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Volumn 6, Issue 6, 2005, Pages 558-564

The nervous system and innate immunity: The neuropeptide connection

Author keywords

[No Author keywords available]

Indexed keywords

ADRENOMEDULLIN; ALPHA ADRENERGIC RECEPTOR STIMULATING AGENT; ALPHA INTERMEDIN; ANTIINFECTIVE AGENT; CD8 ANTIGEN; CHEMOKINE; CHEMOKINE RECEPTOR; CYCLIC AMP; CYTOKINE; DEFENSIN; ENKEPHALIN; FLUCONAZOLE; INDOLICIDIN; INTERLEUKIN 10; INTERLEUKIN 1BETA; INTERLEUKIN 6; INTERLEUKIN 8; LEUCINE ENKEPHALIN; LIPOPOLYSACCHARIDE; MELANOCORTIN RECEPTOR; MESSENGER RNA; METENKEPHALIN; NEUROPEPTIDE; NEUROPEPTIDE Y; PROENKEPHALIN A; SUBSTANCE P; TOLL LIKE RECEPTOR 4; TUMOR NECROSIS FACTOR; UNCLASSIFIED DRUG; ANTIMICROBIAL CATIONIC PEPTIDE; PEPTIDE; PROENKEPHALIN; PROTEIN PRECURSOR;

EID: 20644432642     PISSN: 15292908     EISSN: 15292916     Source Type: Journal    
DOI: 10.1038/ni1209     Document Type: Review
Times cited : (216)

References (92)
  • 1
    • 0033638849 scopus 로고    scopus 로고
    • The sympathetic nerve-an integrative interface between two supersystems: The brain and the immune system
    • Elenkov, I.J., Wilder, R.L., Chrousos, G.P. & Vizi, E.S. The sympathetic nerve-an integrative interface between two supersystems: the brain and the immune system. Pharmacol. Rev. 52, 595-638 (2000).
    • (2000) Pharmacol. Rev. , vol.52 , pp. 595-638
    • Elenkov, I.J.1    Wilder, R.L.2    Chrousos, G.P.3    Vizi, E.S.4
  • 2
    • 0037180778 scopus 로고    scopus 로고
    • The inflammatory reflex
    • Tracey, K.J. The inflammatory reflex. Nature 420, 853-859 (2002).
    • (2002) Nature , vol.420 , pp. 853-859
    • Tracey, K.J.1
  • 3
    • 0036518997 scopus 로고    scopus 로고
    • Innate immunity: The missing link in neuroprotection and neurodegeneration?
    • Nguyen, M.D., Julien, J.P. & Rivest, S. Innate immunity: the missing link in neuroprotection and neurodegeneration? Nat. Rev. Neurosci. 3, 216-227 (2002).
    • (2002) Nat. Rev. Neurosci. , vol.3 , pp. 216-227
    • Nguyen, M.D.1    Julien, J.P.2    Rivest, S.3
  • 4
    • 2942687605 scopus 로고    scopus 로고
    • Elaborate interactions between the immune and nervous systems
    • Steinman, L. Elaborate interactions between the immune and nervous systems. Nat. Immunol. 5, 575-581 (2004).
    • (2004) Nat. Immunol. , vol.5 , pp. 575-581
    • Steinman, L.1
  • 5
    • 2042513493 scopus 로고
    • Magainins, a class of antimicrobial peptides from Xenopus skin: Isolation, characterization of two active forms, and partial cDNA sequence of a precursor
    • Zasloff, M. Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor. Proc. Natl. Acad. Sci. USA 84, 5449-5453 (1987).
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 5449-5453
    • Zasloff, M.1
  • 6
    • 0014575976 scopus 로고
    • In vitro characterization of adrenergic receptors controlling skin gland secretion in two anurans, Rana pipiens and Xenopus laevis
    • Benson, B.J. & Hadley, M.E. In vitro characterization of adrenergic receptors controlling skin gland secretion in two anurans, Rana pipiens and Xenopus laevis. Comp. Biochem. Physiol. 30, 857-864 (1969).
    • (1969) Comp. Biochem. Physiol. , vol.30 , pp. 857-864
    • Benson, B.J.1    Hadley, M.E.2
  • 7
    • 0032444189 scopus 로고    scopus 로고
    • Antimicrobial peptides from amphibian skin: What do they tell us?
    • Simmaco, M., Mignogna, G. & Barra, D. Antimicrobial peptides from amphibian skin: what do they tell us? Biopolymers 47, 435-450 (1998).
    • (1998) Biopolymers , vol.47 , pp. 435-450
    • Simmaco, M.1    Mignogna, G.2    Barra, D.3
  • 9
    • 0141799911 scopus 로고    scopus 로고
    • Defensins: Antimicrobial peptides of innate immunity
    • Ganz, T. Defensins: antimicrobial peptides of innate immunity. Nat. Rev. Immunol. 3, 710-720 (2003).
    • (2003) Nat. Rev. Immunol. , vol.3 , pp. 710-720
    • Ganz, T.1
  • 10
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff, M. Antimicrobial peptides of multicellular organisms. Natur 415, 389-395 (2002).
