A chimeric VIP-PACAP analogue but not VIP pseudopeptides function as VIP receptor antagonists

[1]  J. Bali,et al.  Synthesis of pseudo-peptide analogues of the C-terminal tetrapeptide of gastrin and evaluation of their biological activity on acid secretion. , 2009, International journal of peptide and protein research.

[2]  R. Hart,et al.  Immunmodulation durch gastrointestinale Neuropeptide , 2008, Deutsche medizinische Wochenschrift.

[3]  Ian Foracs Physiology of the Gastrointestinal Tract (3rd ed) , 1995 .

[4]  R. Jensen,et al.  Chimeric galanin analogs that function as antagonists in the CNS are full agonists in gastrointestinal smooth muscle. , 1993, The Journal of pharmacology and experimental therapeutics.

[5]  P. de Neef,et al.  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. , 1992, European journal of biochemistry.

[6]  W. Creutzfeldt,et al.  VIP-receptor antagonist (N-Ac-Tyr1,D-Phe2)-GRF(1–29)-NH2 is a potent agonist for enzyme secretion in isolated rat pancreatic acini , 1992, Regulatory Peptides.

[7]  R. Jensen,et al.  Interaction of Calcitonin Gene‐Related Peptides with Pancreatic Acinar Cells and Dispersed Gastric Smooth Muscle Cells , 1992, Annals of the New York Academy of Sciences.

[8]  V. Pieribone,et al.  M-15: high-affinity chimeric peptide that blocks the neuronal actions of galanin in the hippocampus, locus coeruleus, and spinal cord. , 1991, Proceedings of the National Academy of Sciences of the United States of America.

[9]  D. Coy,et al.  Human growth hormone-releasing hormone analogues with much improved in vitro growth hormone-releasing potencies in rat pituitary cells. , 1991, European journal of pharmacology.

[10]  Ottaway Ca Neuroimmunomodulation in the intestinal mucosa. , 1991 .

[11]  T. Moody,et al.  An antagonist to vasoactive intestinal peptide affects cellular functions in the central nervous system. , 1991, The Journal of pharmacology and experimental therapeutics.

[12]  I. Gozes,et al.  A VIP antagonist distinguishes VIP receptors on spinal cord cells and lymphocytes , 1991, Brain Research.

[13]  R. Jensen,et al.  Reduced peptide bond pseudopeptide analogues of secretin. A new class of secretin receptor antagonists. , 1991, The Journal of biological chemistry.

[14]  D. Coy,et al.  Analogues of growth hormone-releasing factor (1-29) amide containing the reduced peptide bond isostere in the N-terminal region. , 1990, Journal of medicinal chemistry.

[15]  F. Pomerleau,et al.  hCGRP8-37, a calcitonin gene-related peptide antagonist revealing calcitonin gene-related peptide receptor heterogeneity in brain and periphery. , 1990, The Journal of pharmacology and experimental therapeutics.

[16]  K. Gautvik,et al.  The mechanisms by which vasoactive intestinal peptide (VIP) and thyrotropin releasing hormone (TRH) stimulate prolactin release from pituitary cells , 1990, Bioscience reports.

[17]  R. Jensen,et al.  Reduced peptide bond pseudopeptide analogues of substance P. A new class of substance P receptor antagonists with enhanced specificity. , 1989, The Journal of biological chemistry.

[18]  R. Jensen,et al.  Short-chain pseudopeptide bombesin receptor antagonists with enhanced binding affinities for pancreatic acinar and Swiss 3T3 cells display strong antimitotic activity. , 1989, The Journal of biological chemistry.

[19]  I. Gozes,et al.  Vasoactive intestinal peptide potentiates sexual behavior: Inhibition by novel antagonist , 1989, Regulatory Peptides.

[20]  R. Jensen,et al.  Interaction of peptides related to VIP and secretin with guinea pig pancreatic acini. , 1989, The American journal of physiology.

