메뉴 건너뛰기




Volumn 17, Issue 4, 1996, Pages 709-720

Proteases involved in the metabolism of angiotensin II, bradykinin, calcitonin gene-related peptide (CGRP), and neuropeptide Y by vascular smooth muscle cells

Author keywords

Aminopeptidase M; Aminopeptidase P; Angiotensin II; Bradykinin; Calcitonin gene related peptide (CGRP); Carboxypeptidase M; Carboxypeptidase P; Endopeptidase 24.11; Neuropeptide Y; Peptide degradation; Vascular smooth muscle cells

Indexed keywords

AMINOPEPTIDASE; ANGIOTENSIN; ANGIOTENSIN DERIVATIVE; BRADYKININ; BRADYKININ DERIVATIVE; CALCITONIN GENE RELATED PEPTIDE; CAPTOPRIL; CARBOXYPEPTIDASE; ENALAPRILAT; ENZYME INHIBITOR; NEUROPEPTIDE Y; NEUROPEPTIDE Y DERIVATIVE; PROTEINASE;

EID: 0029948534     PISSN: 01969781     EISSN: None     Source Type: Journal    
DOI: 10.1016/0196-9781(96)00066-6     Document Type: Article
Times cited : (98)

References (40)
  • 1
    • 0002087037 scopus 로고
    • Neuropeptide-degrading peptidases
    • Parvez, S. H.; Naoi, T.; Nagatsu, S.; Parvez, S., eds. Amsterdam: Elsevier Science Publishers
    • 1. Checler, F. Neuropeptide-degrading peptidases. In: Parvez, S. H.; Naoi, T.; Nagatsu, S.; Parvez, S., eds. Methods in neurotransmitter and neuropeptide research. Amsterdam: Elsevier Science Publishers; 1993:375-418.
    • (1993) Methods in Neurotransmitter and Neuropeptide Research , pp. 375-418
    • Checler, F.1
  • 2
    • 0026760229 scopus 로고
    • Purification of the main somatostatin-degrading proteases from rat and pig brains, their action on other neuropeptides, and their identification as endopeptidases 24.15 and 24.16
    • 2. Dahms, P.; Mentlein, R. Purification of the main somatostatin-degrading proteases from rat and pig brains, their action on other neuropeptides, and their identification as endopeptidases 24.15 and 24.16. Eur. J. Biochem. 208:145-154; 1992.
    • (1992) Eur. J. Biochem. , vol.208 , pp. 145-154
    • Dahms, P.1    Mentlein, R.2
  • 4
    • 0027526508 scopus 로고
    • Characterization of neutral endopeptidase in vascular smooth muscle cells of rabbit renal cortex
    • 4. Dussaule, J.-C.; Stefanski. A.; Bea, M.-L.; Ronco, P.; Ardaillou, R. Characterization of neutral endopeptidase in vascular smooth muscle cells of rabbit renal cortex. Am. J. Physiol. 264:F45-F52: 1993.
    • (1993) Am. J. Physiol. , vol.264
    • Dussaule, J.-C.1    Stefanski, A.2    Bea, M.-L.3    Ronco, P.4    Ardaillou, R.5
  • 5
    • 0025800166 scopus 로고
    • A large accumulation of nonmuscle myosin occurs at first entry into M phase in rat vascular smooth-muscle cells
    • 5. Graininger, D. J.; Hesketh, T. R.; Metcalfe, J. C.; Weissberg, P. L. A large accumulation of nonmuscle myosin occurs at first entry into M phase in rat vascular smooth-muscle cells. Biochem. J. 277:145-151; 1991.
    • (1991) Biochem. J. , vol.277 , pp. 145-151
    • Graininger, D.J.1    Hesketh, T.R.2    Metcalfe, J.C.3    Weissberg, P.L.4
  • 7
    • 0002168533 scopus 로고
    • Characterization of receptor types for neuropeptide Y and related peptides
    • Colmers, W. F.; Wahlestedt, C., eds. Totowa, NJ: Humana Press
    • 7. Grundemar, E.; Sheikh, S. P.; Wahlestedt, R. Characterization of receptor types for neuropeptide Y and related peptides. In: Colmers, W. F.; Wahlestedt, C., eds. The biology of neuropeptide Y and related peptides. Totowa, NJ: Humana Press: 1993:197-239.
