-PCR shows the presence of cloned PACAP receptors PAC1 (≥2 isoforms), VPAC1, and VPAC2. PACAP-38 dose dependently activates the whole cell atrial KATP current with EC50 = 1–3 nmol/l ( n = 44). Maximal effects occur at 10 nmol/l (91 ± 15 pA/pF, n = 18). Diazoxide further increases the PACAP-activated current by 78% ( P < 0.05; n = 6). H89 (500 nmol/l), a protein kinase A (PKA) inhibitor, reduces the PACAP-activated KATPcurrent to 17.8 ± 9.6% ( n = 5) of the maximal diazoxide-induced current and totally inhibits the cAMP-induced KATP current. A protein kinase C (PKC) inhibitor peptide (50 μmol/l) in the pipette reduces the PACAP-38-induced KATP current to 33 ± 17 pA/pF ( P < 0.05, n = 6) without significantly affecting the currents induced by cAMP or VIP. The results suggest that: 1) PAC1, VPAC1, and VPAC2 are present in atrial myocytes; and 2) PACAP-38 activates the atrial KATP channels through both PKA and PKC pathways.

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