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Volumn 326, Issue 1, 2008, Pages 24-32

Kinin B2 receptor-mediated bradykinin internalization and metalloendopeptidase EP24.15-dependent intracellular bradykinin degradation

Author keywords

[No Author keywords available]

Indexed keywords

BETA 2 ADRENERGIC RECEPTOR; BRADYKININ; CALCIUM ION; METALLOPROTEINASE; MOLECULAR MARKER; PHOSPHATIDYLINOSITIDE; THIMET OLIGOPEPTIDASE; BRADYKININ B2 RECEPTOR;

EID: 45749091327     PISSN: 00223565     EISSN: 15210103     Source Type: Journal    
DOI: 10.1124/jpet.108.136911     Document Type: Article
Times cited : (10)

References (37)
  • 2
    • 16244373008 scopus 로고    scopus 로고
    • 14-3-3 Epsilon modulates the stimulated secretion of endopeptidase 24.15
    • Carreño FR, Goñi CN, Castro LM, and Ferro ES (2005) 14-3-3 Epsilon modulates the stimulated secretion of endopeptidase 24.15. J Neurochem 93:10-25.
    • (2005) J Neurochem , vol.93 , pp. 10-25
    • Carreño, F.R.1    Goñi, C.N.2    Castro, L.M.3    Ferro, E.S.4
  • 3
    • 33845601598 scopus 로고    scopus 로고
    • Human ACE and bradykinin B2 receptors form a complex at the plasma membrane
    • Chen Z, Deddish PA, Minshall RD, Becker RP, Erdös EG, Tan F (2006) Human ACE and bradykinin B2 receptors form a complex at the plasma membrane. FASEB J 20:2261-2270.
    • (2006) FASEB J , vol.20 , pp. 2261-2270
    • Chen, Z.1    Deddish, P.A.2    Minshall, R.D.3    Becker, R.P.4    Erdös, E.G.5    Tan, F.6
  • 4
    • 0033600514 scopus 로고    scopus 로고
    • The association of metalloendopeptidase EC 3.4.24.15 at the extracellular surface of the AtT-20 cell plasma membrane
    • Crack PJ, Wu TJ, Cummins PM, Ferro ES, Tullai JW, Glucksman MJ, and Roberts JL (1999) The association of metalloendopeptidase EC 3.4.24.15 at the extracellular surface of the AtT-20 cell plasma membrane. Brain Res 835:113-124.
    • (1999) Brain Res , vol.835 , pp. 113-124
    • Crack, P.J.1    Wu, T.J.2    Cummins, P.M.3    Ferro, E.S.4    Tullai, J.W.5    Glucksman, M.J.6    Roberts, J.L.7
  • 5
    • 0026585412 scopus 로고
    • Endopeptidase 24.15 modulates bradykinin-induced contraction in guinea-pig trachea
    • Da Silva A, Dhuy J, Waeldele F, Bertrand C, and Landry Y (1992) Endopeptidase 24.15 modulates bradykinin-induced contraction in guinea-pig trachea. Eur J Pharmacol 212:97-99.
    • (1992) Eur J Pharmacol , vol.212 , pp. 97-99
    • Da Silva, A.1    Dhuy, J.2    Waeldele, F.3    Bertrand, C.4    Landry, Y.5
  • 6
    • 0025997928 scopus 로고
    • Specific inhibition of endopeptidase 24.16 by dipeptides
    • Dauch P, Vincent J-P, and Checler F (1991) Specific inhibition of endopeptidase 24.16 by dipeptides. Eur J Biochem 202:269-276.
    • (1991) Eur J Biochem , vol.202 , pp. 269-276
    • Dauch, P.1    Vincent, J.-P.2    Checler, F.3
  • 7
    • 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 WFC and Leeb-Lundberg LMF (1997) Bradykinin sequesters B2 bradykinin receptors and the receptor-coupled Galpha subunits Galphaq and Galphai in caveolae in DDT1 MF-2 smooth muscle cells. J Biol Chem 272:17858-17866.
    • (1997) J Biol Chem , vol.272 , pp. 17858-17866
    • de Weerd, W.F.C.1    Leeb-Lundberg, L.M.F.2
  • 8
    • 0031038233 scopus 로고    scopus 로고
