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Volumn 167, Issue 2, 2008, Pages 229-236

Immunocapture-based fluorometric assay for the measurement of neprilysin-specific enzyme activity in brain tissue homogenates and cerebrospinal fluid

Author keywords

Cerebrospinal fluid; Fluorogenic substrate; Immunocapture; Neprilysin; Thiorphan

Indexed keywords

ANTIBODY; MEMBRANE METALLOENDOPEPTIDASE; NEPRILYSIN ANTIBODY; PEPTIDE; THIORPHAN; UNCLASSIFIED DRUG;

EID: 37049011221     PISSN: 01650270     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jneumeth.2007.08.012     Document Type: Article
Times cited : (42)

References (31)
  • 1
    • 33744957126 scopus 로고    scopus 로고
    • CGS 35601, a triple inhibitor of angiotensin converting enzyme, neutral endopeptidase and endothelin converting enzyme
    • Battistini B., Daull P., and Jeng A.Y. CGS 35601, a triple inhibitor of angiotensin converting enzyme, neutral endopeptidase and endothelin converting enzyme. Cardiovasc Drug Rev 23 (2005) 317-330
    • (2005) Cardiovasc Drug Rev , vol.23 , pp. 317-330
    • Battistini, B.1    Daull, P.2    Jeng, A.Y.3
  • 2
    • 0036077536 scopus 로고    scopus 로고
    • Beta-amyloid catabolism: roles for neprilysin (NEP) and other metallopeptidases?
    • Carson J.A., and Turner A.J. Beta-amyloid catabolism: roles for neprilysin (NEP) and other metallopeptidases?. J Neurochem 81 (2002) 1-8
    • (2002) J Neurochem , vol.81 , pp. 1-8
    • Carson, J.A.1    Turner, A.J.2
  • 3
    • 0029977203 scopus 로고    scopus 로고
    • A highly selective assay for neutral endopeptidase based on the cleavage of a fluorogenic substrate related to Leu-enkephalin
    • Carvalho K.M., Boileau G., Camargo A.C., and Juliano L. A highly selective assay for neutral endopeptidase based on the cleavage of a fluorogenic substrate related to Leu-enkephalin. Anal Biochem 237 (1996) 167-173
    • (1996) Anal Biochem , vol.237 , pp. 167-173
    • Carvalho, K.M.1    Boileau, G.2    Camargo, A.C.3    Juliano, L.4
  • 4
    • 33748790706 scopus 로고    scopus 로고
    • Assembly and selective "in synthesis" labeling of quenched fluorogenic protease substrates
    • Chersi A., Ferracuti S., Falasca G., Butler R.H., and Fruci D. Assembly and selective "in synthesis" labeling of quenched fluorogenic protease substrates. Anal Biochem 357 (2006) 194-199
    • (2006) Anal Biochem , vol.357 , pp. 194-199
    • Chersi, A.1    Ferracuti, S.2    Falasca, G.3    Butler, R.H.4    Fruci, D.5
  • 6
    • 0033766102 scopus 로고    scopus 로고
    • Inhibitor potencies and substrate preference for endothelin-converting enzyme-1 are dramatically affected by pH
    • Fahnoe D.C., Knapp J., Johnson G.D., and Ahn K. Inhibitor potencies and substrate preference for endothelin-converting enzyme-1 are dramatically affected by pH. J Cardiovasc Pharmacol 36 (2000) S22-S25
    • (2000) J Cardiovasc Pharmacol , vol.36
    • Fahnoe, D.C.1    Knapp, J.2    Johnson, G.D.3    Ahn, K.4
  • 7
    • 0028180544 scopus 로고
    • Dns-Gly-(p-NO2)Phe-beta Ala, a specific fluorogenic substrate for neutral endopeptidase 24111
    • Goudreau N., Guis C., Soleilhac J.M., and Roques B.P. Dns-Gly-(p-NO2)Phe-beta Ala, a specific fluorogenic substrate for neutral endopeptidase 24111. Anal Biochem 219 (1994) 87-95
    • (1994) Anal Biochem , vol.219 , pp. 87-95
    • Goudreau, N.1    Guis, C.2    Soleilhac, J.M.3    Roques, B.P.4
  • 8
    • 0030995506 scopus 로고    scopus 로고
    • Suppression of substance P biosynthesis in sensory neurons of dorsal root ganglion by prodrug esters of potent peptidylglycine alpha-amidating monooxygenase inhibitors
    • Jeng A.Y., Fujimoto R.A., Chou M., Tan J., and Erion M.D. Suppression of substance P biosynthesis in sensory neurons of dorsal root ganglion by prodrug esters of potent peptidylglycine alpha-amidating monooxygenase inhibitors. J Biol Chem 272 (1997) 14666-14671
    • (1997) J Biol Chem , vol.272 , pp. 14666-14671
    • Jeng, A.Y.1    Fujimoto, R.A.2    Chou, M.3    Tan, J.4    Erion, M.D.5