    • (2002) Natur , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 12
    • 0036842381 scopus 로고    scopus 로고
    • Antimicrobial peptides from animals: Focus on invertebrates
    • Vizioli, J. & Salzet, M. Antimicrobial peptides from animals: focus on invertebrates. Trends Pharmacol. Sci. 23, 494-496 (2002).
    • (2002) Trends Pharmacol. Sci. , vol.23 , pp. 494-496
    • Vizioli, J.1    Salzet, M.2
  • 13
    • 0346996865 scopus 로고    scopus 로고
    • The antimicrobial peptide LL-37 activates innate immunity at the airway epithelial surface by transactivation of the epidermal growth factor receptor
    • Tjabringa, G.S. et al. The antimicrobial peptide LL-37 activates innate immunity at the airway epithelial surface by transactivation of the epidermal growth factor receptor. J. Immunol. 171, 6690-6696 (2003).
    • (2003) J. Immunol. , vol.171 , pp. 6690-6696
    • Tjabringa, G.S.1
  • 14
    • 0842326097 scopus 로고    scopus 로고
    • Cathelicidins, multifunctional peptides of the innate immunity
    • Zanetti, M. Cathelicidins, multifunctional peptides of the innate immunity. J. Leukoc. Biol. 75, 39-48 (2004).
    • (2004) J. Leukoc. Biol. , vol.75 , pp. 39-48
    • Zanetti, M.1
  • 15
    • 0036884492 scopus 로고    scopus 로고
    • Biology and clinical relevance of naturally occurring antimicrobial peptides
    • Gallo, R.L., Murakami, M., Ohtake, T. & Zaiou, M. Biology and clinical relevance of naturally occurring antimicrobial peptides. J. Allergy Clin. Immunol. 110, 823-831 (2002).
    • (2002) J. Allergy Clin. Immunol. , vol.110 , pp. 823-831
    • Gallo, R.L.1    Murakami, M.2    Ohtake, T.3    Zaiou, M.4
  • 16
    • 0142093059 scopus 로고    scopus 로고
    • Many chemokines including CCL20/MIP-3α display antimicrobial activity
    • Yang, D. et al. Many chemokines including CCL20/MIP-3α display antimicrobial activity. J. Leukoc. Biol. 74, 448-455 (2003).
    • (2003) J. Leukoc. Biol. , vol.74 , pp. 448-455
    • Yang, D.1
  • 17
    • 0034201213 scopus 로고    scopus 로고
    • Neutrophil α-defensin human neutrophil peptide modulates cytokine production in human monocytes and adhesion molecule expression in endothelial cells
    • Chaly, Y.V. et al. Neutrophil α-defensin human neutrophil peptide modulates cytokine production in human monocytes and adhesion molecule expression in endothelial cells. Eur. Cytokine Netw. 11, 257-266 (2000).
    • (2000) Eur. Cytokine Netw. , vol.11 , pp. 257-266
    • Chaly, Y.V.1
  • 18
    • 2542480000 scopus 로고    scopus 로고
    • Multiple roles of antimicrobial defensins, cathelicidins, and eosinophil-derived neurotoxin in host defense
    • Yang, D., Biragyn, A., Hoover, D.M., Lubkowski, J. & Oppenheim, J.J. Multiple roles of antimicrobial defensins, cathelicidins, and eosinophil-derived neurotoxin in host defense. Annu. Rev. Immunol. 22, 181-215 (2004).
    • (2004) Annu. Rev. Immunol. , vol.22 , pp. 181-215
    • Yang, D.1    Biragyn, A.2    Hoover, D.M.3    Lubkowski, J.4    Oppenheim, J.J.5
  • 19
    • 0035879198 scopus 로고    scopus 로고
    • Cutting edge: IFN-inducible ELR-CXC chemokines display defensin-like antimicrobial activity
    • Cole, A.M. et al. Cutting edge: IFN-inducible ELR-CXC chemokines display defensin-like antimicrobial activity. J. Immunol. 167, 623-627 (2001).
    • (2001) J. Immunol. , vol.167 , pp. 623-627
    • Cole, A.M.1
  • 20
    • 0036893696 scopus 로고    scopus 로고
    • Antimicrobial peptides from human platelets
    • Tang, Y.Q., Yeaman, M.R. & Selsted, M.E. Antimicrobial peptides from human platelets. Infect. Immun. 70, 6524-6533 (2002).
    • (2002) Infect. Immun. , vol.70 , pp. 6524-6533
    • Tang, Y.Q.1    Yeaman, M.R.2    Selsted, M.E.3
  • 21
    • 0343938877 scopus 로고    scopus 로고
    • Thrombocytopenia in liver transplant recipients: Predictors, impact on fungal infections, and role of endogenous thrombopoietin
    • Chang, F.Y. et al. Thrombocytopenia in liver transplant recipients: predictors, impact on fungal infections, and role of endogenous thrombopoietin. Transplantation 69, 70-75 (2000).
    • (2000) Transplantation , vol.69 , pp. 70-75
    • Chang, F.Y.1
  • 22
    • 0141918813 scopus 로고    scopus 로고
    • Rapid sequence divergence in mammalian β-defensins by adaptive evolution
    • Maxwell, A.I., Morrison, G.M. & Dorin, J.R. Rapid sequence divergence in mammalian β-defensins by adaptive evolution. Mol. Immunol. 40, 413-421 (2003).
