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Volumn 47, Issue 4, 1999, Pages 447-461

Cellular distribution of endothelin-converting enzyme-1 in human tissues

Author keywords

Endothelin converting enzyme; Human; Immunocytochemistry; In situ hybridization

Indexed keywords

COMPLEMENTARY RNA; ENDOTHELIN; ENDOTHELIN CONVERTING ENZYME; ENDOTHELIN CONVERTING ENZYME INHIBITOR; MESSENGER RNA;

EID: 0032932090     PISSN: 00221554     EISSN: None     Source Type: Journal    
DOI: 10.1177/002215549904700403     Document Type: Article
Times cited : (80)

References (52)
  • 1
    • 0028609612 scopus 로고
    • Interaction of endothelin-3 with endothelin-B receptor is essential for development of epidermal melanocytes and enteric neurons
    • Baynash A, Hosoda K, Giaid A, Richardson J, Emoto N, Hammer R, Yanagisawa M (1994) Interaction of endothelin-3 with endothelin-B receptor is essential for development of epidermal melanocytes and enteric neurons. Cell 79:1277-1285
    • (1994) Cell , vol.79 , pp. 1277-1285
    • Baynash, A.1    Hosoda, K.2    Giaid, A.3    Richardson, J.4    Emoto, N.5    Hammer, R.6    Yanagisawa, M.7
  • 2
    • 0030938927 scopus 로고    scopus 로고
    • Pex/PEX tissue distribution and evidence for a deletion in the 3' region of the Pex gene in X-linked hypophosphatemic mice
    • Beck L, Soumounou Y, Martel J, Krishnamurthy G, Gauthier C, Goodyer C, Tenenhouse H (1997) Pex/PEX tissue distribution and evidence for a deletion in the 3' region of the Pex gene in X-linked hypophosphatemic mice. J Clin Invest 99:1200-1209
    • (1997) J Clin Invest , vol.99 , pp. 1200-1209
    • Beck, L.1    Soumounou, Y.2    Martel, J.3    Krishnamurthy, G.4    Gauthier, C.5    Goodyer, C.6    Tenenhouse, H.7
  • 3
    • 0028233457 scopus 로고
    • In vitro autoradiographic demonstration of endothelin-1 binding sites in the human adrenal cortex
    • Belloni A, Rossi G, Zanin L, Prayer-Galetti T, Pessina A, Nussdorfer G (1994) In vitro autoradiographic demonstration of endothelin-1 binding sites in the human adrenal cortex. Biomed Res 15:95-99
    • (1994) Biomed Res , vol.15 , pp. 95-99
    • Belloni, A.1    Rossi, G.2    Zanin, L.3    Prayer-Galetti, T.4    Pessina, A.5    Nussdorfer, G.6
  • 4
    • 0031055668 scopus 로고    scopus 로고
    • Immunohistochemical double staining of microwave enhanced and nonenhanced nuclear and cytoplasmic antigens
    • Bohle R, Bonczkowitz M, Altmannsberger H, Schulz A (1997) Immunohistochemical double staining of microwave enhanced and nonenhanced nuclear and cytoplasmic antigens. Biotech Histochem 72:10-15
    • (1997) Biotech Histochem , vol.72 , pp. 10-15
    • Bohle, R.1    Bonczkowitz, M.2    Altmannsberger, H.3    Schulz, A.4
  • 6
    • 0029805923 scopus 로고    scopus 로고
    • Differential distribution of endothelin peptides and receptors in human adrenal glands
    • Davenport A, Hoskins S, Kuc R, Plumpton C (1996) Differential distribution of endothelin peptides and receptors in human adrenal glands. Histochem J 28:779-789
    • (1996) Histochem J , vol.28 , pp. 779-789
    • Davenport, A.1    Hoskins, S.2    Kuc, R.3    Plumpton, C.4
  • 7
    • 0029017876 scopus 로고
    • Endothelin-converting enzyme-2 is a membrane-bound, phosphoramidon-sensitive metalloprotease with acidic pH optimum
    • Emoto N, Yanagisawa M (1995) Endothelin-converting enzyme-2 is a membrane-bound, phosphoramidon-sensitive metalloprotease with acidic pH optimum. J Biol Chem 270:15262-15268
    • (1995) J Biol Chem , vol.270 , pp. 15262-15268
    • Emoto, N.1    Yanagisawa, M.2
  • 8
    • 0029315859 scopus 로고
    • Do developing enteric neurons need endothelins?