[21]  M. Fukase,et al.  Calcitonin gene-related peptide receptor antagonist human CGRP-(8-37). , 1989, The American journal of physiology.

[22]  P. Robberecht,et al.  Vasoactive Intestinal Peptide Receptors in Pancreas and Liver. Structure‐Function Relationship a , 1988, Annals of the New York Academy of Sciences.

[23]  R. Jensen,et al.  Probing peptide backbone function in bombesin. A reduced peptide bond analogue with potent and specific receptor antagonist activity. , 1988, The Journal of biological chemistry.

[24]  A. Gronenborn,et al.  Determination of the backbone conformation of secretin by restrained molecular dynamics on the basis of interproton distance data. , 1988, European journal of biochemistry.

[25]  R. Jensen,et al.  Receptors for vasoactive intestinal peptide and secretin on guinea pig pancreatic acini , 1987, Peptides.

[26]  D. Coy,et al.  Solid phase synthesis of peptides containing the CH2NH peptide bond isostere , 1987, Peptides.

[27]  J. T. Turner,et al.  A fragment of vasoactive intestinal peptide, VIP(10–28), is an antagonist of VIP in the colon carcinoma cell line, HT29 , 1986, Peptides.

[28]  E. Kaiser,et al.  Design and biological activity of analogs of growth hormone releasing factor with potential amphiphilic helical carboxyl termini. , 1986, Proceedings of the National Academy of Sciences of the United States of America.

[29]  W. Vale,et al.  Vasoactive intestinal peptide receptor antagonist [4Cl-D-Phe6, Leu17] VIP. , 1986, The American journal of physiology.

[30]  J. Bali,et al.  Synthesis and biological activities of some pseudo-peptide analogues of tetragastrin: the importance of the peptide backbone. , 1985, Journal of medicinal chemistry.

[31]  D. Coy,et al.  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 antagonist. , 1985, Endocrinology.

[32]  D. Coy,et al.  Structure-activity studies on the N-terminal region of growth hormone releasing factor. , 1985, Journal of medicinal chemistry.

[33]  R. Jensen,et al.  Receptors for vasoactive intestinal peptide and secretin on rat pancreatic acini. , 1984, The American journal of physiology.

[34]  D. Coy,et al.  Super-active analogs of growth hormone-releasing factor (1-29)-amide. , 1984, Biochemical and biophysical research communications.

[35]  W. Mattice,et al.  Lipid‐induced conformational changes in glucagon, secretin, and vasoactive intestinal peptide , 1982, Biopolymers.

[36]  R. Jensen,et al.  Interactions of COOH-terminal fragments of cholecystokinin with receptors on dispersed acini from guinea pig pancreas. , 1982, The Journal of biological chemistry.

[37]  S. Peikin,et al.  Kinetics of amylase release by dispersed acini prepared from guinea pig pancreas. , 1978, The American journal of physiology.

[38]  Y. Cheng,et al.  Relationship between the inhibition constant (K1) and the concentration of inhibitor which causes 50 per cent inhibition (I50) of an enzymatic reaction. , 1973, Biochemical pharmacology.

[39]  M. Ondetti,et al.  Secretin. V. Solvent effects and conformational freedom. , 1972, Journal of the American Chemical Society.

[40]  V. Mutt,et al.  Synthesis of secretin. IV. Secondary structure in a miniature protein. , 1969, Journal of the American Chemical Society.

[41]  F. Plum Handbook of Physiology. , 1960 .

[42]  H. Schild pAx and competitive drug antagonism. , 1949, British journal of pharmacology and chemotherapy.

[43]  L. Johnson,et al.  Physiology of the gastrointestinal tract , 2012 .

[44]  G. Fisone,et al.  Galanin and galanin antagonists: molecular and biochemical perspectives. , 1992, Trends in pharmacological sciences.

[45]  S. Said Vasoactive intestinal peptide , 1986 .