    • (2003) Mol. Immunol. , vol.40 , pp. 413-421
    • Maxwell, A.I.1    Morrison, G.M.2    Dorin, J.R.3
  • 24
    • 0034998495 scopus 로고    scopus 로고
    • Induction of human β-defensin-2 expression in human astrocytes by lipopolysaccharide and cytokines
    • Hao, H.N., Zhao, J., Lotoczky, G., Grever, W.E. & Lyman, W.D. Induction of human β-defensin-2 expression in human astrocytes by lipopolysaccharide and cytokines. J. Neurochem. 77, 1027-1035 (2001).
    • (2001) J. Neurochem. , vol.77 , pp. 1027-1035
    • Hao, H.N.1    Zhao, J.2    Lotoczky, G.3    Grever, W.E.4    Lyman, W.D.5
  • 26
    • 2442664007 scopus 로고    scopus 로고
    • TLR-independent control of innate immunity in Caenorhabditis elegans by the TIR domain adaptor protein TIR-1, an ortholog of human SARM
    • Couillault, C. et al. TLR-independent control of innate immunity in Caenorhabditis elegans by the TIR domain adaptor protein TIR-1, an ortholog of human SARM. Nat. Immunol. 5, 488-494 (2004).
    • (2004) Nat. Immunol. , vol.5 , pp. 488-494
    • Couillault, C.1
  • 27
    • 19344371610 scopus 로고    scopus 로고
    • Neuropeptides and neurogenic mechanisms in oral and periodontal inflammation
    • Lundy, F.T. & Linden, G.J. Neuropeptides and neurogenic mechanisms in oral and periodontal inflammation. Crit. Rev. Oral Biol. Med. 15, 82-98 (2004).
    • (2004) Crit. Rev. Oral Biol. Med. , vol.15 , pp. 82-98
    • Lundy, F.T.1    Linden, G.J.2
  • 28
    • 0031895454 scopus 로고    scopus 로고
    • Neuropeptides in the skin: Interactions between the neuroendocrine and the skin immune systems
    • Scholzen, T. et al. Neuropeptides in the skin: interactions between the neuroendocrine and the skin immune systems. Exp. Dermatol. 7, 81-96 (1998).
    • (1998) Exp. Dermatol. , vol.7 , pp. 81-96
    • Scholzen, T.1
  • 29
    • 0242628124 scopus 로고    scopus 로고
    • Basal and activity-induced release of substance P from primary afferent fibres in NK1 receptor knockout mice: Evidence for negative feedback
    • Lever, I.J. et al. Basal and activity-induced release of substance P from primary afferent fibres in NK1 receptor knockout mice: evidence for negative feedback. Neuropharmacology 45, 1101-1110 (2003).
    • (2003) Neuropharmacology , vol.45 , pp. 1101-1110
    • Lever, I.J.1
  • 30
    • 0037126831 scopus 로고    scopus 로고
    • Interaction between interleukin 1β and endogenous neurokinin 1 receptor agonists in mediating plasma extravasation and neutrophil accumulation in the cutaneous microvasculature of the rat
    • Pinter, E., Than, M., Chu, D.Q., Fogg, C. & Brain, S.D. Interaction between interleukin 1β and endogenous neurokinin 1 receptor agonists in mediating plasma extravasation and neutrophil accumulation in the cutaneous microvasculature of the rat. Neurosci. Lett. 318, 13-16 (2002).
    • (2002) Neurosci. Lett. , vol.318 , pp. 13-16
    • Pinter, E.1    Than, M.2    Chu, D.Q.3    Fogg, C.4    Brain, S.D.5
  • 31
    • 0742299373 scopus 로고    scopus 로고
    • Neutral endopeptidase expression and distribution in human skin and wounds
    • Olerud, J.E. et al. Neutral endopeptidase expression and distribution in human skin and wounds. J. Invest. Dermatol. 112, 873-881 (1999).
    • (1999) J. Invest. Dermatol. , vol.112 , pp. 873-881
    • Olerud, J.E.1
  • 32
    • 0037025067 scopus 로고    scopus 로고
    • Direct antimicrobial properties of substance
    • Kowalska, K., Carr, D. B. & Lipkowski, A.W. Direct antimicrobial properties of substance P. Life Sci. 71, 747-750 (2002).
    • (2002) P. Life Sci. , vol.71 , pp. 747-750
    • Kowalska, K.1    Carr, D.B.2    Lipkowski, A.W.3
  • 33
    • 0029829783 scopus 로고    scopus 로고
    • Quantitation of epidermal nerves in diabetic neuropathy
    • Kennedy, W.R., Wendelschafer-Crabb, G. & Johnson, T. Quantitation of epidermal nerves in diabetic neuropathy. Neurology 47, 1042-1048 (1996).
    • (1996) Neurology , vol.47 , pp. 1042-1048
    • Kennedy, W.R.1    Wendelschafer-Crabb, G.2    Johnson, T.3
  • 34
    • 28244463304 scopus 로고
    • National Diabetes Advisory Board, Bethesda, Maryland
    • National Diabetes Advisory Board. NIH Publication 81:2284. (National Diabetes Advisory Board, Bethesda, Maryland, 1980).
