메뉴 건너뛰기




Volumn 97, Issue 1, 2006, Pages 13-21

Modulation of bradykinin signaling by EP24.15 and EP24.16 in cultured trigeminal ganglia

Author keywords

Bradykinin; Lipid raft; Microdomain; Trigeminal

Indexed keywords

AMINOBENZOIC ACID DERIVATIVE; BRADYKININ; BRADYKININ B2 RECEPTOR; INOSITOL PHOSPHATE; NEUROLYSIN; PROTEIN KINASE B; THIMET OLIGOPEPTIDASE;

EID: 33644934747     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2006.03706.x     Document Type: Article
Times cited : (30)

References (40)
  • 1
    • 0034681369 scopus 로고    scopus 로고
    • Differential regulation of the phosphatidylinositol 3-kinase/Akt and p70, S6 kinase pathways by the alpha (1A)-adrenergic receptor in rat-1 fibroblasts
    • Ballou LM. Cross ME. Huang S. McReynolds EM. Zhang BX. Lin RZ. 2000 Differential regulation of the phosphatidylinositol 3-kinase/Akt and p70, S6 kinase pathways by the alpha (1A)-adrenergic receptor in rat-1 fibroblasts JBiolChem 275 4803 4809
    • (2000) JBiolChem , vol.275 , pp. 4803-4809
    • Ballou, L.M.1    Cross, M.E.2    Huang, S.3    McReynolds, E.M.4    Zhang, B.X.5    Lin, R.Z.6
  • 2
    • 0038268664 scopus 로고    scopus 로고
    • Activated G alpha q inhibits p110 alpha phosphatidylinositol 3-kinase and Akt
    • Ballou LM. Lin HY. Fan G. Jiang YP. Lin RZ. 2003 Activated G alpha q inhibits p110 alpha phosphatidylinositol 3-kinase and Akt JBiolChem 278 23 472 23 479
    • (2003) JBiolChem , vol.278 , pp. 23472-23479
    • Ballou, L.M.1    Lin, H.Y.2    Fan, G.3    Jiang, Y.P.4    Lin, R.Z.5
  • 4
    • 0034624060 scopus 로고    scopus 로고
    • Dual regulation of Akt/protein kinase B by heterotrimeric G protein subunits
    • Bommakanti RK. Vinayak S. Simonds WF. 2000 Dual regulation of Akt/protein kinase B by heterotrimeric G protein subunits JBiolChem 275 38 870 38 876
    • (2000) JBiolChem , vol.275 , pp. 38870-38876
    • Bommakanti, R.K.1    Vinayak, S.2    Simonds, W.F.3
  • 5
    • 0032527642 scopus 로고    scopus 로고
    • Structure and origin of ordered lipid domains in biological membranes
    • Brown DA. London E. 1998 Structure and origin of ordered lipid domains in biological membranes JMembr Biol 164 103 114
    • (1998) JMembr Biol , vol.164 , pp. 103-114
    • Brown, D.A.1    London, E.2
  • 6
    • 0034625373 scopus 로고    scopus 로고
    • Structure and function of sphingolipid- and cholesterol-rich membrane rafts
    • Brown DA. London E. 2000 Structure and function of sphingolipid- and cholesterol-rich membrane rafts JBiolChem 275 17221 17224
    • (2000) JBiolChem , vol.275 , pp. 17221-17224
    • Brown, D.A.1    London, E.2
  • 7
    • 0023891243 scopus 로고
    • Neurotensin metabolism in various tissues of central and peripheral origins: Ubiquitous involvement of a novel neurotensin degrading metalloendopeptidase
    • Checler F. Barelli H. Kitabgi P. Vincent JP. 1988 Neurotensin metabolism in various tissues of central and peripheral origins: ubiquitous involvement of a novel neurotensin degrading metalloendopeptidase Biochimie 70 75 82
    • (1988) Biochimie , vol.70 , pp. 75-82
    • Checler, F.1    Barelli, H.2    Kitabgi, P.3    Vincent, J.P.4
  • 8
    • 0021285834 scopus 로고
    • Active site directed N-carboxymethyl peptide inhibitors of a soluble metalloendopeptidase from rat brain
    • Chu TG. Orlowski M. 1984 Active site directed N-carboxymethyl peptide inhibitors of a soluble metalloendopeptidase from rat brain Biochemistry 23 3598 3603
    • (1984) Biochemistry , vol.23 , pp. 3598-3603
