메뉴 건너뛰기




Volumn 334, Issue 1, 1997, Pages 49-53

Contribution of endopeptidase 3.4.24.15 to central neurotensin inactivation

Author keywords

Analgesia; Endopeptidase 3.4.24.15; Mouse; Neurotensin; Phosphinic inhibitor

Indexed keywords

ENZYME INHIBITOR; NEUROTENSIN; PROTEINASE; THIMET OLIGOPEPTIDASE;

EID: 0030800486     PISSN: 00142999     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-2999(97)01209-0     Document Type: Article
Times cited : (38)

References (29)
  • 2
    • 0026698073 scopus 로고
    • Potent inhibition of endopeptidase 24.16 and endopeptidase 24.15 by the phosphonamide peptide N-(phenylethylphosphonyl)-Gly-L-Pro-L-aminohexanoic acid
    • Barelli H., Dive V., Yiotakis A., Vincent J.P., Checler F. Potent inhibition of endopeptidase 24.16 and endopeptidase 24.15 by the phosphonamide peptide N-(phenylethylphosphonyl)-Gly-L-Pro-L-aminohexanoic acid. Biochem. J. 287:1992;621-625.
    • (1992) Biochem. J. , vol.287 , pp. 621-625
    • Barelli, H.1    Dive, V.2    Yiotakis, A.3    Vincent, J.P.4    Checler, F.5
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-259.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-259
    • Bradford, M.M.1
  • 4
    • 0021282159 scopus 로고
    • Involvement of endo-oligopeptidases A and B in the degradation of neurotensin by rabbit brain
    • Camargo A.C.M., Almeida M.L.C., Emson P.C. Involvement of endo-oligopeptidases A and B in the degradation of neurotensin by rabbit brain. J. Neurochem. 42:1984;1758-1761.
    • (1984) J. Neurochem. , vol.42 , pp. 1758-1761
    • Camargo, A.C.M.1    Almeida, M.L.C.2    Emson, P.C.3
  • 5
    • 0027452188 scopus 로고
    • Evidence that enzymatic conversion of N-[1(R,S)-carboxy-3-phenylpropyl]-Ala-Ala-Phe-p-aminobenzoate, a specific inhibitor of endopeptidase 24.15, to N-[1(R,S)-carboxy-3-phenylpropyl]-Ala-Ala is necessary for inhibition of angiotensin-converting enzyme
    • Cardozo C., Orlowski M. Evidence that enzymatic conversion of N-[1(R,S)-carboxy-3-phenylpropyl]-Ala-Ala-Phe-p-aminobenzoate, a specific inhibitor of endopeptidase 24.15, to N-[1(R,S)-carboxy-3-phenylpropyl]-Ala-Ala is necessary for inhibition of angiotensin-converting enzyme. Peptides. 14:1993;1259-1262.
    • (1993) Peptides , vol.14 , pp. 1259-1262
    • Cardozo, C.1    Orlowski, M.2
  • 6
    • 0026451940 scopus 로고
    • Inhibition of angiotensin-converting enzyme by the metalloendopeptidase 3.4.24.15 inhibitor c-Phenylpropyl-Alanyl-Alanyl-phenylalanyl-p-aminobenzoate
    • Chappell M.C., Welches W.R., Brosnihan K.B., Ferrario C.M. Inhibition of angiotensin-converting enzyme by the metalloendopeptidase 3.4.24.15 inhibitor c-Phenylpropyl-Alanyl-Alanyl-phenylalanyl-p-aminobenzoate. Peptides. 13:1992;943-946.
    • (1992) Peptides , vol.13 , pp. 943-946
    • Chappell, M.C.1    Welches, W.R.2    Brosnihan, K.B.3    Ferrario, C.M.4
  • 7
    • 0002087037 scopus 로고
    • Neuropeptide-degrading peptidases
    • In: Nagatsu, T., Parvez, H., Naoi, M., Parvez, S. (Eds.) Elsevier Science Publishers, Amsterdam
    • Checler, F., 1993. Neuropeptide-degrading peptidases. In: Nagatsu, T., Parvez, H., Naoi, M., Parvez, S. (Eds.), Methods in Neurotransmitter and Neuropeptide Research. Part 2. vol. 11. Elsevier Science Publishers, Amsterdam, pp. 375-418.