    • Gershon MD (1995) Do developing enteric neurons need endothelins? Curr Biol 5:601-604
    • (1995) Curr Biol , vol.5 , pp. 601-604
    • Gershon, M.D.1
  • 9
    • 0024318340 scopus 로고
    • Endothelin is a potent mitogen for rat vascular smooth muscle cells
    • Hirata Y, Takagi Y, Fukuda Y, Marumo F (1989) Endothelin is a potent mitogen for rat vascular smooth muscle cells. Atherosclerosis 78:225-228
    • (1989) Atherosclerosis , vol.78 , pp. 225-228
    • Hirata, Y.1    Takagi, Y.2    Fukuda, Y.3    Marumo, F.4
  • 10
    • 0030700341 scopus 로고    scopus 로고
    • Novel activity of endothelin-converting enzyme: Hydrolysis of bradykinin
    • Hoang M, Turner A (1997) Novel activity of endothelin-converting enzyme: hydrolysis of bradykinin. Biochem J 327:23-26
    • (1997) Biochem J , vol.327 , pp. 23-26
    • Hoang, M.1    Turner, A.2
  • 11
    • 0028639196 scopus 로고
    • Targeted and natural (piebald-lethal) mutations of endothelin-B receptor gene produce megacolon associated with spotted coat color in mice
    • Hosoda K, Hammer R, Richardson J, Baynash A, Cheung J, Yanagisawa M (1994) Targeted and natural (piebald-lethal) mutations of endothelin-B receptor gene produce megacolon associated with spotted coat color in mice. Cell 79:1267-1276
    • (1994) Cell , vol.79 , pp. 1267-1276
    • Hosoda, K.1    Hammer, R.2    Richardson, J.3    Baynash, A.4    Cheung, J.5    Yanagisawa, M.6
  • 12
    • 0025025088 scopus 로고
    • Phosphoramidon, a metalloproteinase inhibitor, suppresses the secretion of endothelin-1 from cultured endothelial cells by inhibiting a big endothelin-1 converting enzyme
    • Ikegawa R, Matsumura Y, Tsukahara Y, Takaoka M, Morimoto S (1990) Phosphoramidon, a metalloproteinase inhibitor, suppresses the secretion of endothelin-1 from cultured endothelial cells by inhibiting a big endothelin-1 converting enzyme. Biochem Biophys Res Commun 171:669-675
    • (1990) Biochem Biophys Res Commun , vol.171 , pp. 669-675
    • Ikegawa, R.1    Matsumura, Y.2    Tsukahara, Y.3    Takaoka, M.4    Morimoto, S.5
  • 14
    • 0024553103 scopus 로고
    • Putative precursors of endothelin have less vasoconstrictor activity in vitro but a potent pressor effect
    • Kashiwabara T, Inagaki Y, Ohta H, Iwamatsu A, Nomizu M, Nishikori K (1989) Putative precursors of endothelin have less vasoconstrictor activity in vitro but a potent pressor effect. FEBS Lett 247:73-76
    • (1989) FEBS Lett , vol.247 , pp. 73-76
    • Kashiwabara, T.1    Inagaki, Y.2    Ohta, H.3    Iwamatsu, A.4    Nomizu, M.5    Nishikori, K.6
  • 15
    • 0027164625 scopus 로고
    • Endothelins as regulators of growth and function in endocrine tissues
    • Kennedy R, Haynes W, Webb D (1993) Endothelins as regulators of growth and function in endocrine tissues. Clin Endocrinol 39:259-265
    • (1993) Clin Endocrinol , vol.39 , pp. 259-265
    • Kennedy, R.1    Haynes, W.2    Webb, D.3
  • 16
    • 0024521522 scopus 로고
    • Conversion of big endothelin-1 to 21-residue endothelin-1 is essential for expression of full vasoconstrictor activity: Structure-activity relationships of big endothelin-1