    • (1993) The Biology of Neuropeptide Y and Related Peptides , pp. 197-239
    • Grundemar, E.1    Sheikh, S.P.2    Wahlestedt, R.3
  • 8
    • 0025729999 scopus 로고
    • Aminopeptidase p from rat brain. Purification and action on bioactive peplides
    • 8. Harbeck, H.-T.; Mentlein, R. Aminopeptidase P from rat brain. Purification and action on bioactive peplides. Eur. J. Biochem. 198:451-458; 1991.
    • (1991) Eur. J. Biochem. , vol.198 , pp. 451-458
    • Harbeck, H.-T.1    Mentlein, R.2
  • 9
    • 0021887946 scopus 로고
    • Proteins of the kidney microvillar membrane. Purification and properties of carboxypeptidase P
    • 9. Hedeager-Sørensen, S.; Kenny, A. J. Proteins of the kidney microvillar membrane. Purification and properties of carboxypeptidase P. Biochem. J. 229:251-257; 1985.
    • (1985) Biochem. J. , vol.229 , pp. 251-257
    • Hedeager-Sørensen, S.1    Kenny, A.J.2
  • 11
    • 0017846443 scopus 로고
    • Liver dipeptidyl peptidase IV hydrolyzes substance P
    • 11. Heymann, E.; Mentlein, R. Liver dipeptidyl peptidase IV hydrolyzes substance P. FEBS Lett. 91:360-364; 1978.
    • (1978) FEBS Lett. , vol.91 , pp. 360-364
    • Heymann, E.1    Mentlein, R.2
  • 12
    • 0022710942 scopus 로고
    • Complementary action of dipeptidyl peptidase IV and aminopeptidase m in the digestion of β-casein
    • 12. Heymann, E.; Mentlein, R. Complementary action of dipeptidyl peptidase IV and aminopeptidase M in the digestion of β-casein. J. Dairy Res. 53:229-236; 1986.
    • (1986) J. Dairy Res. , vol.53 , pp. 229-236
    • Heymann, E.1    Mentlein, R.2
  • 13
    • 0026735121 scopus 로고
    • Inhibition by converting enzyme inhibitors of pig kidney aminopeptidase P
    • 13. Hooper, N. M.; Hryszko, J.; Oppong, S. Y.; Turner. A. J. Inhibition by converting enzyme inhibitors of pig kidney aminopeptidase P. Hypertension 19:281-285; 1992.
    • (1992) Hypertension , vol.19 , pp. 281-285
    • Hooper, N.M.1    Hryszko, J.2    Oppong, S.Y.3    Turner, A.J.4
  • 15
    • 85047679362 scopus 로고
    • Plasma neuropeptide Y on admission to a coronary care unit: Raised levels in patients with left heart failure
    • 15. Hulting, J.; Sollevi, A.; Ulmann, B.; Franco-Cereceda, A.; Lundberg, J. M. Plasma neuropeptide Y on admission to a coronary care unit: Raised levels in patients with left heart failure. Cardiovas. Res. 24:102-108; 1990.
    • (1990) Cardiovas. Res. , vol.24 , pp. 102-108
    • Hulting, J.1    Sollevi, A.2    Ulmann, B.3    Franco-Cereceda, A.4    Lundberg, J.M.5
  • 16
  • 17
    • 0023655460 scopus 로고
    • Proteins of the kidney microvillar membrane. Purification and properites of the phosphoramidon-insensitive endopeptidase ("endopeptidase-2") from rat kidney
    • 17. Kenny, A. J.; Ingram, J. Proteins of the kidney microvillar membrane. Purification and properites of the phosphoramidon-insensitive endopeptidase ("endopeptidase-2") from rat kidney. Biochem. J. 245:515-524; 1987.