  • 9
    • 0034327279 scopus 로고    scopus 로고
    • Development of an internally quenched fluorescent substrate selective for endothelin-converting enzyme-1
    • Johnson G.D., and Ahn K. Development of an internally quenched fluorescent substrate selective for endothelin-converting enzyme-1. Anal Biochem 286 (2000) 112-118
    • (2000) Anal Biochem , vol.286 , pp. 112-118
    • Johnson, G.D.1    Ahn, K.2
  • 10
    • 21644462358 scopus 로고    scopus 로고
    • Development of a solid-phase assay for analysis of matrix metalloproteinase activity
    • Lauer-Fields J.L., Nagase H., and Fields G.B. Development of a solid-phase assay for analysis of matrix metalloproteinase activity. J Biomol Tech 15 (2004) 305-316
    • (2004) J Biomol Tech , vol.15 , pp. 305-316
    • Lauer-Fields, J.L.1    Nagase, H.2    Fields, G.B.3
  • 11
    • 0033646276 scopus 로고    scopus 로고
    • Endothelin-converting enzyme inhibitors: current status and perspectives
    • Loffler B.M. Endothelin-converting enzyme inhibitors: current status and perspectives. J Cardiovasc Pharmacol 35 (2000) S79-S82
    • (2000) J Cardiovasc Pharmacol , vol.35
    • Loffler, B.M.1
  • 12
    • 33749475139 scopus 로고    scopus 로고
    • Decreased expression and activity of neprilysin in Alzheimer disease are associated with cerebral amyloid angiopathy
    • Miners J.S., Van Helmond Z., Chalmers K., Wilcock G., Love S., and Kehoe P.G. Decreased expression and activity of neprilysin in Alzheimer disease are associated with cerebral amyloid angiopathy. J Neuropathol Exp Neurol 65 (2006) 1012-1021
    • (2006) J Neuropathol Exp Neurol , vol.65 , pp. 1012-1021
    • Miners, J.S.1    Van Helmond, Z.2    Chalmers, K.3    Wilcock, G.4    Love, S.5    Kehoe, P.G.6
  • 14
    • 0038013935 scopus 로고    scopus 로고
    • Characterization of endothelin-converting enzyme-2.Implication for a role in the nonclassical processing of regulatory peptides
    • Mzhavia N., Pan H., Che F.Y., Fricker L.D., and Devi L.A. Characterization of endothelin-converting enzyme-2.Implication for a role in the nonclassical processing of regulatory peptides. J Biol Chem 278 (2003) 14704-14711
    • (2003) J Biol Chem , vol.278 , pp. 14704-14711
    • Mzhavia, N.1    Pan, H.2    Che, F.Y.3    Fricker, L.D.4    Devi, L.A.5
  • 16
    • 0035872886 scopus 로고    scopus 로고
    • Selective neurotensin-derived internally quenched fluorogenic substrates for neurolysin (EC 3.4. 24. 16): comparison with thimet oligopeptidase (EC 3. 4. 24. 15) and neprilysin (EC 3. 4. 24. 11)
    • Oliveira V., Campos M., Hemerly J.P., Ferro E.S., Camargo A.C., Juliano M.A., and Juliano L. Selective neurotensin-derived internally quenched fluorogenic substrates for neurolysin (EC 3.4. 24. 16): comparison with thimet oligopeptidase (EC 3. 4. 24. 15) and neprilysin (EC 3. 4. 24. 11). Anal Biochem 292 (2001) 257-265
    • (2001) Anal Biochem , vol.292 , pp. 257-265
    • Oliveira, V.1    Campos, M.2    Hemerly, J.P.3    Ferro, E.S.4    Camargo, A.C.5    Juliano, M.A.6    Juliano, L.7
  • 18
    • 24944538873 scopus 로고    scopus 로고
    • Vasopeptidase inhibition for blood pressure control: emerging experience
    • Quaschning T. Vasopeptidase inhibition for blood pressure control: emerging experience. Curr Pharm Des 11 (2005) 3293-3299
    • (2005) Curr Pharm Des , vol.11 , pp. 3293-3299
    • Quaschning, T.1
  • 19
    • 0032729644 scopus 로고    scopus 로고
    • Characterization of a kinin inactivating serine endopeptidase H2 (kininase) from human urine using fluorogenic substrates
    • Quinto B.M., Juliano L., Juliano M., Carmona A.K., Stella R.C., and Casarini D.E. Characterization of a kinin inactivating serine endopeptidase H2 (kininase) from human urine using fluorogenic substrates. Immunopharmacology 45 (1999) 223-228
    • (1999) Immunopharmacology , vol.45 , pp. 223-228
    • Quinto, B.M.1    Juliano, L.2    Juliano, M.3    Carmona, A.K.4    Stella, R.C.5    Casarini, D.E.6
  • 20
