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Volumn 17, Issue 4, 1996, Pages 601-607

The in vivo metabolism of cholecystokinin (CCK-8) is essentially ensured by aminopeptidase A

Author keywords

Aminopeptidase A; CCK 8; Cholecystokinin; Cortex; Degradation; EC 33 (3 amino 4 thio butyl sulfonate); Hippocampus; In vivo binding assay; K+ evoked release; Mouse; Peptidase inhibitors; Rat

Indexed keywords

AMINOPEPTIDASE; CHOLECYSTOKININ; CHOLECYSTOKININ RECEPTOR; EC 33; ENZYME INHIBITOR; PROTEINASE INHIBITOR; UNCLASSIFIED DRUG;

EID: 0029978990     PISSN: 01969781     EISSN: None     Source Type: Journal    
DOI: 10.1016/0196-9781(96)00036-8     Document Type: Article
Times cited : (57)

References (47)
  • 1
    • 0026567796 scopus 로고
    • Opioid control of the in vitro release of cholecystokinin-like material from the rat substantia nigra
    • 1. Benoliel, J. J.; Mauborgne, A.; Bourgoin, S.; Legrand, J. C.; Hamon, M.; Cesselin, F. Opioid control of the in vitro release of cholecystokinin-like material from the rat substantia nigra. J. Neurochem. 58:916-922; 1992.
    • (1992) J. Neurochem. , vol.58 , pp. 916-922
    • Benoliel, J.J.1    Mauborgne, A.2    Bourgoin, S.3    Legrand, J.C.4    Hamon, M.5    Cesselin, F.6
  • 3
    • 0028237882 scopus 로고
    • The panicogenic effects of cholecystokinin-tetrapeptide are antagonized by L-365,260, a central cholecystokinin receptor antagonist, in patients with panic disorder
    • 3. Bradwejn, J.; Koszycki, D.; Couétoux du Tertre, A.; et al. The panicogenic effects of cholecystokinin-tetrapeptide are antagonized by L-365,260, a central cholecystokinin receptor antagonist, in patients with panic disorder. Arch. Gen. Psychiatry 51:486-493; 1994.
    • (1994) Arch. Gen. Psychiatry , vol.51 , pp. 486-493
    • Bradwejn, J.1    Koszycki, D.2    Couétoux Du Tertre, A.3
  • 5
    • 0024792536 scopus 로고
    • In vivo studies on the enhancement of cholecystokinin release in the rat striatum by dopamine depletion
    • 5. Butcher, S. P.; Varro, A.; Kelly, J. S.; Dockray, G. J. In vivo studies on the enhancement of cholecystokinin release in the rat striatum by dopamine depletion. Brain Res. 505:119-122; 1989.
    • (1989) Brain Res. , vol.505 , pp. 119-122
    • Butcher, S.P.1    Varro, A.2    Kelly, J.S.3    Dockray, G.J.4
  • 7
    • 0028322136 scopus 로고
    • Investigation of the active site of aminopeptidase A using a series of new thiol-containing inhibitors
    • 7. Chauvel, E. N.; Coric, P.; Llorens-Cortès, C.; Wilk, S.; Roques, B. P.; Fournié-Zaluski, M. C. Investigation of the active site of aminopeptidase A using a series of new thiol-containing inhibitors. J. Med. Chem. 37:1339-1346; 1994.
    • (1994) J. Med. Chem. , vol.37 , pp. 1339-1346
    • Chauvel, E.N.1    Coric, P.2    Llorens-Cortès, C.3    Wilk, S.4    Roques, B.P.5    Fournié-Zaluski, M.C.6
  • 9
    • 0022271280 scopus 로고
    • Comparative distribution of cholecystokinin and other neuropeptides
    • 9. Crawley, J. N. Comparative distribution of cholecystokinin and other neuropeptides. Ann. NY Acad. Sci. 448:1-8; 1985.
    • (1985) Ann. NY Acad. Sci. , vol.448 , pp. 1-8
    • Crawley, J.N.1
  • 11
    • 0019509538 scopus 로고
    • Degradation of cholecystokinin-like peptides by a crude rat brain synaptosomal fraction: A study by high pressure liquid chromatography
    • 11. Deschodt-Lanckman, M., Bui. N. D.; Noyer, M.; Christophe, J. Degradation of cholecystokinin-like peptides by a crude rat brain synaptosomal fraction: A study by high pressure liquid chromatography. Regul. Pept. 2:15-30; 1981.