    • Degradation of bradykinin by bovine tracheal epithelium and isolated epithelial cells
    • Dendorfer A, Vordermark D, and Dominiak P (1997) Degradation of bradykinin by bovine tracheal epithelium and isolated epithelial cells. Br J Pharmacol 120:121-129.
    • (1997) Br J Pharmacol , vol.120 , pp. 121-129
    • Dendorfer, A.1    Vordermark, D.2    Dominiak, P.3
  • 10
    • 0032524670 scopus 로고    scopus 로고
    • A single position in the third transmembrane domains of the human B1 and B2 bradykinin receptors is adjacent to and discriminates between the C-terminal residues of subtype-selective ligands
    • Fathy D, Mathis SA, Leeb T, and Leeb-Lundberg LMF (1998) A single position in the third transmembrane domains of the human B1 and B2 bradykinin receptors is adjacent to and discriminates between the C-terminal residues of subtype-selective ligands. J Biol Chem 273:12210-12218.
    • (1998) J Biol Chem , vol.273 , pp. 12210-12218
    • Fathy, D.1    Mathis, S.A.2    Leeb, T.3    Leeb-Lundberg, L.M.F.4
  • 12
    • 8644245895 scopus 로고    scopus 로고
    • Intracellular peptides as putative natural regulators of protein interactions
    • Ferro ES, Hyslop S, and Camargo ACM (2004) Intracellular peptides as putative natural regulators of protein interactions. J Neurochem 91:769-777.
    • (2004) J Neurochem , vol.91 , pp. 769-777
    • Ferro, E.S.1    Hyslop, S.2    Camargo, A.C.M.3
  • 13
    • 0031956450 scopus 로고    scopus 로고
    • Agonist-induced redistribution of bradykinin B2 receptor in caveolae
    • Haasemann M, Cartaud J, Müller-Esterl W, and Dunia I (1998) Agonist-induced redistribution of bradykinin B2 receptor in caveolae. J Cell Sci 111:917-928.
    • (1998) J Cell Sci , vol.111 , pp. 917-928
    • Haasemann, M.1    Cartaud, J.2    Müller-Esterl, W.3    Dunia, I.4
  • 15
    • 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, and Roberts JL (2004) Metalloendopeptidase EC3.4.24.15 is constitutively released from the exofacial leaflet of lipid rafts in GT1-7 cells. J Neurochem 90:819-828.
    • (2004) J Neurochem , vol.90 , pp. 819-828
    • Jeske, N.A.1    Glucksman, M.J.2    Roberts, J.L.3
  • 17
    • 0036070769 scopus 로고    scopus 로고
    • Negative and positive regulatory epitopes in the C-terminal domains of the human B1 and B2 bradykinin receptor subtypes determine receptor coupling efficacy to G(q/11)-mediated phospholipase Cβ activity
    • Kang DS and Leeb-Lundberg LMF (2002) Negative and positive regulatory epitopes in the C-terminal domains of the human B1 and B2 bradykinin receptor subtypes determine receptor coupling efficacy to G(q/11)-mediated phospholipase Cβ activity. Mol Pharmacol 62:281-288.
    • (2002) Mol Pharmacol , vol.62 , pp. 281-288
    • Kang, D.S.1    Leeb-Lundberg, L.M.F.2
  • 18
    • 0141974949 scopus 로고    scopus 로고
    • Regulation of cell-surface major histocompatibility complex class I expression by the endopeptidase EC3.4.24.15 (thimet oligopeptidase)
    • Kim SI, Pabon A, Swanson TA, and Glucksman MJ (2003) Regulation of cell-surface major histocompatibility complex class I expression by the endopeptidase EC3.4.24.15 (thimet oligopeptidase). Biochem J 375:111-120.
    • (2003) Biochem J , vol.375 , pp. 111-120
    • Kim, S.I.1    Pabon, A.2    Swanson, T.A.3    Glucksman, M.J.4