    • (1987) Biochem. J. , vol.245 , pp. 515-524
    • Kenny, A.J.1    Ingram, J.2
  • 18
    • 0024324450 scopus 로고
    • Calcitonin gene-related peptide is metabolized by an endopeptidase hydrolyzing substance P
    • 18. Le Grevès, P.; Nyberg, F.; Hökfelt, T.; Terenius, L. Calcitonin gene-related peptide is metabolized by an endopeptidase hydrolyzing substance P. Regul. Pept. 25:277-286; 1989.
    • (1989) Regul. Pept. , vol.25 , pp. 277-286
    • Le Grevès, P.1    Nyberg, F.2    Hökfelt, T.3    Terenius, L.4
  • 19
    • 0025991223 scopus 로고
    • Degradation of the neuropeptide somatostatin by cultivated neuronal and glial cells
    • 19. Lucius, R.; Mentlein, R. Degradation of the neuropeptide somatostatin by cultivated neuronal and glial cells. J. Biol. Chem. 266:18907-18913; 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 18907-18913
    • Lucius, R.1    Mentlein, R.2
  • 20
    • 0028988354 scopus 로고
    • Enkephalin metabolism by microglia aminopeptidase N (CD13)
    • 20. Lucius, R.; Sievers, J.; Mentlein, R. Enkephalin metabolism by microglia aminopeptidase N (CD13). J. Neurochem. 64:1841-1847; 1995.
    • (1995) J. Neurochem. , vol.64 , pp. 1841-1847
    • Lucius, R.1    Sievers, J.2    Mentlein, R.3
  • 21
    • 85030198646 scopus 로고    scopus 로고
    • Metabolism of neuropeptide Y and calcitonin gene-related peptide by cultivated neurons and glial cells
    • in press
    • 21. Ludwig, R.; Feindt, J.; Lucius, R.; Petersen, A.; Mentlein, R. Metabolism of neuropeptide Y and calcitonin gene-related peptide by cultivated neurons and glial cells. Mol. Brain Res. (in press).
    • Mol. Brain Res.
    • Ludwig, R.1    Feindt, J.2    Lucius, R.3    Petersen, A.4    Mentlein, R.5
  • 23
    • 0024291209 scopus 로고
    • Proline residues in the maturation and degradation of peptide hormones and neuropeptides
    • 23. Mentlein, R. Proline residues in the maturation and degradation of peptide hormones and neuropeptides. FEBS Lett. 234:251-256; 1988.
    • (1988) FEBS Lett. , vol.234 , pp. 251-256
    • Mentlein, R.1
  • 24
    • 0024418307 scopus 로고
    • Binding and internalization of gold-conjugated somatostatin and growth hormone-releasing hormone in cultured rat somatotropes
    • 24. Mentlein, R.; Buchholz, C.; Krisch, B. Binding and internalization of gold-conjugated somatostatin and growth hormone-releasing hormone in cultured rat somatotropes. Cell Tissue Res. 258:309-317; 1989.
    • (1989) Cell Tissue Res. , vol.258 , pp. 309-317
    • Mentlein, R.1    Buchholz, C.2    Krisch, B.3
  • 25
    • 0028079465 scopus 로고
    • Endopeptidases 24.16 and 24.15 are responsible for the degradation of somatostatin, neurotensin, and other neuropeptides by cultivated rat cortical astrocytes
    • 25. Mentlein, R.; Dahms, P. Endopeptidases 24.16 and 24.15 are responsible for the degradation of somatostatin, neurotensin, and other neuropeptides by cultivated rat cortical astrocytes. J. Neurochem. 62:27-36; 1994.
