Modulation of Immune Function by Intestinal Neuropeptides

References

• McGillis J P, Mitsuhashi M, Payan DC. Immunomodulation by tachykinin neuropeptides. Ann NY Acad Sci 1990; 594: 85–94
   PubMed Web of Science ®Google Scholar
• McGuigan JE. Hormones of the gastrointestinal tract. Endocrinology, L J DeGroot, G M Besser, G F Cahill, et al. W.B. Saunders Co, Philadelphia 1989; 2741–68
   Google Scholar
• Feher E, Burnstock G. Ultrastructural localisation of substance P, vasoactive intestinal polypeptide, somatostatin and neuropeptide Y immunoreactivity in perivascular nerve plexuses of the gut. Blood Vessels 1986; 23: 125–36
   PubMedGoogle Scholar
• Gates T S, Zimmerman R P, Mantyh C R, et al. Substance P and substance K receptor binding sites in the human gastrointestinal tract: localization by autoradiography. Peptides 1988; 9: 1207–19
   PubMed Web of Science ®Google Scholar
• Bellinger D L, Lorton D, Romano T D, Olschowka J A, Felten S Y, Felten DL. Neuropeptide innervation of lymphoid organs. Ann NY Acad Sci 1990; 594: 17–33
   PubMed Web of Science ®Google Scholar
• Payan D G, McGillis J P, Organist ML. Binding charcteristics and affinity labeling of protein constituents of the human IM-9 lumphoblast receptor for substance P. J Biol Chem 1986; 261: 14321–9
   PubMed Web of Science ®Google Scholar
• Payan D G, Brewster D R, Missirian Bastian A, Goetzl EJ. Substance P recognition by subset of human T lymphocytes. J Clin Invest 1984; 74: 1532–9
   PubMed Web of Science ®Google Scholar
• McGillis J P, Organist M L, Payan DG. Immunoaffinity purification of membrane protein constituents of the IM-9 lymphoblast receptor for substance P. Anal Biochem 1987; 164: 502–13
   PubMed Web of Science ®Google Scholar
• Payan D G, Brewster D R, Goetzl EJ. Stereospecific receptors for substance P on cultured human IM-9 lymphoblasts. J Immunol 1984; 133: 3260–5
   PubMed Web of Science ®Google Scholar
• Organist M L, Harvey J P, McGillis J P, Payan DG. Processing of the human IM-9 lymphoblast substance P receptor. Biosynthetic and degradation studies using a monoclonal antibody. Biochem Biophys Res Commun 1988; 151: 535–41
   PubMed Web of Science ®Google Scholar
• Yokota Y, Sasai Y, Tanaka K, et al. Molecular characterization of a functional cDNA for rat substance P receptor. J Biol Chem 1989; 264: 17649–52
   PubMed Web of Science ®Google Scholar
• Hershey A D, Krause JE. Molecular characterization of a functional cDNA encoding the rat substance P receptor. Science 1990; 247: 958–62
   PubMed Web of Science ®Google Scholar
• Scicchitano R, Bienenstock J, Stanisz AM. The differential effect with time of neuropeptides on the proliferative responses of murine Peyer's patch and splenic lymphocytes. Brain Behav Immun 1987; I: 231–7
   Google Scholar
• Payan D G, Brewster D R, Goetzl EJ. Specific stimulation of human T lymphocytes by substance P. J Immunol 1983; 131: 1613–5
   PubMed Web of Science ®Google Scholar
• Stanisz A M, Befus D, Bienenstock J. Differential effects of vasoactive intestinal peptide, substance P, and somatostatin on immunoglobulin synthesis and proliferations by lymphocytes from Peyer's patches, mesenteric lymph nodes, and spleen. J Immunol 1986; 136: 152–6
   PubMed Web of Science ®Google Scholar
• Wagner F, Fink R, Hart R, Dancygier H. Substance P enhances interferon-gamma production by human blood mononuclear cells. Regul Pept 1987; 19: 355–64