    • (1981) Regul. Pept. , vol.2 , pp. 15-30
    • Deschodt-Lanckman, M.1    Bui, N.D.2    Noyer, M.3    Christophe, J.4
  • 12
    • 0024433127 scopus 로고
    • Novel activity of angiotensin-converting enzyme. Hydrolysis of cholecystokinin and gastrin analogues with release of the C-amidated C-terminal dipeptide
    • 12. Dubreuil, P.; Fulcrand, P.; Rodriguez, M.; Fulcrand, H.; Laur, J.; Martinez, J. Novel activity of angiotensin-converting enzyme. Hydrolysis of cholecystokinin and gastrin analogues with release of the C-amidated C-terminal dipeptide. Biochem. J. 262:125-130; 1989.
    • (1989) Biochem. J. , vol.262 , pp. 125-130
    • Dubreuil, P.1    Fulcrand, P.2    Rodriguez, M.3    Fulcrand, H.4    Laur, J.5    Martinez, J.6
  • 13
    • 0022560373 scopus 로고
    • Investigation on the metabolism of CCK-8 analogues by rat brain slices
    • 13. Durieux, C., Charpentier, B.; Pélaprat, D.; Roques, B. P. Investigation on the metabolism of CCK-8 analogues by rat brain slices. Neuropeptides 7:1-9; 1986.
    • (1986) Neuropeptides , vol.7 , pp. 1-9
    • Durieux, C.1    Charpentier, B.2    Pélaprat, D.3    Roques, B.P.4
  • 17
    • 0021689369 scopus 로고
    • Morphine analgesia potentiated but tolerance not affected by active immunization against cholecystokinin
    • 17. Faris, P. L.; McLaughlin, C. L.; Baile, C. A.; Olney, J. W.; Komisaruk, B. R. Morphine analgesia potentiated but tolerance not affected by active immunization against cholecystokinin. Science 226:1215-1217; 1984.
    • (1984) Science , vol.226 , pp. 1215-1217
    • Faris, P.L.1    McLaughlin, C.L.2    Baile, C.A.3    Olney, J.W.4    Komisaruk, B.R.5
  • 18
    • 0026654502 scopus 로고
    • Potent and systemically active aminopeptidase N inhibitors designed from active site investigation
    • 18. Fournié-Zaluski, M. C.; Coric, P.; Turcaud, S.; et al. Potent and systemically active aminopeptidase N inhibitors designed from active site investigation. J. Med. Chem. 35:1259-1266; 1992.
    • (1992) J. Med. Chem. , vol.35 , pp. 1259-1266
    • Fournié-Zaluski, M.C.1    Coric, P.2    Turcaud, S.3
  • 19
    • 0028243867 scopus 로고
    • New thiol inhibitors of neutral endopeptidase EC 3.4.24.11: Synthesis and enzyme active-site recognition
    • 19. Gomez-Monterrey, I.; Beaumont, A.; Nemecek, P.; Roques, B. P.; Fournié-Zaluski, M. C. New thiol inhibitors of neutral endopeptidase EC 3.4.24.11: Synthesis and enzyme active-site recognition. J. Med. Chem. 37:1865-1873; 1994.
    • (1994) J. Med. Chem. , vol.37 , pp. 1865-1873
    • Gomez-Monterrey, I.1    Beaumont, A.2    Nemecek, P.3    Roques, B.P.4    Fournié-Zaluski, M.C.5
  • 20
    • 0024548301 scopus 로고
    • Reduction of food intake by central administration of cholecystokinin octapeptide in the rat is dependent upon inhibition of brain peptidases
    • 20. Griesbacher, T.; Leighton, G. E.; Hill, R. G.; Hughes, J. Reduction of food intake by central administration of cholecystokinin octapeptide in the rat is dependent upon inhibition of brain peptidases. Br. J. Pharmacol. 96:236-242; 1989.
    • (1989) Br. J. Pharmacol. , vol.96 , pp. 236-242
    • Griesbacher, T.1    Leighton, G.E.2    Hill, R.G.3    Hughes, J.4
  • 21
    • 0027478603 scopus 로고
    • Localization of immunoreactive glutamyl aminopeptidase in rat brain. II. Distribution and correlation with angiotensin II
    • 21. Healy, D. P.; Wilk, S. Localization of immunoreactive glutamyl aminopeptidase in rat brain. II. Distribution and correlation with angiotensin II. Brain Res. 606:295-303; 1993.