    • Chu, T.G.1    Orlowski, M.2
  • 9
    • 0021860568 scopus 로고
    • Soluble metalloendopeptidase from rat brain: Action on enkephalin- containing peptides and other bioactive peptides
    • Chu TG. Orlowski M. 1985 Soluble metalloendopeptidase from rat brain: action on enkephalin- containing peptides and other bioactive peptides Endocrinology 116 1418 1425
    • (1985) Endocrinology , vol.116 , pp. 1418-1425
    • Chu, T.G.1    Orlowski, M.2
  • 10
    • 0033523012 scopus 로고    scopus 로고
    • Zinc coordination and substrate catalysis within the neuropeptide processing enzyme endopeptidase EC 3.4.24.15. Identification of active site histidine and glutamate residues
    • Cummins PM. Pabon A. Margulies EH. Glucksman MJ. 1999 Zinc coordination and substrate catalysis within the neuropeptide processing enzyme endopeptidase EC 3.4.24.15. Identification of active site histidine and glutamate residues JBiolChem 274 16 003 16 009
    • (1999) JBiolChem , vol.274 , pp. 16003-16009
    • Cummins, P.M.1    Pabon, A.2    Margulies, E.H.3    Glucksman, M.J.4
  • 11
    • 0025997928 scopus 로고
    • Specific inhibition of endopeptidase 24.16 by dipeptides
    • Dauch P. Vincent JP. Checler F. 1991 Specific inhibition of endopeptidase 24.16 by dipeptides Eur JBiochem 202 269 276
    • (1991) Eur JBiochem , vol.202 , pp. 269-276
    • Dauch, P.1    Vincent, J.P.2    Checler, F.3
  • 12
    • 0028892366 scopus 로고
    • Molecular cloning and expression of rat brain endopeptidase 3.4.24.16
    • Dauch P. Vincent JP. Checler F. 1995 Molecular cloning and expression of rat brain endopeptidase 3.4.24.16 JBiolChem 270 27 266 27 271
    • (1995) JBiolChem , vol.270 , pp. 27266-27271
    • Dauch, P.1    Vincent, J.P.2    Checler, F.3
  • 15
    • 0003502036 scopus 로고
    • McGraw-Hill New York
    • Fields HL. 1987 Pain McGraw-Hill New York
    • (1987) Pain
    • Fields, H.L.1
  • 16
    • 0035943423 scopus 로고    scopus 로고
    • Emerging themes in lipid rafts and caveolae
    • Galbiati F. Razani B. Lisanti MP. 2001 Emerging themes in lipid rafts and caveolae Cell 106 403 411
    • (2001) Cell , vol.106 , pp. 403-411
    • Galbiati, F.1    Razani, B.2    Lisanti, M.P.3
  • 17
    • 0031013519 scopus 로고    scopus 로고
    • Bradykinin receptors
    • Hall JM. 1997 Bradykinin receptors General Pharmacol 28 1 6
    • (1997) General Pharmacol , vol.28 , pp. 1-6
    • Hall, J.M.1
  • 18
    • 0033584964 scopus 로고    scopus 로고
    • Endothelin-1-induced GLUT4 translocation is mediated via Galpha (q/11) protein and phosphatidylinositol 3-kinase in 3T3-L1 adipocytes
    • Imamura T. Ishibashi K. Dalle S. Ugi S. Olefsky JM. 1999a Endothelin-1-induced GLUT4 translocation is mediated via Galpha (q/11) protein and phosphatidylinositol 3-kinase in 3T3-L1 adipocytes JBiolChem 274 33 691 33 695
    • (1999) JBiolChem , vol.274 , pp. 33691-33695
    • Imamura, T.1    Ishibashi, K.2    Dalle, S.3    Ugi, S.4    Olefsky, J.M.5
  • 21
    • 4143066846 scopus 로고    scopus 로고
    • Metalloendopeptidase EC3.4.24.15 is constitutively released from the exofacial leaflet of lipid rafts in GT1-7 cells
    • Jeske NA. Glucksman MJ. Roberts JL. 2004 Metalloendopeptidase EC3.4.24.15 is constitutively released from the exofacial leaflet of lipid rafts in GT1-7 cells JNeurochem 90 819 828
    • (2004) JNeurochem , vol.90 , pp. 819-828
    • Jeske, N.A.1    Glucksman, M.J.2    Roberts, J.L.3
  • 22
    • 0034629391 scopus 로고    scopus 로고