   PubMed Web of Science ®Google Scholar
• Scicchitano R, Bienenstock J, Stanisz AM. In vivo immunomodulation by the neuropeptide substance P. Immunol 1988; 63: 733–5
   PubMed Web of Science ®Google Scholar
• Hartung H P, Toyka KV. Activation of macrophages by substance P: induction of oxidative burst and thromboxane release. Eur J Pharmacol 1983; 89: 301–5
   PubMed Web of Science ®Google Scholar
• Hartung H P, Wolters K, Toyka KV. Substance P: binding properties and studies on cellular responses in guinea pig macrophages. J Immunol 1986; 136: 3856–63
   PubMed Web of Science ®Google Scholar
• Peck R. Neuropeptides modulating macrophage function. Ann NY Acad Sci 1987; 496: 264–70
   PubMed Web of Science ®Google Scholar
• Laurenzi M A, Persson M A, Dalsgaard C J, Haegerstrand A. The neuropeptide substance P stimulates production of inter-leukin 1 in human blood monocytes: activated cells are preferentially influenced by the neuropeptide. Scand J Immunol 1990; 31: 529–33
   PubMed Web of Science ®Google Scholar
• Lotz M, Vaughan J H, Carson DA. Effect of neuropeptides on production of inflammatory cytokines by human monocytes. Science 1988; 241: 1218–21
   PubMed Web of Science ®Google Scholar
• Ruff M R, Wahl S M, Pert CB. Substance P receptor-mediated chemotaxis of human monocytes. Peptides 1985; 6: 107–11
   PubMed Web of Science ®Google Scholar
• Serra M C, Bazzoni F, Delia Bianca V, Greskowiak M, Rossi F. Activation of human neutrophils by substance P. Effect on oxidative metabolism, exocytosis, cytosolic Ca2 ' concentration and inositol phosphate formation. J Immunol 1988; 141: 2118–24
   PubMed Web of Science ®Google Scholar
• Hafstrom I, Gyllenhammer H, Palmblad J, Ringertz B. Substance P activates and modulates neutrophil oxidative metabolism and aggregation. J Rheumatol 1989; 16: 1033–7
   PubMed Web of Science ®Google Scholar
• Cornaglia Ferraris P, Cornara L, Melodia A. Sensory neuropeptides (substance P) and 4–11 SP enhance human neutrophils chemiluminescence; the role of L-arginine. Int J Immunopharmacol 1986; 8: 463–8
   PubMed Web of Science ®Google Scholar
• Ali H, Leung K B, Pearce F L, Hayes N A, Foreman JC. Comparsion of the histamine-releasing action of substance P on mast cells and basophils from different species and tissues. Int Arch Allergy Appl Immunol 1986; 79: 413–8
   PubMedGoogle Scholar
• Mannaioni P F, Fantozzi R, Giannella E, Masini E. Pathophysiological significance of the distribution of histamine receptor sub-types: a proposed dual role for histamine in inflammation and type I hypersensitivity reactions. Agents Actions 1988; 24: 26–34
   PubMedGoogle Scholar
• Bar-Shavit Z, Goldman R, Stabinsky Y, et al. Enhancement of phagocytosis—a newly found activity of substance P residing in its n-terminal tetrapeptide sequence. Biochem Biophys Res Commun 1980; 94: 1445–51
   PubMed Web of Science ®Google Scholar
• Wass J AH. Somatostatin. Endocrinology, L J DeGroot, G M Besser, GF Cahill, et al. W.B. Saunders Co, Philadelphia, 199: 152–3
   Google Scholar
• Scicchitano R, Dazin P, Bienenstock J, Payan D G, Stanisz AM. Distribution of somatostatin receptors on murine spleen and Peyer's patch T and B lymphocytes. Brain Behav Immun 1987; 1: 173–84
   PubMedGoogle Scholar