    • (1980) National Diabetes Advisory Board. NIH Publication , vol.81 , pp. 2284
  • 35
    • 0036436789 scopus 로고    scopus 로고
    • Diminished neuropeptide levels contribute to the impaired cutaneous healing response associated with diabetes mellitus
    • Gibran, N.S. et al. Diminished neuropeptide levels contribute to the impaired cutaneous healing response associated with diabetes mellitus. J. Surg. Res. 108, 122-128 (2002).
    • (2002) J. Surg. Res. , vol.108 , pp. 122-128
    • Gibran, N.S.1
  • 36
    • 0035486840 scopus 로고    scopus 로고
    • Localized antimicrobial peptide expression in human gingiva
    • Dale, B.A. et al. Localized antimicrobial peptide expression in human gingiva. J. Periodontal Res. 36, 285-294 (2001).
    • (2001) J. Periodontal Res. , vol.36 , pp. 285-294
    • Dale, B.A.1
  • 37
    • 0032790393 scopus 로고    scopus 로고
    • Immunocytochemical localization of substance P neurokinin-1 receptors in rat gingival tissue
    • Kido, M.A., Yamaza, T., Goto, T. & Tanaka, T. Immunocytochemical localization of substance P neurokinin-1 receptors in rat gingival tissue. Cell Tissue Res. 297, 213-222 (1999).
    • (1999) Cell Tissue Res. , vol.297 , pp. 213-222
    • Kido, M.A.1    Yamaza, T.2    Goto, T.3    Tanaka, T.4
  • 38
    • 0023753067 scopus 로고
    • Effect of neuropeptides on production of inflammatory cytokines by human monocytes
    • Lotz, M., Vaughan, J.H. & Carson, D.A. Effect of neuropeptides on production of inflammatory cytokines by human monocytes. Science 241, 1218-1221 (1988).
    • (1988) Science , vol.241 , pp. 1218-1221
    • Lotz, M.1    Vaughan, J.H.2    Carson, D.A.3
  • 39
    • 0029556316 scopus 로고
    • The submandibular gland: A key organ in the neuro-immunoregulatory network?
    • Sabbadini, E. & Berczi, I. The submandibular gland: a key organ in the neuro-immunoregulatory network? Neuroimmunomodulation 2, 184-202 (1995).
    • (1995) Neuroimmunomodulation , vol.2 , pp. 184-202
    • Sabbadini, E.1    Berczi, I.2
  • 40
    • 0344483901 scopus 로고    scopus 로고
    • Production of β-defensin antimicrobial peptides by the oral mucosa and salivary glands
    • Mathews, M. et al. Production of β-defensin antimicrobial peptides by the oral mucosa and salivary glands. Infect. Immun. 67, 2740-2745 (1999).
    • (1999) Infect. Immun. , vol.67 , pp. 2740-2745
    • Mathews, M.1
  • 41
    • 0037068959 scopus 로고    scopus 로고
    • Deficiency of antibacterial peptides in patients with morbus Kostmann: An observation study
    • Putsep, K., Carlsson, G., Boman, H. & Andersson, M. Deficiency of antibacterial peptides in patients with morbus Kostmann: an observation study. Lancet 360, 1144-1149 (2002).
    • (2002) Lancet , vol.360 , pp. 1144-1149
    • Putsep, K.1    Carlsson, G.2    Boman, H.3    Andersson, M.4
  • 43
    • 0037899136 scopus 로고    scopus 로고
    • Developmental control of foraging and social behavior by the Drosophila neuropeptide Y-like system
    • Wu, Q. et al. Developmental control of foraging and social behavior by the Drosophila neuropeptide Y-like system. Neuron 39, 147-161 (2003).
    • (2003) Neuron , vol.39 , pp. 147-161
    • Wu, Q.1
  • 44
    • 0037222949 scopus 로고    scopus 로고
    • Relevance of neuropeptide Y for the neuroimmune crosstalk
    • Bedoui, S. et al. Relevance of neuropeptide Y for the neuroimmune crosstalk. J. Neuroimmunol. 134, 1-11 (2003).
    • (2003) J. Neuroimmunol. , vol.134 , pp. 1-11
    • Bedoui, S.1
  • 45
    • 0035912179 scopus 로고    scopus 로고
    • Neuropeptide Y functions as a neuroproliferative factor
    • Hansel, D.E., Eipper, B.A. & Ronnett, G.V. Neuropeptide Y functions as a neuroproliferative factor. Nature 410, 940-944 (2001).
    • (2001) Nature , vol.410 , pp. 940-944
    • Hansel, D.E.1    Eipper, B.A.2    Ronnett, G.V.3
  • 46
    • 0242317366 scopus 로고    scopus 로고
    • Neuro'-peptides in glia: Focus on NPY and galanin
    • Ubink, R., Calza, L. & Hokfelt, T. 'Neuro'-peptides in glia: focus on NPY and galanin. Trends Neurosci. 26, 604-609 (2003).
    • (2003) Trends Neurosci. , vol.26 , pp. 604-609
    • Ubink, R.1    Calza, L.2    Hokfelt, T.3
  • 47
    • 0343932591 scopus 로고    scopus 로고
    • Expression of neuropeptide Y in olfactory ensheathing cells during prenatal development
    • Ubink, R. & Hokfelt, T. Expression of neuropeptide Y in olfactory ensheathing cells during prenatal development. J. Comp. Neurol. 423, 13-25 (2000).