    • The trimeric GTP-binding protein (G (q) /g (11) alpha subunit is required for insulin-stimulated GLUT4 translocation in 3T3L1 adipocytes
    • Kanzaki M. Watson RT. Artemyev NO. Pessin JE. 2000 The trimeric GTP-binding protein (G (q) /G (11) alpha subunit is required for insulin-stimulated GLUT4 translocation in 3T3L1 adipocytes JBiolChem 275 7167 7175
    • (2000) JBiolChem , vol.275 , pp. 7167-7175
    • Kanzaki, M.1    Watson, R.T.2    Artemyev, N.O.3    Pessin, J.E.4
  • 23
    • 0032559854 scopus 로고    scopus 로고
    • Cholesterol is required for surface transport of influenza virus hemagglutinin
    • Keller P. Simons K. 1998 Cholesterol is required for surface transport of influenza virus hemagglutinin JCell Biol 140 1357 1367
    • (1998) JCell Biol , vol.140 , pp. 1357-1367
    • Keller, P.1    Simons, K.2
  • 24
    • 0023877289 scopus 로고
    • Bradykinin stimulates a rise in cytosolic calcium in renal glomerular mesangial cells via a pertussis toxin insensitive pathway
    • Kremer S. Harper P. Hegele R. Skorecki K. 1988 Bradykinin stimulates a rise in cytosolic calcium in renal glomerular mesangial cells via a pertussis toxin insensitive pathway Can JPhysiolPharmacol 66 43 48
    • (1988) Can JPhysiolPharmacol , vol.66 , pp. 43-48
    • Kremer, S.1    Harper, P.2    Hegele, R.3    Skorecki, K.4
  • 25
    • 2242478438 scopus 로고    scopus 로고
    • Human B1 and B2 bradykinin receptors and their agonists target caveolae-related lipid rafts to different degrees in HEK293 cells
    • Lamb ME. Zhang C. Shea T. Kyle DJ. Leeb-Lundberg LM. 2002 Human B1 and B2 bradykinin receptors and their agonists target caveolae-related lipid rafts to different degrees in HEK293 cells Biochemistry 41 14 340 14 347
    • (2002) Biochemistry , vol.41 , pp. 14340-14347
    • Lamb, M.E.1    Zhang, C.2    Shea, T.3    Kyle, D.J.4    Leeb-Lundberg, L.M.5
  • 26
    • 0031795591 scopus 로고    scopus 로고
    • Identification of reggie-1 and reggie-2 as plasmamembrane-associated proteins which cocluster with activated GPI-anchored cell adhesion molecules in non-caveolar micropatches in neurons
    • Lang DM. Lommel S. Jung M. Ankerhold R. Petrausch B. Laessing U. Wiechers MF. Plattner H. Stuermer CA. 1998 Identification of reggie-1 and reggie-2 as plasmamembrane-associated proteins which cocluster with activated GPI-anchored cell adhesion molecules in non-caveolar micropatches in neurons JNeurobiol 37 502 523
    • (1998) JNeurobiol , vol.37 , pp. 502-523
    • Lang, D.M.1    Lommel, S.2    Jung, M.3    Ankerhold, R.4    Petrausch, B.5    Laessing, U.6    Wiechers, M.F.7    Plattner, H.8    Stuermer, C.A.9
  • 28
    • 0034695484 scopus 로고    scopus 로고
    • Lipid-dependent targeting of G proteins into rafts
    • Moffett S. Brown DA. Linder ME. 2000 Lipid-dependent targeting of G proteins into rafts JBiolChem 275 2191 2198
    • (2000) JBiolChem , vol.275 , pp. 2191-2198
    • Moffett, S.1    Brown, D.A.2    Linder, M.E.3
  • 29
    • 0032497830 scopus 로고    scopus 로고
    • Molecular cloning and expression of rat bradykinin B1 receptor
    • Ni A. Chai KX. Chao L. Chao J. 1998 Molecular cloning and expression of rat bradykinin B1 receptor BiochimBiophysActa 1442 177 185
    • (1998) BiochimBiophysActa , vol.1442 , pp. 177-185
    • Ni, A.1    Chai, K.X.2    Chao, L.3    Chao, J.4
  • 30
    • 0020824984 scopus 로고
    • A soluble metalloendopeptidase from rat brain. Purification of the enzyme and determination of specificity with synthetic and natural peptides
