• Publications
  • Influence
Structural requirements for the occupancy of pituitary adenylate-cyclase-activating-peptide (PACAP) receptors and adenylate cyclase activation in human neuroblastoma NB-OK-1 cell membranes. Discovery
In these structure activity studies, the 46 analogs of the 27-amino-acid form of the pituitary-adenylate-cyclase-activating peptide, PACAP(1-27), and the 38-amino-acid form, PACAP(1-38), were eitherExpand
  • 212
  • 14
Fragments of pituitary adenylate cyclase activating polypeptide discriminate between type I and II recombinant receptors.
Pituitary adenylate cyclase activating polypeptide (PACAP) analogues were tested for their ability to occupy the recombinant selective PACAP receptors (PACAP type I receptor) or the non-selectiveExpand
  • 78
  • 13
Molecular cloning and functional characterization of a human VIP receptor from SUP-T1 lymphoblasts.
We have cloned and sequenced a cDNA isolated from a human SUP-T1 lymphoblast cell line library. It encoded a 457 amino acids protein having 87% identity with the rat PACAP type II, VIP2 receptor.Expand
  • 160
  • 10
Presence of highly selective receptors for PACAP (pituitary adenylate cyclase activating peptide) in membranes from the rat pancreatic acinar cell line AR 4‐2J
We characterized highly selective receptors for PACAP, the pituitary adenylate cyclase activating peptide, in the tumoral acinar cell line AR 4‐2J derived from the rat pancreas. PACAP, a novelExpand
  • 118
  • 6
The two forms of the pituitary adenylate cyclase activating polypeptide (PACAP (1–27) and PACAP (1–38)) interact with distinct receptors on rat pancreatic AR 4‐2J cell membranes
The existence of specific receptors for the two PACAPs (Pituirary Adenylate Cyclase Activating Peptides of 27 and 38 amino acids) was previously demonstrated on membranes from the pancreatic acinarExpand
  • 69
  • 4
Ghrelin is produced by the human erythroleukemic HEL cell line and involved in an autocrine pathway leading to cell proliferation.
Ghrelin, a ligand of the GH secretagogue receptor (GHS-R 1a), is a 28-amino acid peptide with an unusual octanoyl group on Ser3, crucial for its biological activity. For the first time, ghrelin andExpand
  • 56
  • 4
Interaction of growth hormone-releasing factor (GRF) and 14 GRF analogs with vasoactive intestinal peptide (VIP) receptors of rat pancreas. Discovery of (N-Ac-Tyr1,D-Phe2)-GRF(1-29)-NH2 as a VIP
Adenylate cyclase stimulation by GH-releasing factor (GRF) and 14 GRF analogs (modified in the N-terminal part) was compared to the capacity of the same peptides to inhibit [125I]iodo-vasoactiveExpand
  • 153
  • 3
Antagonistic properties are shifted back to agonistic properties by further N-terminal shortening of pituitary adenylate-cyclase-activating peptides in human neuroblastoma NB-OK-1 cell membranes.
N-terminally shortened analogs of the 27-amino-acid and 38-amino-acid forms of the pituitary-adenylate-cyclase-activating neuropeptide, PACAP(1-27) and PACAP(1-38), were synthesized by a solid-phaseExpand
  • 55
  • 3
Addition of the (28-38) peptide sequence of PACAP to the VIP sequence modifies peptide selectivity and efficacy.
Chimeric peptides were synthesized by adding the C-terminal extension 28-38 of the pituitary adenylate cyclase activating polypeptide (PACAP) to the sequences (1-27), (2-27), (3-27) and (6-27) ofExpand
  • 26
  • 3
A new type of functional VIP receptor has an affinity for helodermin in human SUP‐T1 lymphoblasts
A new type of VIP receptor was characterized in human SUP‐T1 lymphoblasts. The order of potency of unlabeled peptides in the presence of [125I]helodermin, was: helodermin(1–35)‐NH2 =Expand
  • 62
  • 2
...
1
2
3
4
5
...