    • (2000) J. Comp. Neurol. , vol.423 , pp. 13-25
    • Ubink, R.1    Hokfelt, T.2
  • 48
    • 0033864917 scopus 로고    scopus 로고
    • A hamster model of equine herpesvirus 9 induced encephalitis
    • Fukushi, H. et al. A hamster model of equine herpesvirus 9 induced encephalitis. J. Neurovirol. 6, 314-319 (2000).
    • (2000) J. Neurovirol. , vol.6 , pp. 314-319
    • Fukushi, H.1
  • 49
    • 0023729911 scopus 로고
    • Olfactory neural pathway in mouse hepatitis virus nasoencephalitis
    • Barthold, S.W. Olfactory neural pathway in mouse hepatitis virus nasoencephalitis. Acta Neuropathol. (Berl.) 76, 502-506 (1988).
    • (1988) Acta Neuropathol. (Berl.) , vol.76 , pp. 502-506
    • Barthold, S.W.1
  • 50
    • 0344198505 scopus 로고    scopus 로고
    • Pneumococcal carriage results in ganglioside-mediated olfactory tissue infection
    • van Ginkel, F.W. et al. Pneumococcal carriage results in ganglioside-mediated olfactory tissue infection. Proc. Natl, Acad. Sci. USA 100, 14363-14367 (2003).
    • (2003) Proc. Natl, Acad. Sci. USA , vol.100 , pp. 14363-14367
    • Van Ginkel, F.W.1
  • 51
    • 0038386684 scopus 로고    scopus 로고
    • Expansion of the BPI family by duplication on human chromosome 20: Characterization of the RY gene cluster in 20q11.21 encoding olfactory transporters/antimicrobial-like peptides
    • Andrault, J.B., Gaillard, I., Giorgi, D. & Rouquier, S. Expansion of the BPI family by duplication on human chromosome 20: characterization of the RY gene cluster in 20q11.21 encoding olfactory transporters/antimicrobial-like peptides. Genomics 82, 172-184 (2003).
    • (2003) Genomics , vol.82 , pp. 172-184
    • Andrault, J.B.1    Gaillard, I.2    Giorgi, D.3    Rouquier, S.4
  • 52
    • 1642575358 scopus 로고    scopus 로고
    • Phylogenetic and evolutionary analysis of the PLUNC gene family
    • Bingle, C.D. et al. Phylogenetic and evolutionary analysis of the PLUNC gene family. Protein Sci. 13, 422-430 (2004).
    • (2004) Protein Sci. , vol.13 , pp. 422-430
    • Bingle, C.D.1
  • 53
    • 0032007337 scopus 로고    scopus 로고
    • Role of the bactericidal/permeability-increasing protein in host defence
    • Elsbach, P. & Weiss, J. Role of the bactericidal/permeability- increasing protein in host defence. Curr. Opin. Immunol. 10, 45-49 (1998).
    • (1998) Curr. Opin. Immunol. , vol.10 , pp. 45-49
    • Elsbach, P.1    Weiss, J.2
  • 54
    • 0037066689 scopus 로고    scopus 로고
    • Plunc, a member of the secretory gland protein family, is up-regulated in nasal respiratory epithelium after olfactory bulbectomy
    • Sung, Y.K. et al. Plunc, a member of the secretory gland protein family, is up-regulated in nasal respiratory epithelium after olfactory bulbectomy. J. Biol. Chem. 277, 12762-12769 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 12762-12769
    • Sung, Y.K.1
  • 55
    • 0030023749 scopus 로고    scopus 로고
    • Broad spectrum antibiotic activity of the skin-PYY
    • Vouldoukis, I., Shai, Y., Nicolas, P. & Mor, A. Broad spectrum antibiotic activity of the skin-PYY. FEBS Lett. 380, 237-240 (1996).
    • (1996) FEBS Lett. , vol.380 , pp. 237-240
    • Vouldoukis, I.1    Shai, Y.2    Nicolas, P.3    Mor, A.4
  • 56
    • 0037445824 scopus 로고    scopus 로고
    • Regulation of production and secretion of adrenomedullin in the cardiovascular system
    • Eto, T., Kato, J. & Kitamura, K. Regulation of production and secretion of adrenomedullin in the cardiovascular system. Regul. Pept. 112, 61-69 (2003).
    • (2003) Regul. Pept. , vol.112 , pp. 61-69
    • Eto, T.1    Kato, J.2    Kitamura, K.3
  • 57
    • 0031763330 scopus 로고    scopus 로고
    • Novel sites of adrenomedullin gene expression in mouse and rat tissues
    • Cameron, V.A. & Fleming, A.M. Novel sites of adrenomedullin gene expression in mouse and rat tissues. Endocrinology 139, 2253-2264 (1998).
    • (1998) Endocrinology , vol.139 , pp. 2253-2264
    • Cameron, V.A.1    Fleming, A.M.2
  • 58
    • 0034887742 scopus 로고    scopus 로고
    • Alternative splicing of the proadrenomedullin gene results in differential expression of gene products
    • Martinez, A., Hodge, D.L., Garayoa, M., Young, H.A. & Cuttitta, F. Alternative splicing of the proadrenomedullin gene results in differential expression of gene products. J. Mol. Endocrinol. 27, 31-41 (2001).