    • (1993) Brain Res. , vol.606 , pp. 295-303
    • Healy, D.P.1    Wilk, S.2
  • 22
    • 0020594325 scopus 로고
    • Cholecystokinin-immunoreactive neurons in rat and monkey cerebral cortex make symmetric synapses and have intimate associations with blood vessels
    • 22. Hendry, S. H. C.; Jones, E. G.; Beinfeld, M. C. Cholecystokinin-immunoreactive neurons in rat and monkey cerebral cortex make symmetric synapses and have intimate associations with blood vessels. Proc. Natl. Acad. Sci. USA 80:2400-2404; 1983.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 2400-2404
    • Hendry, S.H.C.1    Jones, E.G.2    Beinfeld, M.C.3
  • 23
    • 0025677681 scopus 로고
    • Influences of cholecystokinin and analogues on memory processes
    • 23. Itoh, S.; Lal, H. Influences of cholecystokinin and analogues on memory processes. Drug Dev. Res. 21:257-276; 1990.
    • (1990) Drug Dev. Res. , vol.21 , pp. 257-276
    • Itoh, S.1    Lal, H.2
  • 24
    • 0019446272 scopus 로고
    • Antinociceptive effect of centrally administered caerulcin and cholecystokinin octapeptide (CCK-8)
    • 24. Jurna, I.; Zetler, G. Antinociceptive effect of centrally administered caerulcin and cholecystokinin octapeptide (CCK-8). Eur. J. Pharmacol. 73:323-331; 1981.
    • (1981) Eur. J. Pharmacol. , vol.73 , pp. 323-331
    • Jurna, I.1    Zetler, G.2
  • 25
    • 0025292103 scopus 로고
    • Neuropeptide processing in regional brain slices: Effect of conformation and sequence
    • 25. Li, Z. W.; Bijl, W. A. A. J.; Van Nispen, J. W.; Brendel, K.; Davis, T. P. Neuropeptide processing in regional brain slices: Effect of conformation and sequence. J. Pharmacol. Exp. Ther. 253:851-857; 1990.
    • (1990) J. Pharmacol. Exp. Ther. , vol.253 , pp. 851-857
    • Li, Z.W.1    Bijl, W.A.A.J.2    Van Nispen, J.W.3    Brendel, K.4    Davis, T.P.5
  • 26
    • 0018881875 scopus 로고
    • The use of in vitro brain slices for multi-disciplinary studies of synaptic function
    • 26. Lynch, G.; Schubert, P. The use of in vitro brain slices for multi-disciplinary studies of synaptic function. Annu. Rev. Neurosci. 3:1-22; 1980.
    • (1980) Annu. Rev. Neurosci. , vol.3 , pp. 1-22
    • Lynch, G.1    Schubert, P.2
  • 28
    • 0021224624 scopus 로고
    • Endopeptidase-24.11 and aminopeptidase activity in brain synaptic membranes are jointly responsible for the hydrolysis of cholecystokinin octapeptide (CCK-8)
    • 28. Matsas, R.; Turner, A. J.; Kenny, A. J. Endopeptidase-24.11 and aminopeptidase activity in brain synaptic membranes are jointly responsible for the hydrolysis of cholecystokinin octapeptide (CCK-8). FEBS Lett. 175:124-128; 1984.
    • (1984) FEBS Lett. , vol.175 , pp. 124-128
    • Matsas, R.1    Turner, A.J.2    Kenny, A.J.3
  • 29
    • 0020557092 scopus 로고
    • Pathway of inactivation of cholecystokinin octapeptide (CCK-8) by synaptosomal fractions
    • 29. McDermott, J. R.; Dodd, P. R.; Edwardson, J. A.; Hardy, J. A.; Smith, A. I. Pathway of inactivation of cholecystokinin octapeptide (CCK-8) by synaptosomal fractions. Neurochem. Int. 5:641-647; 1983.
    • (1983) Neurochem. Int. , vol.5 , pp. 641-647
    • McDermott, J.R.1    Dodd, P.R.2    Edwardson, J.A.3    Hardy, J.A.4    Smith, A.I.5
  • 30
    • 0029050038 scopus 로고
    • Evidence for a high-affinity uptake system for cholecystokinin octapeptide (CCK-8) in rat cortical synaptosomes
    • 30. Migaud, M.; Roques, B. P.; Durieux, C. Evidence for a high-affinity uptake system for cholecystokinin octapeptide (CCK-8) in rat cortical synaptosomes. Eur. J. Neurosci. 7:1074-1079; 1995.