    • Orlowski M. Michaud C. Chu TG. 1983 A soluble metalloendopeptidase from rat brain. Purification of the enzyme and determination of specificity with synthetic and natural peptides Eur JBiochem 135 81 88
    • (1983) Eur JBiochem , vol.135 , pp. 81-88
    • Orlowski, M.1    Michaud, C.2    Chu, T.G.3
  • 31
    • 0027479821 scopus 로고
    • Evolutionary families of peptidases
    • Rawlings ND. Barrett AJ. 1993 Evolutionary families of peptidases BiochemJ 290 205 218
    • (1993) BiochemJ , vol.290 , pp. 205-218
    • Rawlings, N.D.1    Barrett, A.J.2
  • 33
    • 0033952163 scopus 로고    scopus 로고
    • A novel stable inhibitor of endopeptidases EC 3.4.24.15 and 3.4.24.16 potentiates bradykinin-induced hypotension
    • Smith AI. Lew RA. Shrimpton CN. Evans RG. Abbenante G. 2000 A novel stable inhibitor of endopeptidases EC 3.4.24.15 and 3.4.24.16 potentiates bradykinin-induced hypotension Hypertension 35 626 630
    • (2000) Hypertension , vol.35 , pp. 626-630
    • Smith, A.I.1    Lew, R.A.2    Shrimpton, C.N.3    Evans, R.G.4    Abbenante, G.5
  • 35
    • 0035171631 scopus 로고    scopus 로고
    • Glycosylphosphatidyl inositol-anchored proteins and fyn kinase assemble in noncaveolar plasma membrane microdomains defined by reggie-1 and - 2
    • Stuermer CA. Lang DM. Kirsch F. Wiechers M. Deininger SO. Plattner H. 2001 Glycosylphosphatidyl inositol-anchored proteins and fyn kinase assemble in noncaveolar plasma membrane microdomains defined by reggie-1 and - 2 Mol BiolCell 12 3031 3045
    • (2001) Mol BiolCell , vol.12 , pp. 3031-3045
    • Stuermer, C.A.1    Lang, D.M.2    Kirsch, F.3    Wiechers, M.4    Deininger, S.O.5    Plattner, H.6
  • 37
    • 0029781361 scopus 로고    scopus 로고
    • Distinct properties of neuronal and astrocytic endopeptidase 3.4.24.16: A study on differentiation, subcellular distribution, and secretion processes
    • Vincent B. Beaudet A. Dauch P. Vincent JP. Checler F. 1996 Distinct properties of neuronal and astrocytic endopeptidase 3.4.24.16: a study on differentiation, subcellular distribution, and secretion processes JNeurosci 16 5049 5059
    • (1996) JNeurosci , vol.16 , pp. 5049-5059
    • Vincent, B.1    Beaudet, A.2    Dauch, P.3    Vincent, J.P.4    Checler, F.5
  • 38
    • 0031023969 scopus 로고    scopus 로고
    • Stably transfected human cells overexpressing rat brain endopeptidase 3.4.24.16: Biochemical characterization of the activity and expression of soluble and membrane-associated counterparts
    • Vincent B. Dauch P. Vincent JP. Checler F. 1997 Stably transfected human cells overexpressing rat brain endopeptidase 3.4.24.16: biochemical characterization of the activity and expression of soluble and membrane-associated counterparts JNeurochem 68 837 845
    • (1997) JNeurochem , vol.68 , pp. 837-845
    • Vincent, B.1    Dauch, P.2    Vincent, J.P.3    Checler, F.4
  • 39
    • 0030757027 scopus 로고    scopus 로고
    • Bradykinin sequesters B2 bradykinin receptors and the receptor-coupled Galpha subunits Galphaq and Galphai in caveolae in DDT1 MF-2 smooth muscle cells
    • de Weerd WF. Leeb-Lundberg LM. 1997 Bradykinin sequesters B2 bradykinin receptors and the receptor-coupled Galpha subunits Galphaq and Galphai in caveolae in DDT1 MF-2 smooth muscle cells JBiolChem 272 17 858 17 866
    • (1997) JBiolChem , vol.272 , pp. 17858-17866
    • De Weerd, W.F.1    Leeb-Lundberg, L.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.