    • (2001) J. Mol. Endocrinol. , vol.27 , pp. 31-41
    • Martinez, A.1    Hodge, D.L.2    Garayoa, M.3    Young, H.A.4    Cuttitta, F.5
  • 59
    • 0032574982 scopus 로고    scopus 로고
    • RAMPs regulate the transport and ligand specificity of the calcitonin-receptor-like receptor
    • McLatchie, L.M. et al. RAMPs regulate the transport and ligand specificity of the calcitonin-receptor-like receptor. Nature 393, 333-339 (1998).
    • (1998) Nature , vol.393 , pp. 333-339
    • McLatchie, L.M.1
  • 60
    • 0036130816 scopus 로고    scopus 로고
    • Functional interaction of G protein-coupled receptors of the adrenomedullin peptide family with accessory receptor-activity-modifying proteins (RAMP)
    • Born, W., Muff, R. & Fischer, J.A. Functional interaction of G protein-coupled receptors of the adrenomedullin peptide family with accessory receptor-activity-modifying proteins (RAMP). Microsc. Res. Tech. 57, 14-22 (2002).
    • (2002) Microsc. Res. Tech. , vol.57 , pp. 14-22
    • Born, W.1    Muff, R.2    Fischer, J.A.3
  • 61
    • 0031663474 scopus 로고    scopus 로고
    • Induction of adrenomedullin mRNA and protein by lipopolysaccharide and paclitaxel (Taxol) in murine macrophages
    • Zaks-Zilberman, M., Salkowski, C.A., Elsasser, T., Cuttitta, F. & Vogel, S.N. Induction of adrenomedullin mRNA and protein by lipopolysaccharide and paclitaxel (Taxol) in murine macrophages. Infect. Immun. 66, 4669-4675 (1998).
    • (1998) Infect. Immun. , vol.66 , pp. 4669-4675
    • Zaks-Zilberman, M.1    Salkowski, C.A.2    Elsasser, T.3    Cuttitta, F.4    Vogel, S.N.5
  • 62
    • 0032934134 scopus 로고    scopus 로고
    • An investigation into the antimicrobial effects of adrenomedullin on members of the skin, oral, respiratory tract and gut microflora
    • Allaker, R.P., Zihni, C. & Kapas, S. An investigation into the antimicrobial effects of adrenomedullin on members of the skin, oral, respiratory tract and gut microflora. FEMS Immunol. Med. Microbiol. 23, 289-293 (1999).
    • (1999) FEMS Immunol. Med. Microbiol. , vol.23 , pp. 289-293
    • Allaker, R.P.1    Zihni, C.2    Kapas, S.3
  • 63
    • 0034888528 scopus 로고    scopus 로고
    • Adrenomedullin expression in pathogen-challenged oral epithelial cells
    • Kapas, S. et al. Adrenomedullin expression in pathogen-challenged oral epithelial cells. Peptides 22, 1485-1489 (2001).
    • (2001) Peptides , vol.22 , pp. 1485-1489
    • Kapas, S.1
  • 64
    • 0037445828 scopus 로고    scopus 로고
    • Adrenomedullin and mucosal defence: Interaction between host and microorganism
    • Allaker, R.P. & Kapas, S. Adrenomedullin and mucosal defence: interaction between host and microorganism. Regul. Pept. 112, 147-152 (2003).
    • (2003) Regul. Pept. , vol.112 , pp. 147-152
    • Allaker, R.P.1    Kapas, S.2
  • 65
    • 0034802638 scopus 로고    scopus 로고
    • Adrenomedullin and proadrenomudullin N-terminal 20 peptide (PAMP) are present in human colonic epithelia and exert an antimicrobial effect
    • Marutsuka, K. et al. Adrenomedullin and proadrenomudullin N-terminal 20 peptide (PAMP) are present in human colonic epithelia and exert an antimicrobial effect. Exp. Physiol. 86, 543-545 (2001).
    • (2001) Exp. Physiol. , vol.86 , pp. 543-545
    • Marutsuka, K.1
  • 66
    • 0037237885 scopus 로고    scopus 로고
    • Adrenomedullin: Expression and possible role in human skin and hair growth
    • Muller, F.B. et al. Adrenomedullin: expression and possible role in human skin and hair growth. Br. J. Dermatol. 148, 30-38 (2003).
    • (2003) Br. J. Dermatol. , vol.148 , pp. 30-38
    • Muller, F.B.1
  • 67
    • 0030670077 scopus 로고    scopus 로고
    • Expression of adrenomedullin and its receptor in normal and malignant human skin: A potential pluripotent role in the integument
    • Martinez, A. et al. Expression of adrenomedullin and its receptor in normal and malignant human skin: a potential pluripotent role in the integument. Endocrinology 138, 5597-5604 (1997).
    • (1997) Endocrinology , vol.138 , pp. 5597-5604
    • Martinez, A.1
  • 68
    • 12244253012 scopus 로고    scopus 로고
    • Adrenomedullin in gingival crevicular fluid in periodontal health and disease
    • Lundy, F.T. et al. Adrenomedullin in gingival crevicular fluid in periodontal health and disease. J. Dent. Res. 80, 1176 (2001).