    • 0034530754 scopus 로고    scopus 로고
    • Characterization of a prolyl endopeptidase (kininase) from human urine using fluorogenic quenched substrates
    • Quinto B.M., Juliano M.A., Hirata I., Carmona A.K., Juliano L., and Casarini D.E. Characterization of a prolyl endopeptidase (kininase) from human urine using fluorogenic quenched substrates. Int J Biochem Cell Biol 32 (2000) 1161-1172
    • (2000) Int J Biochem Cell Biol , vol.32 , pp. 1161-1172
    • Quinto, B.M.1    Juliano, M.A.2    Hirata, I.3    Carmona, A.K.4    Juliano, L.5    Casarini, D.E.6
  • 21
    • 2942627719 scopus 로고    scopus 로고
    • Specificity comparison of a serine endopeptidase (SH1) and a serine thiol endopeptidase (STH2) purified from human urine
    • Quinto B.M., Juliano M.A., Hirata I., Carmona A.K., Juliano L., and Casarini D.E. Specificity comparison of a serine endopeptidase (SH1) and a serine thiol endopeptidase (STH2) purified from human urine. Int J Biochem Cell Biol 36 (2004) 1933-1944
    • (2004) Int J Biochem Cell Biol , vol.36 , pp. 1933-1944
    • Quinto, B.M.1    Juliano, M.A.2    Hirata, I.3    Carmona, A.K.4    Juliano, L.5    Casarini, D.E.6
  • 22
    • 19544365690 scopus 로고    scopus 로고
    • Flexibility in substrate recognition by thimet oligopeptidase as revealed by denaturation studies
    • Sigman J.A., Patwa T.H., Tablante A.V., Joseph C.D., Glucksman M.J., and Wolfson A.J. Flexibility in substrate recognition by thimet oligopeptidase as revealed by denaturation studies. Biochem J 388 (2005) 255-261
    • (2005) Biochem J , vol.388 , pp. 255-261
    • Sigman, J.A.1    Patwa, T.H.2    Tablante, A.V.3    Joseph, C.D.4    Glucksman, M.J.5    Wolfson, A.J.6
  • 23
    • 22744448900 scopus 로고    scopus 로고
    • Involvement of neutral endopeptidase in neoplastic progression
    • Sumitomo M., Shen R., and Nanus D.M. Involvement of neutral endopeptidase in neoplastic progression. Biochim Biophys Acta 1751 (2005) 52-59
    • (2005) Biochim Biophys Acta , vol.1751 , pp. 52-59
    • Sumitomo, M.1    Shen, R.2    Nanus, D.M.3
  • 24
    • 0142042450 scopus 로고    scopus 로고
    • Dual ACE and neutral endopeptidase inhibitors: novel therapy for patients with cardiovascular disorders
    • Tabrizchi R. Dual ACE and neutral endopeptidase inhibitors: novel therapy for patients with cardiovascular disorders. Drugs 63 (2003) 2185-2202
    • (2003) Drugs , vol.63 , pp. 2185-2202
    • Tabrizchi, R.1
  • 26
    • 0038201945 scopus 로고    scopus 로고
    • Exploring the structure and function of zinc metallopeptidases: old enzymes and new discoveries
    • Turner A.J. Exploring the structure and function of zinc metallopeptidases: old enzymes and new discoveries. Biochem Soc Trans 31 (2003) 723-727
    • (2003) Biochem Soc Trans , vol.31 , pp. 723-727
    • Turner, A.J.1
  • 28
    • 0035112440 scopus 로고    scopus 로고
    • The neprilysin (NEP) family of zinc metalloendopeptidases: genomics and function
    • Turner A.J., Isaac R.E., and Coates D. The neprilysin (NEP) family of zinc metalloendopeptidases: genomics and function. Bioessays 23 (2001) 261-269
    • (2001) Bioessays , vol.23 , pp. 261-269
    • Turner, A.J.1    Isaac, R.E.2    Coates, D.3
  • 29
    • 0030899822 scopus 로고    scopus 로고
    • Mammalian membrane metallopeptidases: NEP, ECE, KELL, and PEX
    • Turner A.J., and Tanzawa K. Mammalian membrane metallopeptidases: NEP, ECE, KELL, and PEX. FASEB J 11 (1997) 355-364
    • (1997) FASEB J , vol.11 , pp. 355-364
    • Turner, A.J.1    Tanzawa, K.2
  • 30
    • 26244462301 scopus 로고    scopus 로고
    • Proteolytic mechanisms in amyloid-beta metabolism: therapeutic implications for Alzheimer's disease
    • Vardy E.R., Catto A.J., and Hooper N.M. Proteolytic mechanisms in amyloid-beta metabolism: therapeutic implications for Alzheimer's disease. Trends Mol Med 11 (2005) 464-472
    • (2005) Trends Mol Med , vol.11 , pp. 464-472
    • Vardy, E.R.1    Catto, A.J.2    Hooper, N.M.3


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