• Bhathena S J, Louie J, Schechter G P, Redman R S, Wahl L, Recant L. Identification of human mononuclear leukocytes bearing receptors for somatostatin and glucagon. Diabetes 1981; 30: 127–31
   PubMed Web of Science ®Google Scholar
• Sreedharan S P, Kodama K T, Peterson K E, Goetzl EJ. Distinct subsets of somatostatin receptors on cultured human lymphocytes. J Biol Chem 1989; 264: 949–52
   PubMed Web of Science ®Google Scholar
• Krco C J, Gores A, Go VL. Gastrointestinal regulatory peptides modulate in vitro immune reactions of mouse lymphoid cells. Clin Immunol Immunopathol 1986; 39: 308–18
   PubMedGoogle Scholar
• Pawlikowski M, Stepien H, Kunert Radek J, Zelazowski P, Schally AV. Immunomodulatory action of somatostatin. Ann NY Acad Sci 1987; 496: 233–39
   PubMed Web of Science ®Google Scholar
• Pawlikowski M, Stepien H, Radek J, Schally AV. Effect of somatostatin on the proliferation of mouse spleen lymphocytes in vitro. Biochem Biophys Res Commun 1985; 129: 52–5
   PubMed Web of Science ®Google Scholar
• Johansson O, Sandberg G. Effect of the neuropeptides beta-MSH, neurotensin, NPY, PHI, somatostatin and substance P on proliferation of lymphocytes in vitro. Acta Physiol Scand 1989; 137: 107–11
   PubMedGoogle Scholar
• Payan D G, Hess C A, Goetzl EJ. Inhibition by somatostatin of the proliferation of T-lymphocytes and Molt-4 lymphoblasts. Cell Immunol 1984; 84: 433–8
   PubMed Web of Science ®Google Scholar
• Malec P, Zeman K, Markiewicz K, Tchorzewski H, Nowak Z, Baj Z. Short-term somatostatin infusion affects T lymphocyte responsiveness in humans. Immunopharmacology 1989; 17: 45–9
   PubMed Web of Science ®Google Scholar
• Vehmeyer K, Schuff Werner P, Nagel GA. Suppressed colony formation of peripheral blood lymphocytes in a patient with somatostatinoma. Clin Immunol Immunopathol 1986; 41: 290–4
   PubMedGoogle Scholar
• Foris G, Gyimesi E, Komaromi I. The mechanism of anit-body-dependent cellular cytotoxicity stimulation by somatostatin in rat peritoneal macrophages. Cell Immunol 1985; 90: 217–25
   PubMed Web of Science ®Google Scholar
• Cornell R P, McClellan CC. Modulation of hepatic reticuloendothelial system phagocytosis by pancreatic hormones. J Reticuloendothel Soc 1982; 32: 397–407
   PubMedGoogle Scholar
• Goetzl E J, Payan DG. Inhibition by somatostatin of the release of mediators from human basophils and rat leukemic basophils. J Immunol 1984; 133: 3255–9
   PubMed Web of Science ®Google Scholar
• Goetzl E J, Chernov T, Renold F, Payan DG. Neuropeptide regulation of the expression of immediate hypersensitivity. J Immunol 1985; 135: 802–5
   Web of Science ®Google Scholar
• Goetzl E J, Chernov Rogan T, Cooke M P, Renold F, Payan DG. Endogenous somatostatin-like peptides of rat basophilic leukemia cells. J Immunol 1985; 135: 2707–12
   PubMed Web of Science ®Google Scholar
• Ottaway C A, Lewis D L, Asa SL. Vasoactive intestinal pep-tide-containing nerves in Peyer's patches. Brain Behav Immun 1987; 1: 148–58
   PubMedGoogle Scholar
• Beed E A, O'Dorisio M S, O'Dorisio T M, Gaginella TS. Demonstration of a functional receptor for vasoactive intestinal polypeptide on Molt 4b T lymphoblasts. Regul Pept 1983; 6: 1–12
   PubMedGoogle Scholar
• Danek A, O'Dorisio M S, O'Dorisio T M, George JM. Specific binding sites for vasoactive intestinal polypeptide on nonadherent peripheral blood lymphocytes. J Immunol 1983; 131: 1173–7