    • (1994) J. Neurochem. , vol.62 , pp. 27-36
    • Mentlein, R.1    Dahms, P.2
  • 26
    • 0027494070 scopus 로고
    • Proteolytic processing of neuropeptide Y and peptide YY by dipeptidyl peptidase IV
    • 26. Mentlein, R.; Dahms, P.; Grandt, D.; Krüger, R. Proteolytic processing of neuropeptide Y and peptide YY by dipeptidyl peptidase IV. Regul. Pept. 49:133-144; 1993.
    • (1993) Regul. Pept. , vol.49 , pp. 133-144
    • Mentlein, R.1    Dahms, P.2    Grandt, D.3    Krüger, R.4
  • 27
    • 0025042324 scopus 로고
    • Proline-specific proteases in cultivated neuronal and glial cells
    • 27. Mentlein, R.; von Kolszynski, M.; Sprang, R.; Lucius, R. Proline-specific proteases in cultivated neuronal and glial cells. Brain Res. 527:159-162; 1990.
    • (1990) Brain Res. , vol.527 , pp. 159-162
    • Mentlein, R.1    Von Kolszynski, M.2    Sprang, R.3    Lucius, R.4
  • 28
    • 0024592793 scopus 로고
    • Purification of two dipeptidyl peptidases II from rat brain and their action on proline-containing neuropeptides
    • 28. Mentlein, R.; Struckhoff, G. Purification of two dipeptidyl peptidases II from rat brain and their action on proline-containing neuropeptides. J. Neurochem. 52:1284-1293; 1989.
    • (1989) J. Neurochem. , vol.52 , pp. 1284-1293
    • Mentlein, R.1    Struckhoff, G.2
  • 29
    • 0027365714 scopus 로고
    • Possible action of placental aminopeptidase N in feto-placental unit
    • 29. Mitzutani, S.; Goto, K.; Nomura, S.; et al. Possible action of placental aminopeptidase N in feto-placental unit. Res. Commun. Chem. Pathol. Pharmacol. 82:65-80; 1993.
    • (1993) Res. Commun. Chem. Pathol. Pharmacol. , vol.82 , pp. 65-80
    • Mitzutani, S.1    Goto, K.2    Nomura, S.3
  • 30
    • 0023353011 scopus 로고
    • Aminopeptidase P from bovine lung: Solubilization, properties and potential role in bradykinin degradation
    • 30. Orawski, A. T.; Susz, J. P.; Simmons, W. H. Aminopeptidase P from bovine lung: Solubilization, properties and potential role in bradykinin degradation. Mol. Cell. Biochem. 75:123-132; 1987.
    • (1987) Mol. Cell. Biochem. , vol.75 , pp. 123-132
    • Orawski, A.T.1    Susz, J.P.2    Simmons, W.H.3
  • 31
    • 0027225474 scopus 로고
    • Vasoactive peptides and characterization of their receptors
    • 31. Regoli, D.; D'Orleans-Juste, P.; Rouissi, N.; Rhaled, N. E. Vasoactive peptides and characterization of their receptors. Regul. Pept. 45:323-340; 1993.
    • (1993) Regul. Pept. , vol.45 , pp. 323-340
    • Regoli, D.1    D'Orleans-Juste, P.2    Rouissi, N.3    Rhaled, N.E.4
  • 32
    • 0024461541 scopus 로고
    • Peptidase enzymes of the pulmonary vascular surface
    • 32. Ryan, J. W. Peptidase enzymes of the pulmonary vascular surface. Am. J. Physiol. 257:L53-L60; 1989.
    • (1989) Am. J. Physiol. , vol.257
    • Ryan, J.W.1
  • 33
    • 0026535512 scopus 로고
    • Purification and characterization of guinea pig serum aminoacylproline hydrolase (aminopeptidase P)
    • 33. Ryan, J. W.; Valido, F.; Berryer, P.; Chung, A. Y. K.; Ripka, J. E. Purification and characterization of guinea pig serum aminoacylproline hydrolase (aminopeptidase P). Biochim. Biophys. Acta 1119:140-147; 1992.