    • (1995) Eur. J. Neurosci. , vol.7 , pp. 1074-1079
    • Migaud, M.1    Roques, B.P.2    Durieux, C.3
  • 31
    • 0023184931 scopus 로고
    • 1251]Bolton-Hunter CCK-8. Functional significance of subregional distribution
    • 1251]Bolton-Hunter CCK-8. Functional significance of subregional distribution. Neurochem. Int. 10:495-508; 1987.
    • (1987) Neurochem. Int. , vol.10 , pp. 495-508
    • Pélaprat, D.1    Broer, Y.2    Studier, J.M.3
  • 32
    • 0027475050 scopus 로고
    • Neutral endopeptidase 24.11 : Structure, inhibition and experimental and clinical pharmacology
    • 32. Roques, B. P.; Noble, F.; Daugé, V.; Fournié-Zaluski, M. C.; Beaumont, A. Neutral endopeptidase 24.11 : structure, inhibition and experimental and clinical pharmacology. Pharmacol. Rev. 45:87-146; 1993.
    • (1993) Pharmacol. Rev. , vol.45 , pp. 87-146
    • Roques, B.P.1    Noble, F.2    Daugé, V.3    Fournié-Zaluski, M.C.4    Beaumont, A.5
  • 33
    • 0019258298 scopus 로고
    • The enkephalinase inhibitor thiorphan shows antinociceptive activity in mice
    • 33. Roques, B. P.; Fournié-Zaluski, M. C.; Soroca, E.; et al. The enkephalinase inhibitor thiorphan shows antinociceptive activity in mice. Nature 288:286-288; 1980.
    • (1980) Nature , vol.288 , pp. 286-288
    • Roques, B.P.1    Fournié-Zaluski, M.C.2    Soroca, E.3
  • 34
    • 0023739454 scopus 로고
    • A serine peptidase responsible for the inactivation of endogenous cholecystokinin in brain
    • 34. Rose, C.; Camus, A.; Schwartz, J. C. A serine peptidase responsible for the inactivation of endogenous cholecystokinin in brain. Proc. Natl. Acad. Sci. USA 85:8326-8330; 1988.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 8326-8330
    • Rose, C.1    Camus, A.2    Schwartz, J.C.3
  • 35
    • 0028930197 scopus 로고
    • Characterization of a serine peptidase responsible for the inactivation of endogenous cholecystokinin in human brain
    • 35. Rose, C.; Vargas, F.; Silhouette, B.; Devaux, B.; Schwartz, J. C. Characterization of a serine peptidase responsible for the inactivation of endogenous cholecystokinin in human brain. Neuropeptides 28:157-160; 1995.
    • (1995) Neuropeptides , vol.28 , pp. 157-160
    • Rose, C.1    Vargas, F.2    Silhouette, B.3    Devaux, B.4    Schwartz, J.C.5
  • 36
  • 37
    • 0022271305 scopus 로고
    • The satiety effect of cholecystokinin, recent progress and current problems
    • 37. Smith, G. P.; Gibbs, J. The satiety effect of cholecystokinin, recent progress and current problems. Ann. NY Acad. Sci. 448:417-423; 1985.
    • (1985) Ann. NY Acad. Sci. , vol.448 , pp. 417-423
    • Smith, G.P.1    Gibbs, J.2
  • 38
    • 0027414701 scopus 로고
    • Localization of immunoreactive glutamyl aminopeptidase in rat brain. I. Association with cerebral microvessels
    • 38. Song, L; Wilk, E.; Wilk, S.; Healy, D. P. Localization of immunoreactive glutamyl aminopeptidase in rat brain. I. Association with cerebral microvessels. Brain Res. 606:286-294; 1993.
    • (1993) Brain Res. , vol.606 , pp. 286-294
    • Song, L.1    Wilk, E.2    Wilk, S.3    Healy, D.P.4
  • 39
    • 0019323605 scopus 로고
    • Purification by affinity chromatography using amastatin and properties of aminopeptidase A from pig kidney
    • 39. Tobe, H.; Kojima, F.; Aoyagi, T.; Umezawa, H. Purification by affinity chromatography using amastatin and properties of aminopeptidase A from pig kidney. Biochim. Biophys. Acta 613:459-468; 1980.