    • (1993) Methods in Neurotransmitter and Neuropeptide Research , vol.11 , Issue.PART 2 , pp. 375-418
    • Checler, F.1
  • 9
    • 0022966470 scopus 로고
    • High affinity receptor sites and rapid proteolytic inactivation of neurotensin in primary cultured neurons
    • Checler F., Mazella J., Kitabgi P., Vincent J.P. High affinity receptor sites and rapid proteolytic inactivation of neurotensin in primary cultured neurons. J. Neurochem. 47:1986;1742-1748.
    • (1986) J. Neurochem. , vol.47 , pp. 1742-1748
    • Checler, F.1    Mazella, J.2    Kitabgi, P.3    Vincent, J.P.4
  • 10
    • 0023891243 scopus 로고
    • Neurotensin metabolism in various tissues from central and peripheral origins. Ubiquitous involvement of a novel neurotensin degrading metalloendopeptidase
    • Checler F., Barelli H., Kitabgi P., Vincent J.P. Neurotensin metabolism in various tissues from central and peripheral origins. Ubiquitous involvement of a novel neurotensin degrading metalloendopeptidase. Biochimie. 70:1988;75-82.
    • (1988) Biochimie , vol.70 , pp. 75-82
    • Checler, F.1    Barelli, H.2    Kitabgi, P.3    Vincent, J.P.4
  • 11
    • 0026099824 scopus 로고
    • Neurotensin and neuromedin N are differently metabolized in ventral tegmental area and nucleus accumbens
    • Checler F., Dauch P., Masuo Y., Vincent J.P. Neurotensin and neuromedin N are differently metabolized in ventral tegmental area and nucleus accumbens. J. Neurochem. 56:1991;1320-1328.
    • (1991) J. Neurochem. , vol.56 , pp. 1320-1328
    • Checler, F.1    Dauch, P.2    Masuo, Y.3    Vincent, J.P.4
  • 12
    • 77957790544 scopus 로고
    • Identification and distribution of endopeptidase 24.16 in the central nervous system
    • In: Conn., M.P. (Ed), Academic Press.
    • Checler, F., Dauch, P., Barelli, H., Dive, V., Masuo, Y., Vincent, B., Vincent, J.P., 1995. Identification and distribution of endopeptidase 24.16 in the central nervous system. In: Conn., M.P. (Ed), Methods in Neurosciences, vol. 23. Academic Press., pp. 363-382.
    • (1995) Methods in Neurosciences , vol.23 , pp. 363-382
    • Checler, F.1    Dauch, P.2    Barelli, H.3    Dive, V.4    Masuo, Y.5    Vincent, B.6    Vincent, J.P.7
  • 13
    • 0021285834 scopus 로고
    • Active site directed N-carboxymethyl peptide inhibitors of a soluble metalloendopeptidase from rat brain
    • Chu T.G., Orlowski M. Active site directed N-carboxymethyl peptide inhibitors of a soluble metalloendopeptidase from rat brain. Biochemistry. 23:1984;3598-3603.
    • (1984) Biochemistry , vol.23 , pp. 3598-3603
    • Chu, T.G.1    Orlowski, M.2
  • 15
    • 0023932837 scopus 로고
    • Potentiation by thiorphan and bestatin of the naloxone-insensitive analgesic effects of neurotensin and neuromedin N
    • Coquerel A., Dubuc I., Kitabgi P., Costentin P. Potentiation by thiorphan and bestatin of the naloxone-insensitive analgesic effects of neurotensin and neuromedin N. Neurochem. Int. 12:1988;361-366.
    • (1988) Neurochem. Int. , vol.12 , pp. 361-366
    • Coquerel, A.1    Dubuc, I.2    Kitabgi, P.3    Costentin, P.4
  • 16
    • 0028892366 scopus 로고
    • Molecular cloning and expression of rat brain endopeptidase 3.4.24.16
    • Dauch P., Vincent J.P., Checler F. Molecular cloning and expression of rat brain endopeptidase 3.4.24.16. J. Biol. Chem. 270:1995;27266-27271.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27266-27271