    • Kimura S, Kaysuya Y, Sawamura T, Shinmi O, Sugita Y, Yanagisawa M, Goto K, Masaki T (1989) Conversion of big endothelin-1 to 21-residue endothelin-1 is essential for expression of full vasoconstrictor activity: structure-activity relationships of big endothelin-1. J Cardiovasc Pharmacol 13:S5-7
    • (1989) J Cardiovasc Pharmacol , vol.13
    • Kimura, S.1    Kaysuya, Y.2    Sawamura, T.3    Shinmi, O.4    Sugita, Y.5    Yanagisawa, M.6    Goto, K.7    Masaki, T.8
  • 17
    • 0023765634 scopus 로고
    • Endothelin stimulates c-fos and c-myc expression and proliferation of vascular smooth muscle cells
    • Komuro I, Kurihara H, Sugiyama I, Yoshizumi M, Takaku F, Yazaki Y (1988) Endothelin stimulates c-fos and c-myc expression and proliferation of vascular smooth muscle cells. FEBS Lett 238:249-252
    • (1988) FEBS Lett , vol.238 , pp. 249-252
    • Komuro, I.1    Kurihara, H.2    Sugiyama, I.3    Yoshizumi, M.4    Takaku, F.5    Yazaki, Y.6
  • 18
    • 0030859683 scopus 로고    scopus 로고
    • Construction, expression and characterization of a soluble form of human endothelin-converting enzyme
    • Korth P, Egidy G, Parnot C, LeMoullec JM, Corvol P, Pinet F (1997) Construction, expression and characterization of a soluble form of human endothelin-converting enzyme. FEBS Lett 417:365-370
    • (1997) FEBS Lett , vol.417 , pp. 365-370
    • Korth, P.1    Egidy, G.2    Parnot, C.3    LeMoullec, J.M.4    Corvol, P.5    Pinet, F.6
  • 21
    • 0030799481 scopus 로고    scopus 로고
    • Prevention and reversal vasospasm by an endothelin-converting enzyme inhibitor, CGS 26303, in an experimental model of subarachnoid hemorrhage
    • Kwan A, Bavhek M, Jeng A, Maniara W, Toyoda T, Lappe R, Kassell N, Lee K (1997) Prevention and reversal vasospasm by an endothelin-converting enzyme inhibitor, CGS 26303, in an experimental model of subarachnoid hemorrhage. J Neurosurg 87: 281-286
    • (1997) J Neurosurg , vol.87 , pp. 281-286
    • Kwan, A.1    Bavhek, M.2    Jeng, A.3    Maniara, W.4    Toyoda, T.5    Lappe, R.6    Kassell, N.7    Lee, K.8
  • 22
    • 0025779323 scopus 로고
    • Molecular cloning and primary structure of Kell blood group protein
    • Lee S, Zambas E, Marsh W, Redman C (1991) Molecular cloning and primary structure of Kell blood group protein. Proc Natl Acad Sci USA 88:6353-6357
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 6353-6357
    • Lee, S.1    Zambas, E.2    Marsh, W.3    Redman, C.4
  • 26
    • 0023868637 scopus 로고
    • Molecular cloning and aminoacid sequence of human enkephalinase (neutral endopeptidase)
    • Malfroy B, Kuang W, Seedburg P, Mason A, Schofield P (1988) Molecular cloning and aminoacid sequence of human enkephalinase (neutral endopeptidase). FEBS Lett 229:206-210
    • (1988) FEBS Lett , vol.229 , pp. 206-210
    • Malfroy, B.1    Kuang, W.2    Seedburg, P.3    Mason, A.4    Schofield, P.5
  • 28
    • 0028987867 scopus 로고