  • 19
    • 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, and Leeb-Lundberg LMF (2002) Human B1 and B2 bradykinin receptors and their agonists target caveolae-related lipid rafts to different degrees in HEK293 cells. Biochemistry 41:14340-14347.
    • (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.F.5
  • 20
    • 0025324527 scopus 로고
    • Guanine nucleotide regulation of B2 kinin receptor binding: Time-dependent formation of a guanine nucleotide-sensitive receptor state from which [3H]bradykinin dissociates slowly
    • Leeb-Lundberg LMF and Mathis SA (1990) Guanine nucleotide regulation of B2 kinin receptor binding: time-dependent formation of a guanine nucleotide-sensitive receptor state from which [3H]bradykinin dissociates slowly. J Biol Chem 265:9621-9627.
    • (1990) J Biol Chem , vol.265 , pp. 9621-9627
    • Leeb-Lundberg, L.M.F.1    Mathis, S.A.2
  • 21
    • 14144251086 scopus 로고    scopus 로고
    • International union of pharmacology. XLV. Classification of the kinin receptor family: From molecular mechanisms to pathophysiological consequences
    • Leeb-Lundberg LMF, Marceau F, Müller-Esterl F, Pettibone DJ, and Zuraw BL (2005) International union of pharmacology. XLV. Classification of the kinin receptor family: from molecular mechanisms to pathophysiological consequences. Pharmacol Rev 57:27-77.
    • (2005) Pharmacol Rev , vol.57 , pp. 27-77
    • Leeb-Lundberg, L.M.F.1    Marceau, F.2    Müller-Esterl, F.3    Pettibone, D.J.4    Zuraw, B.L.5
  • 22
    • 0031027029 scopus 로고    scopus 로고
    • The sixth transmembrane domains of the human B1 and B2 bradykinin receptors are structurally compatible and involved in discriminating between subtype-selective agonists
    • Leeb T, Mathis SA, and Leeb-Lundberg LMF (1997) The sixth transmembrane domains of the human B1 and B2 bradykinin receptors are structurally compatible and involved in discriminating between subtype-selective agonists. J Biol Chem 272:311-317.
    • (1997) J Biol Chem , vol.272 , pp. 311-317
    • Leeb, T.1    Mathis, S.A.2    Leeb-Lundberg, L.M.F.3
  • 24
    • 0026531241 scopus 로고
    • Receptor-mediated internalization of bradykinin. DDT1 MF-2 smooth muscle cells process internalized bradykinin via multiple degradative pathways
    • Munoz CM and Leeb-Lundberg LMF (1992) Receptor-mediated internalization of bradykinin. DDT1 MF-2 smooth muscle cells process internalized bradykinin via multiple degradative pathways. J Biol Chem 267:303-309.
    • (1992) J Biol Chem , vol.267 , pp. 303-309
    • Munoz, C.M.1    Leeb-Lundberg, L.M.F.2
  • 25
    • 0037686697 scopus 로고    scopus 로고
    • Metalloendopeptidases EC 3.4.24.15/16 regulate bradykinin activity in the cerebral microvasculature
    • H1942-H1948
    • Norman MU, Lew RA, Smith AI, and Hickey MJ (2003) Metalloendopeptidases EC 3.4.24.15/16 regulate bradykinin activity in the cerebral microvasculature. Am J Physiol Heart Circ Physiol 284:H1942-H1948.
    • (2003) Am J Physiol Heart Circ Physiol , vol.284
    • Norman, M.U.1    Lew, R.A.2    Smith, A.I.3    Hickey, M.J.4
  • 27
    • 0024406166 scopus 로고
    • Endopeptidase 24.15 from rat testes. Isolation of the enzyme and its specificity toward synthetic and natural peptidase, including enkephalin-containing peptides