    • Dauch, P.1    Vincent, J.P.2    Checler, F.3
  • 17
    • 0026512238 scopus 로고
    • Specificity of neurotensin metabolism by regional rat brain slices
    • Davis T.P., Gillespie T.J., Konings P.N.M. Specificity of neurotensin metabolism by regional rat brain slices. J. Neurochem. 58:1992;608-617.
    • (1992) J. Neurochem. , vol.58 , pp. 608-617
    • Davis, T.P.1    Gillespie, T.J.2    Konings, P.N.M.3
  • 18
    • 84935383230 scopus 로고
    • Synthetic analgesics (II): Dithienylbutenyl and dithienylbutylamines
    • Eddy N.B., Leimblach D. Synthetic analgesics (II): Dithienylbutenyl and dithienylbutylamines. J. Pharmacol. Exp. Ther. 107:1953;385-393.
    • (1953) J. Pharmacol. Exp. Ther. , vol.107 , pp. 385-393
    • Eddy, N.B.1    Leimblach, D.2
  • 19
    • 0029155961 scopus 로고
    • Development of highly potent and selective phosphinic peptide inhibitors of zinc endopeptidase 24.15 using combinatorial chemistry
    • Jiràcek J., Yiotakis A., Vincent B., Lecoq A., Nicolaou A., Checler F., Dive V. Development of highly potent and selective phosphinic peptide inhibitors of zinc endopeptidase 24.15 using combinatorial chemistry. J. Biol. Chem. 270:1995;21701-21706.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21701-21706
    • Jiràcek, J.1    Yiotakis, A.2    Vincent, B.3    Lecoq, A.4    Nicolaou, A.5    Checler, F.6    Dive, V.7
  • 20
    • 0029741201 scopus 로고    scopus 로고
    • Development of the first potent and selective inhibitor iof the zinc-endopeptidase 3.4.24.16 using a systematic approach based on combinatorial chemistry of phosphinic peptides
    • Jiràcek J., Yiotakis A., Vincent B., Checler F., Dive V. Development of the first potent and selective inhibitor iof the zinc-endopeptidase 3.4.24.16 using a systematic approach based on combinatorial chemistry of phosphinic peptides. J. Biol. Chem. 271:1996;19606-19611.
    • (1996) J. Biol. Chem. , vol.271 , pp. 19606-19611
    • Jiràcek, J.1    Yiotakis, A.2    Vincent, B.3    Checler, F.4    Dive, V.5
  • 21
    • 0026722326 scopus 로고
    • Effects of thiorphan, bestatin and a novel metallopeptidase inhibitor JMV 390-1 on the recovery of neurotensin and neuromedin N released from mouse hypothalamus
    • Kitabgi P., Dubuc I., Nouel D., Costentin J., Cuber J.-C., Fulcrand H., Doulut S., Rodriguez M., Martinez J. Effects of thiorphan, bestatin and a novel metallopeptidase inhibitor JMV 390-1 on the recovery of neurotensin and neuromedin N released from mouse hypothalamus. Neurosci. Lett. 142:1992;200-204.
    • (1992) Neurosci. Lett. , vol.142 , pp. 200-204
    • Kitabgi, P.1    Dubuc, I.2    Nouel, D.3    Costentin, J.4    Cuber, J.-C.5    Fulcrand, H.6    Doulut, S.7    Rodriguez, M.8    Martinez, J.9
  • 22
    • 0026039410 scopus 로고
    • Structure/function relationships in the inhibition of thimet oligopeptidase by carboxyphenylpropyl-peptides
    • Knight G., Barrett A.J. Structure/function relationships in the inhibition of thimet oligopeptidase by carboxyphenylpropyl-peptides. FEBS Lett. 294:1991;183-186.
    • (1991) FEBS Lett. , vol.294 , pp. 183-186
    • Knight, G.1    Barrett, A.J.2
  • 24
    • 0023871927 scopus 로고
    • Substrate-related potent inhibitors of brain metalloendopeptidase