    • Possible role of endothelin in endothelial regulation of vascular tone
    • Masaki T (1995) Possible role of endothelin in endothelial regulation of vascular tone. Annu Rev Pharmacol Toxicol 35:235-255
    • (1995) Annu Rev Pharmacol Toxicol , vol.35 , pp. 235-255
    • Masaki, T.1
  • 29
    • 0026077104 scopus 로고
    • Molecular and cellular mechanism of endothelin regulation: Implications for vascular function
    • Masaki T, Kimura S, Yanagisawa M, Goto K (1991) Molecular and cellular mechanism of endothelin regulation: implications for vascular function. Circulation 84:1457-1468
    • (1991) Circulation , vol.84 , pp. 1457-1468
    • Masaki, T.1    Kimura, S.2    Yanagisawa, M.3    Goto, K.4
  • 30
    • 0030913098 scopus 로고    scopus 로고
    • Endothelins stimulate deoxyribonucleic acid synthesis and cell proliferation in rat adrenal zona glomerulosa, acting through an endothelin A receptor coupled with protein kinase C- and tyrosine kinase-dependent signalling pathways
    • Mazzochi G, Rossi G, Rebuffat P, Malendowicz L, Markowska A, Nussdorfer G (1997) Endothelins stimulate deoxyribonucleic acid synthesis and cell proliferation in rat adrenal zona glomerulosa, acting through an endothelin A receptor coupled with protein kinase C- and tyrosine kinase-dependent signalling pathways. Endocrinology 138:2333-2337
    • (1997) Endocrinology , vol.138 , pp. 2333-2337
    • Mazzochi, G.1    Rossi, G.2    Rebuffat, P.3    Malendowicz, L.4    Markowska, A.5    Nussdorfer, G.6
  • 31
    • 0025975337 scopus 로고
    • Phosphoramidon blocks the pressor activity of porcine big endothelin-1-(1-39) in vivo and conversion of big endothelin-1-1-39-to endothelin-1-(1-21) in vitro
    • McMahon E, Palomo M, Moore W, McDonald J, Stern M (1991) Phosphoramidon blocks the pressor activity of porcine big endothelin-1-(1-39) in vivo and conversion of big endothelin-1-(1-39-to endothelin-1-(1-21) in vitro. Proc Natl Acad Sci USA 88:703-707
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 703-707
    • McMahon, E.1    Palomo, M.2    Moore, W.3    McDonald, J.4    Stern, M.5
  • 36
    • 0027475050 scopus 로고
    • Neutral endopeptidase 24.11: Structure, inhibition, and experimental and clinical pharmacology
    • Roques B, Noble F, Dauge V, Fournie-Zaluski M, Beaumont A (1993) Neutral endopeptidase 24.11: structure, inhibition, and experimental and clinical pharmacology. Pharmacol Rev 45:87-146
    • (1993) Pharmacol Rev , vol.45 , pp. 87-146
    • Roques, B.1    Noble, F.2    Dauge, V.3    Fournie-Zaluski, M.4    Beaumont, A.5
  • 41
    • 0028792143 scopus 로고
    • Enhancement of mRNA in situ hybridization signal by microwave heating
    • Sibony M, Commo F, Callard P, Gasc J (1995) Enhancement of mRNA in situ hybridization signal by microwave heating. Lab Invest 73:586-591
    • (1995) Lab Invest , vol.73 , pp. 586-591
    • Sibony, M.1    Commo, F.2    Callard, P.3    Gasc, J.4
  • 43
    • 0027454492 scopus 로고
    • Purification and characterization of endothelin-converting enzyme from rat lung