    • (2001) J. Dent. Res. , vol.80 , pp. 1176
    • Lundy, F.T.1
  • 69
    • 0033303560 scopus 로고    scopus 로고
    • Underlying disease stress augments plasma and tissue adrenomedullin (AM) responses to endotoxin: Colocalized increases in AM and inducible nitric oxide synthase within pancreatic islets
    • Elsasser, T.H. et al. Underlying disease stress augments plasma and tissue adrenomedullin (AM) responses to endotoxin: colocalized increases in AM and inducible nitric oxide synthase within pancreatic islets. Endocrinology 140, 5402-5411 (1999).
    • (1999) Endocrinology , vol.140 , pp. 5402-5411
    • Elsasser, T.H.1
  • 71
    • 0033736084 scopus 로고    scopus 로고
    • New aspects on the melanocortins and their receptors
    • Wikberg, J.E. et al. New aspects on the melanocortins and their receptors. Pharmacol. Res. 42, 393-420 (2000).
    • (2000) Pharmacol. Res. , vol.42 , pp. 393-420
    • Wikberg, J.E.1
  • 72
    • 0033665323 scopus 로고    scopus 로고
    • Neuropeptide regulation of immunity. The immunosuppressive activity of α-melanocyte-stimulating hormone (α-MSH)
    • Taylor, A.W., Yee, D.G., Nishida, T. & Namba, K. Neuropeptide regulation of immunity. The immunosuppressive activity of α-melanocyte- stimulating hormone (α-MSH). Ann. NY Acad. Sci. 917, 239-247 (2000).
    • (2000) Ann. NY Acad. Sci. , vol.917 , pp. 239-247
    • Taylor, A.W.1    Yee, D.G.2    Nishida, T.3    Namba, K.4
  • 73
    • 0033803235 scopus 로고    scopus 로고
    • α-melanocyte-stimulating hormone in normal human physiology and disease states
    • Catania, A., Airaghi, L., Colombo, G. & Lipton, J.M. α-melanocyte-stimulating hormone in normal human physiology and disease states. Trends Endocrinol. Metab. 11, 304-308 (2000).
    • (2000) Trends Endocrinol. Metab. , vol.11 , pp. 304-308
    • Catania, A.1    Airaghi, L.2    Colombo, G.3    Lipton, J.M.4
  • 74
    • 0036804765 scopus 로고    scopus 로고
    • Melanocortin peptides and their receptors: New targets for anti-inflammatory therapy
    • Getting, S.J. Melanocortin peptides and their receptors: new targets for anti-inflammatory therapy. Trends Pharmacol. Sci. 23, 447-449 (2002).
    • (2002) Trends Pharmacol. Sci. , vol.23 , pp. 447-449
    • Getting, S.J.1
  • 75
    • 0034408112 scopus 로고    scopus 로고
    • Marshaling the anti-inflammatory influence of the neuroimmunomodulator α-MSH
    • Lipton, J.M., Catania, A. & Ichiyama, T. Marshaling the anti-inflammatory influence of the neuroimmunomodulator α-MSH. News Physiol. Sci. 15, 192-195 (2000).
    • (2000) News Physiol. Sci. , vol.15 , pp. 192-195
    • Lipton, J.M.1    Catania, A.2    Ichiyama, T.3
  • 77
    • 0032787486 scopus 로고    scopus 로고
    • UV light and MSH receptors
    • Chakraborty, A.K. et al. UV light and MSH receptors. Ann. NY Acad. Sci. 885, 100-116 (1999).
    • (1999) Ann. NY Acad. Sci. , vol.885 , pp. 100-116
    • Chakraborty, A.K.1
  • 78
    • 0030682439 scopus 로고    scopus 로고
    • Immunohistochemical characterization of HSP, α-MSH, Merkel cells and neuronal markers in acute UV dermatitis and acute contact dermatitis in vivo
    • Bayerl, C., Lauk, J., Moll, I. & Jung, E.G. Immunohistochemical characterization of HSP, α-MSH, Merkel cells and neuronal markers in acute UV dermatitis and acute contact dermatitis in vivo. Inflamm. Res. 46, 409-411 (1997).
    • (1997) Inflamm. Res. , vol.46 , pp. 409-411
    • Bayerl, C.1    Lauk, J.2    Moll, I.3    Jung, E.G.4
  • 79
    • 0038051132 scopus 로고    scopus 로고
    • New insights into the functions of α-MSH and related peptides in the immune system
    • Luger, T.A., Scholzen, T.E., Brzoska, T. & Bohm, M. New insights into the functions of α-MSH and related peptides in the immune system. Ann. NY Acad. Sci. 994, 133-140 (2003).
    • (2003) Ann. NY Acad. Sci. , vol.994 , pp. 133-140
    • Luger, T.A.1    Scholzen, T.E.2    Brzoska, T.3    Bohm, M.4
  • 80
    • 0035156142 scopus 로고    scopus 로고
    • Involvement of pro-enkephalin-derived peptides in immunity
    • Salzet, M. & Tasiemski, A. Involvement of pro-enkephalin-derived peptides in immunity. Dev. Comp. Immunol. 25, 177-185 (2001).