    • (1980) Biochim. Biophys. Acta , vol.613 , pp. 459-468
    • Tobe, H.1    Kojima, F.2    Aoyagi, T.3    Umezawa, H.4
  • 40
    • 0021857736 scopus 로고
    • Are there neuropeptide-specific peptidases?
    • 40. Turner, A. J.; Matsas, R.; Kenny, A. J. Are there neuropeptide-specific peptidases? Biochem. Pharmacol. 34:1347-1356; 1985.
    • (1985) Biochem. Pharmacol. , vol.34 , pp. 1347-1356
    • Turner, A.J.1    Matsas, R.2    Kenny, A.J.3
  • 41
    • 0000723918 scopus 로고
    • Immunohistochemical localization of cholecystokinin- and gastrin-like peptides in the brain and hypophysis of the rat
    • 41. Vanderhaeghen, J. J.; Lotstra, F.; de Mey, J.; Gilles, C. Immunohistochemical localization of cholecystokinin- and gastrin-like peptides in the brain and hypophysis of the rat. Proc. Natl. Acad. Sci. USA 77:1190-1194; 1980.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 1190-1194
    • Vanderhaeghen, J.J.1    Lotstra, F.2    De Mey, J.3    Gilles, C.4
  • 42
    • 0022349804 scopus 로고
    • In vivo and in vitro effects of kelatorphan on enkephalin metabolism in rodent brain
    • 42. Waksman, G.; Bouboutou, R.; Devin, J.; et al. In vivo and in vitro effects of kelatorphan on enkephalin metabolism in rodent brain. Eur. J. Pharmacol. 117:233-243; 1985.
    • (1985) Eur. J. Pharmacol. , vol.117 , pp. 233-243
    • Waksman, G.1    Bouboutou, R.2    Devin, J.3
  • 43
    • 0026672627 scopus 로고
    • Brain and gastrointestinal cholecystokinin receptor family: Structure and functional expression
    • 43. Wank, S. A.; Pisegna, J. R.; de Weerth, A. Brain and gastrointestinal cholecystokinin receptor family: Structure and functional expression. Proc. Natl. Acad. Sci. USA 89:8691-8695; 1992.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 8691-8695
    • Wank, S.A.1    Pisegna, J.R.2    De Weerth, A.3
  • 44
    • 0000358425 scopus 로고
    • Glutamyl aminopeptidase (aminopeptidase A), the BP-1/6C3 antigen
    • 44. Wilk, S. ; Healy, D. P. Glutamyl aminopeptidase (aminopeptidase A), the BP-1/6C3 antigen. Adv. Neuroimmunol. 3:195-207; 1993.
    • (1993) Adv. Neuroimmunol. , vol.3 , pp. 195-207
    • Wilk, S.1    Healy, D.P.2
  • 45
    • 0027236292 scopus 로고
    • Purification and characterization of tripeptidylpeptidase-II from postmorten human brain
    • 45. Wilson, C.; Gibson, A. M.; McDermott, J. R. Purification and characterization of tripeptidylpeptidase-II from postmorten human brain; Neurochem. Res. 18:743-749; 1993.
    • (1993) Neurochem. Res. , vol.18 , pp. 743-749
    • Wilson, C.1    Gibson, A.M.2    McDermott, J.R.3
  • 46
    • 0025139262 scopus 로고
    • Molecular cloning of the murine BP-1/6C3 antigen: A member of the zinc-dependent metallopeptidase family
    • 46. Wu, Q.; Lahti, J. M.; Air, G. M.; Burrows, P. D.; Cooper, M. D. Molecular cloning of the murine BP-1/6C3 antigen: A member of the zinc-dependent metallopeptidase family. Proc. Natl. Acad. Sci. USA 87:993-997; 1990.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 993-997
    • Wu, Q.1    Lahti, J.M.2    Air, G.M.3    Burrows, P.D.4    Cooper, M.D.5
  • 47
    • 0022261370 scopus 로고
    • Assessment of the role of "enkephalinase" in cholecystokinin inactivation
    • 47. Zuzel, K. A.; Rose, C.; Schwartz, J. C. Assessment of the role of "enkephalinase" in cholecystokinin inactivation. Neuroscience 15:149-158; 1985.
    • (1985) Neuroscience , vol.15 , pp. 149-158
    • Zuzel, K.A.1    Rose, C.2    Schwartz, J.C.3


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