    • Takahashi M, Matsushita Y, Iijima Y, Tanzawa K (1993) Purification and characterization of endothelin-converting enzyme from rat lung. J Biol Chem 268:21394-21398
    • (1993) J Biol Chem , vol.268 , pp. 21394-21398
    • Takahashi, M.1    Matsushita, Y.2    Iijima, Y.3    Tanzawa, K.4
  • 44
    • 0029160578 scopus 로고
    • A gene (PEX) with homologies to endopeptidases is mutated in patients with X-linked hypophosphataemic rickets
    • The HYP Consortium (1995) A gene (PEX) with homologies to endopeptidases is mutated in patients with X-linked hypophosphataemic rickets. Nature Genet 11:130-136
    • (1995) Nature Genet , vol.11 , pp. 130-136
  • 45
    • 0030899822 scopus 로고    scopus 로고
    • Mammalian membrane metallopetidases: NEP, ECE, Kell and PEX
    • Turner A, Tanzawa K (1997) Mammalian membrane metallopetidases: NEP, ECE, Kell and PEX. FASEB J 11:355-364
    • (1997) FASEB J , vol.11 , pp. 355-364
    • Turner, A.1    Tanzawa, K.2
  • 46
    • 0029585975 scopus 로고
    • Organization of the gene encoding the human endothelin-converting enzyme (ECE-1)
    • Valdenaire O, Rohrbacher E, Mattei M (1995) Organization of the gene encoding the human endothelin-converting enzyme (ECE-1). J Biol Chem 270:29794-29798
    • (1995) J Biol Chem , vol.270 , pp. 29794-29798
    • Valdenaire, O.1    Rohrbacher, E.2    Mattei, M.3
  • 47
    • 0028778055 scopus 로고
    • A matter of life and breath
    • VanHoutte P (1994) A matter of life and breath. Nature 368:693-694
    • (1994) Nature , vol.368 , pp. 693-694
    • Vanhoutte, P.1
  • 49
    • 0027992642 scopus 로고
    • ECE-1: A membrane-bound metalloprotease that catalyzes the proteolytic activation of big endothelin-1
    • Xu D, Emoto N, Giad A, Slaughter C, Kaw S, deWit D, Yanagisawa M (1994) ECE-1: a membrane-bound metalloprotease that catalyzes the proteolytic activation of big endothelin-1. Cell 78:473-485
    • (1994) Cell , vol.78 , pp. 473-485
    • Xu, D.1    Emoto, N.2    Giad, A.3    Slaughter, C.4    Kaw, S.5    DeWit, D.6    Yanagisawa, M.7
  • 51
    • 0024465081 scopus 로고
    • Molecular biology and biochemistry of the endothelins
    • Yanagisawa M, Masaki T (1989) Molecular biology and biochemistry of the endothelins. Trends Pharmacol Sci 10:374-378
    • (1989) Trends Pharmacol Sci , vol.10 , pp. 374-378
    • Yanagisawa, M.1    Masaki, T.2
  • 52
    • 0031940499 scopus 로고    scopus 로고
    • Dual genetic pathways of endothelin-mediated intercellular signalling revealed by targeted disruption of endorhelin converting enzyme-1 gene
    • Yanagisawa H, Yanagisawa M, Kapur R, Richardson J, Williams S, Clouthier D, deWit D, Emoto N, Hammer R (1998) Dual genetic pathways of endothelin-mediated intercellular signalling revealed by targeted disruption of endorhelin converting enzyme-1 gene. Development 125:825-836
    • (1998) Development , vol.125 , pp. 825-836
    • Yanagisawa, H.1    Yanagisawa, M.2    Kapur, R.3    Richardson, J.4    Williams, S.5    Clouthier, D.6    DeWit, D.7    Emoto, N.8    Hammer, R.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.