    • Orlowski M., Michaud C., Molineaux C.J. Substrate-related potent inhibitors of brain metalloendopeptidase. Biochemistry. 27:1988;597-602.
    • (1988) Biochemistry , vol.27 , pp. 597-602
    • Orlowski, M.1    Michaud, C.2    Molineaux, C.J.3
  • 25
    • 0025966563 scopus 로고
    • Analgesic responses elicited by endogenous enkephalins (protected by mixed peptidase inhibitors) in a variety of morphine-sensitive noxious tests
    • Schmidt C., Peyroux J., Noble F., Fournié-Zaluski M.C., Roques B.P. Analgesic responses elicited by endogenous enkephalins (protected by mixed peptidase inhibitors) in a variety of morphine-sensitive noxious tests. Eur. J. Pharmacol. 192:1991;253-262.
    • (1991) Eur. J. Pharmacol. , vol.192 , pp. 253-262
    • Schmidt, C.1    Peyroux, J.2    Noble, F.3    Fournié-Zaluski, M.C.4    Roques, B.P.5
  • 26
    • 0029119487 scopus 로고
    • Phosphorus-containing peptides as mixed inhibitors of endopeptidase 3.4.24.15 and 3.4.24.16: Effect on neurotensin degradation in vitro and in vivo
    • Vincent B., Dive V., Yiotakis A., Smadja C., Maldonado R., Vincent J.P., Checler F. Phosphorus-containing peptides as mixed inhibitors of endopeptidase 3.4.24.15 and 3.4.24.16: Effect on neurotensin degradation in vitro and in vivo. Br. J. Pharmacol. 115:1995;1053-1063.
    • (1995) Br. J. Pharmacol. , vol.115 , pp. 1053-1063
    • Vincent, B.1    Dive, V.2    Yiotakis, A.3    Smadja, C.4    Maldonado, R.5    Vincent, J.P.6    Checler, F.7
  • 27
    • 0030958889 scopus 로고    scopus 로고
    • A novel selective and potent phosphinic peptide inhibitor of endopeptidase 3.4.24.16: Effect on neurotensin-induced analgesia and neuronal inactivation
    • Vincent B., Jiracek J., Noble F., Loog M., Roques B., Dive V., Vincent J.P., Checler F. A novel selective and potent phosphinic peptide inhibitor of endopeptidase 3.4.24.16: Effect on neurotensin-induced analgesia and neuronal inactivation. Br. J. Pharmacol. 121:1997;705-710.
    • (1997) Br. J. Pharmacol. , vol.121 , pp. 705-710
    • Vincent, B.1    Jiracek, J.2    Noble, F.3    Loog, M.4    Roques, B.5    Dive, V.6    Vincent, J.P.7    Checler, F.8
  • 28
    • 0027359062 scopus 로고
    • Endopeptidase 3.4.24.11 converts N-1(R,S)-carboxy-3-phenylpropyl-Ala-Ala-Phe-p-carboxyanilide into a potent inhibitor of angiotensin-converting enzyme
    • Williams C.H., Yamamoto T., Walsh D., Allsop D. Endopeptidase 3.4.24.11 converts N-1(R,S)-carboxy-3-phenylpropyl-Ala-Ala-Phe-p-carboxyanilide into a potent inhibitor of angiotensin-converting enzyme. Biochem. J. 294:1993;681-684.
    • (1993) Biochem. J. , vol.294 , pp. 681-684
    • Williams, C.H.1    Yamamoto, T.2    Walsh, D.3    Allsop, D.4
  • 29
    • 0029821713 scopus 로고    scopus 로고
    • Protection of hydroxyphosphinyl function of phosphinic dipeptides by adamantyl. Application to the solid-phase synthesis of phosphinic peptides
    • Yiotakis A., Vassilou S., Jiracek J., Dive V. Protection of hydroxyphosphinyl function of phosphinic dipeptides by adamantyl. Application to the solid-phase synthesis of phosphinic peptides. J. Org. Chem. 61:1996;6601-6605.
    • (1996) J. Org. Chem. , vol.61 , pp. 6601-6605
    • Yiotakis, A.1    Vassilou, S.2    Jiracek, J.3    Dive, V.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.