   PubMed Web of Science ®Google Scholar
• Ottaway C A, Greenberg GR. Interaction of vasoactive intestinal peptide with mouse lymphocytes: specific binding and the modulation of mitogen responses. J Immunol 1984; 132: 417–23
   PubMed Web of Science ®Google Scholar
• O'Dorisio M S, Shannon B T, Fleshman D J, Campolito LB. Identification of high affinity receptors for vasoactive intestinal peptide on human lymphocytes of B cell lineage. J Immunol 1989; 142: 3533–6
   PubMed Web of Science ®Google Scholar
• Ottaway CA. Selective effects of vasoactive intestinal peptide on the mitogenic response of murine T cells. Immunology 1987; 62: 291–7
   PubMed Web of Science ®Google Scholar
• Ottaway CA. In vitro alteration of receptors for vasoactive intestinal peptide changes the in vivo localization of mouse T cells. J Exp Med 1984; 160: 1054–69
   PubMed Web of Science ®Google Scholar
• Moore TC. Modification of lymphocyte traffic by vasoactive neurotransmitter substances. Immunology 1984; 52: 511–8
   PubMed Web of Science ®Google Scholar
• Moore T C, Spruck C H, Said SI. Depression of lymphocyte traffic in sheep by vasoactive intestinal peptide (VIP). Immunology 1988; 64: 475–8
   PubMed Web of Science ®Google Scholar
• Rola-Leszczynski M, Bolduc D, St Pierre S. The effects of vasoactive intestinal peptide on human natural killer cell function. J Immunol 1985; 135: 2569–73
   PubMed Web of Science ®Google Scholar
• O'Dorisio M S, Hermina N S, O'Dorisio T M, Balcerzak SP. Vasoactive intestinal polypeptide modulation of lymphocyte adenylate cyclase. J Immunol 1981; 127: 2551–4
   PubMed Web of Science ®Google Scholar
• Calvo J R, Guerrero J M, Molinero P, Blasco R, Goberna R. Interaction of vasoactive intestinal peptide (VIP) with human peripheral blood lymphocytes: specific binding and cyclic AMP production. Gen Pharmacol 1986; 17: 185–9
   PubMedGoogle Scholar
• O'Dorisio M S, Wood C L, Wenger G D, Vassalo LM. Cyclic AMP-dependent protein kinase in Molt 4b lymphoblasts: identification by photoaffinity labeling and activation in intact cells by vasoactive intestinal polypeptide (VIP) and peptide histidine isoleucine (PHI). J Immunol 1985; 134: 4078–86
   PubMed Web of Science ®Google Scholar
• Wiik P, Opstad P K, Byum A. Binding of vasoactive intestinal polypeptide (VIP) by human blood monocytes: demonstration of specific binding sites. Regul Pept 1985; 12: 145–53
   PubMed Web of Science ®Google Scholar
• Wiik P, Haugen A H, Lvhaug D, Byum A, Opstad PK. Effect of VIP on the respiratory burst in human monocytes ex vivo during prolonged strain and energy deficiency. Peptides 1989; 10: 819–23
   PubMed Web of Science ®Google Scholar
• Wiik P. Vasoactive intestinal peptide inhibits the respiratory burst in human monocytes by a cyclic AMP-mediated mechanism. Regul Pept 1989; 25: 187–97
   PubMed Web of Science ®Google Scholar
• McIlwain H, Bachelard H. S. Biochemistry and the central nervous systemsecond edition. Churchill Livingston, New York 1985; 497–500
   Google Scholar
• Felten D L, Felten S Y, Carlson S L, Olschowka J A, Livnat S. Noradrenergic and peptidergic innervation of lymphoid tissue. J Immunol 1985; 135: 755–65
   PubMed Web of Science ®Google Scholar
• Wybran J, Schandene L, Van Vorren J P, et al. Immunologic patterns of methionine-enkephalin, and therapeutic implications in AIDS, ARC, and cancer. Ann NY Acad Sci 1987; 496: 108–14