    • Orlowski M, Reznik S, Ayala J, and Pierotti AR (1989) Endopeptidase 24.15 from rat testes. Isolation of the enzyme and its specificity toward synthetic and natural peptidase, including enkephalin-containing peptides. Biochem J 261:951-958.
    • (1989) Biochem J , vol.261 , pp. 951-958
    • Orlowski, M.1    Reznik, S.2    Ayala, J.3    Pierotti, A.R.4
  • 29
    • 0027377170 scopus 로고
    • Modulatory effect of endopeptidase inhibitors on bradykinin-induced contraction of rat uterus
    • Schriefer JA and Molineaux CJ (1993) Modulatory effect of endopeptidase inhibitors on bradykinin-induced contraction of rat uterus. J Pharmacol Exp Ther 266:700-706.
    • (1993) J Pharmacol Exp Ther , vol.266 , pp. 700-706
    • Schriefer, J.A.1    Molineaux, C.J.2
  • 30
    • 18844457567 scopus 로고    scopus 로고
    • EP24.15 interacts with the angiotensin II type I receptor and bradykinin B2 receptor
    • Shivakumar BR, Wang Z, Hammond TG, and Harriset RC (2005) EP24.15 interacts with the angiotensin II type I receptor and bradykinin B2 receptor. Cell Biochem Funct 23:195-204.
    • (2005) Cell Biochem Funct , vol.23 , pp. 195-204
    • Shivakumar, B.R.1    Wang, Z.2    Hammond, T.G.3    Harriset, R.C.4
  • 31
    • 0036799813 scopus 로고    scopus 로고
    • Soluble metalloendopeptidases and neuroendocrine signaling
    • Shrimpton CN, Smith AI, and Lew RA (2002) Soluble metalloendopeptidases and neuroendocrine signaling. Endocr Rev 23:647-664.
    • (2002) Endocr Rev , vol.23 , pp. 647-664
    • Shrimpton, C.N.1    Smith, A.I.2    Lew, R.A.3
  • 33
    • 0027051024 scopus 로고
    • Bradykinin-degrading enzymes: Structure, function, distribution, and potential roles in cardiovascular pharmacology
    • Skidgel RA (1992) Bradykinin-degrading enzymes: structure, function, distribution, and potential roles in cardiovascular pharmacology. J Cardiovasc Pharmacol 20:S4-S9.
    • (1992) J Cardiovasc Pharmacol , vol.20
    • Skidgel, R.A.1
  • 34
    • 0033952163 scopus 로고    scopus 로고
    • Smith AI, Lew RA, Shrimpton CN, Evans RG, and 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.
    • Smith AI, Lew RA, Shrimpton CN, Evans RG, and 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.
  • 35
    • 0027082698 scopus 로고
    • Bradykinin binding to B2 kinin receptors and stimulation of phosphoinositide turnover and arachidonic acid release in primary cultures of cells from the late pregnant myometrium
    • Tropea MM, Munoz CM, and Leeb-Lundberg LMF (1992) Bradykinin binding to B2 kinin receptors and stimulation of phosphoinositide turnover and arachidonic acid release in primary cultures of cells from the late pregnant myometrium. Can J Physiol Pharmacol 70:1360-1371.
    • (1992) Can J Physiol Pharmacol , vol.70 , pp. 1360-1371
    • Tropea, M.M.1    Munoz, C.M.2    Leeb-Lundberg, L.M.F.3
  • 36
    • 0033789728 scopus 로고    scopus 로고
    • Degradation of bradykinin by peritoneal and alveolar macrophages of the guinea pig
    • Vietinghoff G and Paegelow I (2000) Degradation of bradykinin by peritoneal and alveolar macrophages of the guinea pig. Peptides 21:1249-1255.
    • (2000) Peptides , vol.21 , pp. 1249-1255
    • Vietinghoff, G.1    Paegelow, I.2


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