    • (2001) Dev. Comp. Immunol. , vol.25 , pp. 177-185
    • Salzet, M.1    Tasiemski, A.2
  • 82
    • 0028079678 scopus 로고
    • Lipopolysaccharide induces proenkephalin gene expression in rat lymph nodes and adrenal glands
    • Behar, O., Ovadia, H., Polakiewicz, R.D. & Rosen, H. Lipopolysaccharide induces proenkephalin gene expression in rat lymph nodes and adrenal glands. Endocrinology 134, 475-481 (1994).
    • (1994) Endocrinology , vol.134 , pp. 475-481
    • Behar, O.1    Ovadia, H.2    Polakiewicz, R.D.3    Rosen, H.4
  • 83
    • 0032520701 scopus 로고    scopus 로고
    • Evidence for opioid receptors on cells involved in host defense and the immune system
    • Sharp, B.M., Roy, S. & Bidlack, J.M. Evidence for opioid receptors on cells involved in host defense and the immune system. J. Neuroimmunol. 83, 45-56 (1998).
    • (1998) J. Neuroimmunol. , vol.83 , pp. 45-56
    • Sharp, B.M.1    Roy, S.2    Bidlack, J.M.3
  • 85
    • 0033305704 scopus 로고    scopus 로고
    • Evidence for functional localization of the proenkephalin-processing enzyme, prohormone thiol protease, to secretory vesicles of chromaffin cells
    • Hook, V.Y. et al. Evidence for functional localization of the proenkephalin-processing enzyme, prohormone thiol protease, to secretory vesicles of chromaffin cells. Endocrinology 140, 3744-3754 (1999).
    • (1999) Endocrinology , vol.140 , pp. 3744-3754
    • Hook, V.Y.1
  • 86
    • 0032491406 scopus 로고    scopus 로고
    • Characterization of antibacterial COOH-terminal proenkephalin-A-derived peptides (PEAP) in infectious fluids. Importance of enkelytin, the antibacterial PEAP209-237 secreted by stimulated chromaffin cells
    • Goumon, Y. et al. Characterization of antibacterial COOH-terminal proenkephalin-A-derived peptides (PEAP) in infectious fluids. Importance of enkelytin, the antibacterial PEAP209-237 secreted by stimulated chromaffin cells. J. Biol. Chem. 273, 29847-29856 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 29847-29856
    • Goumon, Y.1
  • 87
    • 0034646659 scopus 로고    scopus 로고
    • Antibacterial and antifungal activities of vasostatin-1, the N-terminal fragment of chromogranin A
    • Lugardon, K. et al. Antibacterial and antifungal activities of vasostatin-1, the N-terminal fragment of chromogranin A. J. Biol. Chem. 275, 10745-10753 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 10745-10753
    • Lugardon, K.1
  • 88
    • 0037024657 scopus 로고    scopus 로고
    • Structural and biological characterization of chromofungin, the antifungal chrornogranin A(47-66)-derived peptide
    • Lugardon, K. et al. Structural and biological characterization of chromofungin, the antifungal chrornogranin A(47-66)-derived peptide. Ann. NY Acad. Sci. 971, 359-361 (2002).
    • (2002) Ann. NY Acad. Sci. , vol.971 , pp. 359-361
    • Lugardon, K.1
  • 89
    • 85047690831 scopus 로고
    • Processing of chrornogranin B in bovine adrenal medulla. Identification of secretolytin, the endogenous C-terminal fragment of residues 614-626 with antibacterial activity
    • Strub, J.M. et al. Processing of chrornogranin B in bovine adrenal medulla. Identification of secretolytin, the endogenous C-terminal fragment of residues 614-626 with antibacterial activity. Eur. J. Biochem. 229, 356-368 (1995).
    • (1995) Eur. J. Biochem. , vol.229 , pp. 356-368
    • Strub, J.M.1
  • 90
    • 0037100533 scopus 로고    scopus 로고
    • Presence of chromogranin-derived antimicrobial peptides in plasma during coronary artery bypass surgery and evidence of an immune origin of these peptides
    • Tasiemski, A. et al. Presence of chromogranin-derived antimicrobial peptides in plasma during coronary artery bypass surgery and evidence of an immune origin of these peptides. Blood 100, 553-559 (2002).
    • (2002) Blood , vol.100 , pp. 553-559
    • Tasiemski, A.1
  • 91
    • 0028240042 scopus 로고
    • Structure, synthesis, and activity of dermaseptin b, a novel vertebrate defensive peptide from frog skin: Relationship with adenoregulin
    • Mor, A., Amiche, M. & Nicolas, P. Structure, synthesis, and activity of dermaseptin b, a novel vertebrate defensive peptide from frog skin: relationship with adenoregulin. Biochemistry 33, 6642-6650 (1994).
    • (1994) Biochemistry , vol.33 , pp. 6642-6650
    • Mor, A.1    Amiche, M.2    Nicolas, P.3
  • 92
    • 15844422471 scopus 로고    scopus 로고
    • The isolation and characterization of a novel corticostatin/defensin-like peptide from the kidney
    • Bateman, A. et al. The isolation and characterization of a novel corticostatin/defensin-like peptide from the kidney. J. Biol. Chem, 271, 10654-10659 (1996).
    • (1996) J. Biol. Chem , vol.271 , pp. 10654-10659
    • Bateman, A.1


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