   PubMed Web of Science ®Google Scholar
• Mehrishi J N, Mills IH. Opiate receptors on lymphocytes and platelets in man. Clin Immunol Immunopathol 1983; 27: 240–9
   PubMedGoogle Scholar
• Hucklebridge F H, Hudspith B N, Muhamed J, Lydyard P M, Brostoff J. Methionine-enkephalin stimulates in vitro proliferation of human peripheral lymphocytes via delta-opioid receptors. Brain Behav Immunol 1989; 3: 183–9
   PubMedGoogle Scholar
• Kharkevich D D, Kadagidze ZG. The effect of the stimulation of opioid receptors on lymphocyte functional activity in vivo. Biull Eksp Biol Med 1989; 108: 315–6
   PubMedGoogle Scholar
• Li G, Fraker PJ. Methionine-enkephalin alteration of mito-genic and mixed lymphocyte culture responses in zinc-deficient mice. Chung Kuo Yao Li Hsueh Pao 1989; 10: 216–21
   PubMed Web of Science ®Google Scholar
• Plontnikoff N P, Miller GC. Enkephalins as immunomodula-tors. Int J Immunopharmacol 1983; 5: 437–41
   PubMedGoogle Scholar
• Zonzulia A A, Voronkova T L, Patsakova E, Ivanushkin AM. Importance of opiate receptor ligands in regulating lymphocyte proliferative activity. Farmakol Toksikol 1987; 50: 58–9
   Google Scholar
• Faith R E, Liang H J, Plotnikoff N P, Murgo A J, Nimeh NF. Neuroimmunomodulation with enkephalins: in vitro enhancement of natural killer cell activity in peripheral blood lymphocytes from cancer patients. Natl Immun Cell Growth Regul 1987; 6: 88–98
   PubMedGoogle Scholar
• Ye S, Applegren R R, Davis J M, Cheung HT. Modulation of lymphocyte motility by beta-endorphin and met-enkephalin. Immunopharmacology 1989; 17: 81–9
   PubMedGoogle Scholar
• Plotnikoff N P, Murgo A J, Miller G C, Corder C N, Faith RE. Enkephalins: immunomodulators. Fed Proc 1985; 44: 118–22
   PubMedGoogle Scholar
• De Carolis C, De Sanctis G, Perricone R, et al. Evidence for an inhibitory role of beta-endorphin and other opioids on human total T rosette formation. Experientia 1984; 40: 738–9
   PubMedGoogle Scholar
• Jankovic B D, Marie D. Enkephalins and immunity I: in vivo suppression and potentiation of humoral immune response. Ann NY Acad Sci 1987; 496: 115–25
   PubMed Web of Science ®Google Scholar
• Marie D, Jankovic BD. Enkephalins and immunity. II: in vivo modulation of cell-mediated immunity. Ann NY Acad Sci 1987; 496: 126–36
   PubMed Web of Science ®Google Scholar
• Foris G, Medgyesi G A, Hauck M. Bidirectional effect of met-enkephalin on macrophage effector functions. Mol Cell Biochem 1986; 69: 127–37
   PubMed Web of Science ®Google Scholar
• Petty H R, Berg KA. Combinative ligand-receptor interactions: epinephrine depresses RAW264 macrophage antibody-dependent phagocytosis in the absence and presence of met-enkephalin. J Cell Physiol 1988; 134: 281–6
   PubMed Web of Science ®Google Scholar
• Foris G, Medgyesi G A, Gyimesi E, Hauck M. Metenkephalin induced alterations of macrophage functions. Mol Immunol 1984; 21: 747–50
   PubMed Web of Science ®Google Scholar
• Yang S X, Li XY. Enhancement of interleukin-1 production in mouse peritoneal macrophages by methionine-enkephalin. Chung Kuo Yao Li Hsueh Pao 1989; 10: 266–70
   PubMed Web of Science ®Google Scholar
• Willems J, Leclercq G, Joniau M. Enhanced oxygen metabolism of peritoneal macrophages in the presence of murine neuroblastoma cells is partly caused by enkephalins. J Neuroimmunol 1988; 19: 269–78