    • (1992) Biochim. Biophys. Acta , vol.1119 , pp. 140-147
    • Ryan, J.W.1    Valido, F.2    Berryer, P.3    Chung, A.Y.K.4    Ripka, J.E.5
  • 34
    • 0024502906 scopus 로고
    • Binding of monoiodinated neuropeptide Y to hippocampal membranes and human neuroblastoma cell lines
    • 34. Sheikh, S. P.; O'Hare, M. M. T.; Tortora, O.; Schwartz, T. W. Binding of monoiodinated neuropeptide Y to hippocampal membranes and human neuroblastoma cell lines. J. Biol. Chem. 264:6648-6654; 1989.
    • (1989) J. Biol. Chem. , vol.264 , pp. 6648-6654
    • Sheikh, S.P.1    O'Hare, M.M.T.2    Tortora, O.3    Schwartz, T.W.4
  • 35
    • 0023153985 scopus 로고
    • Metabolism of neuropeptides. Hydrolysis of the angiotensins, bradykinin, substance P and oxytocin by pig kidney microvillar membranes
    • 35. Stephenson, S. L.; Kenny, A. J. Metabolism of neuropeptides. Hydrolysis of the angiotensins, bradykinin, substance P and oxytocin by pig kidney microvillar membranes. Biochem. J. 241:237-247; 1987.
    • (1987) Biochem. J. , vol.241 , pp. 237-247
    • Stephenson, S.L.1    Kenny, A.J.2
  • 36
    • 0023748129 scopus 로고
    • The metabolism of neuropeptides. Hydrolysis of peptides by the phosphoramidon-insensitive rat kidney enzyme "endopeptidase-2" and by rat microvillar membranes
    • 36. Stephenson, S. L.; Kenny, A. J. The metabolism of neuropeptides. Hydrolysis of peptides by the phosphoramidon-insensitive rat kidney enzyme "endopeptidase-2" and by rat microvillar membranes. Biochem. J. 255:45-51; 1988.
    • (1988) Biochem. J. , vol.255 , pp. 45-51
    • Stephenson, S.L.1    Kenny, A.J.2
  • 38
    • 0028302546 scopus 로고
    • Metabolism of substance P and neurokinin A by human vascular endothelium and smooth muscle
    • 38. Wang, L.; Sadoun, E.; Stephens, R. E.; Ward, P. E. Metabolism of substance P and neurokinin A by human vascular endothelium and smooth muscle. Peptides 15:497-503; 1994.
    • (1994) Peptides , vol.15 , pp. 497-503
    • Wang, L.1    Sadoun, E.2    Stephens, R.E.3    Ward, P.E.4
  • 39
    • 0027359062 scopus 로고
    • Endopeptidase 3.4.24.11 converts N-1 (R,S)carboxy-3-phenylpropyl-Ala-Ala-Phe-carboxyanilide into a potent inhibitor of angiotensin-converting enzyme
    • 39. Williams, C. H.; Yamamoto, T.; Walsh, D. M.; Allsop, D. Endopeptidase 3.4.24.11 converts N-1 (R,S)carboxy-3-phenylpropyl-Ala-Ala-Phe-carboxyanilide into a potent inhibitor of angiotensin-converting enzyme. Biochem. J. 294:681-684; 1993.
    • (1993) Biochem. J. , vol.294 , pp. 681-684
    • Williams, C.H.1    Yamamoto, T.2    Walsh, D.M.3    Allsop, D.4
  • 40
    • 0003080075 scopus 로고
    • Origin and actions of neuropeptide Y in the cardiovascular system
    • Colmers, W. F.; Wahlestedt, C., eds. Totowa, NJ: Humana Press
    • 40. Zukowska-Grojec, Z.; Wahlestedt, C. Origin and actions of neuropeptide Y in the cardiovascular system. In: Colmers, W. F.; Wahlestedt, C., eds. The biology of neuropeptide Y and related peptides. Totowa, NJ: Humana Press; 1993:315-388.
    • (1993) The Biology of Neuropeptide Y and Related Peptides , pp. 315-388
    • Zukowska-Grojec, Z.1    Wahlestedt, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.