   PubMed Web of Science ®Google Scholar
• Cameron DJ. Effect of neuropeptides on macrophage mediated cytotoxicity in normal donors and cancer patients. Jpn J Exp Med 1987; 57: 31–9
   PubMedGoogle Scholar
• Prieto J, Subira M L, Castilla A, Arroyo J L, Serrano M. Opioid peptides modulate the organization of vimentin filaments, phagocytic activity, and expression of surface molecules in monocytes. Scand J Immunol 1989; 29: 391–8
   PubMed Web of Science ®Google Scholar
• Simpkins C O, Alailima S T, Tate E A, Johnson M. The effect of enkephalins and prostaglandins on O-2 release by neutrophils. J Surg Res 1986; 41: 645–52
   PubMed Web of Science ®Google Scholar
• van Epps D E, Kutvirt SL. Modulation of human neutrophil adherence by beta-endorphin and met-enkephalin. J Neuroimmunol 1987; 15: 219–28
   PubMed Web of Science ®Google Scholar
• Macintyre I. Calciton In: physiology, biosynthesis, secretion, metabolism, and mode of action. Endocrinology, L J DeGroot, G M Besser, G F Cahill, et al. W.B. Saunders Co, Philadelphia 1989; 892–901
   Google Scholar
• Stead R H, Tomioka M, Quinonez G, Simon G T, Felten S Y, Bienenstock J. Intestinal mucosal mast cells in normal and nematode-infected rat intestines are in intimate contact with peptidergic nerves. Proc Natl Acad Sci USA 1987; 84: 2975–9
   PubMed Web of Science ®Google Scholar
• Umeda Y, Arisawa M. Characterization of the calcitonin gene-related peptide receptor in mouse T lymphocytes. Neuropeptides 1989; 14: 237–42
   PubMed Web of Science ®Google Scholar
• Umeda Y, Takamiya M, Yoshizaki H, Arisawa M. Inhibition of mitogen-stimulated T lymphocyte proliferation by calcitonin gene-related peptide. Biochem Bophys Res Commun 1988; 154: 227–35
   PubMed Web of Science ®Google Scholar
• Nong Y H, Titus R G, Ribeiro J M, Remold HG. Peptides encoded by the calcitonin gene inhibit macrophage function. J Immunol 1989; 143: 45–9
   PubMed Web of Science ®Google Scholar
• Abello J, Kaiserlian-Nicolas D, Cuber J C, Revillard J P, Chayvialle JA. Identification of high affinity calcitonin gene-related peptide receptors on a murine macrophage-like cell line. Ann NY Acad Sci 1990; 594: 364–6
   Web of Science ®Google Scholar
• Manley H C, Haynes LW. Eosinophil chemotactic response to rat CGRP-1 is increased after exposure to trypsin or guinea-pig lung particulate fraction. Neuropeptides 1989; 13: 29–34
   PubMed Web of Science ®Google Scholar
• Soder O, Hellström PM. Neuropeptide regulation of human thymocyte, guinea pig T lymphocyte and rat B lymphocyte mitogenesis. Int Arch Allergy Appl Immunol 1987; 84: 205–11
   PubMedGoogle Scholar
• Jones J V, James H, Mansour M. Neuropeptide Y modulates t cell proliferation in vitro: A new interaction of the immune and neuroendocrine systems. Ann NY Acad Sci 1990; 594: 388–90
   Web of Science ®Google Scholar
• Freier S, Lebenthal E. The neuroendocrine-immune network in the gastrointestinal tract. The neuroendocrine-immune network, S Freier. CRC Press Inc, Boca Raton 1990; 239–55
   Google Scholar
• McMillen M A, Ferrara A, Schaefer H C, Goldenring J R, Zucker K A, Modlin IM. Cholecystokinin mediates a calcium signal in human peripheral blood mononuclear cells and is a co-mitogen. Ann NY Acad Sci 1990; 594: 399–402
   Web of Science ®Google Scholar