Hypothesized and found mechanisms for potentiation bradykinin actions

Signal Transduction

Volumn 6, Issue 1, 2006, Pages 5-18

  Mueller, Sylvia ^a   Paegelow, Inge ^b   Reissmann, Siegmund ^a  

^a FRIEDRICH SCHILLER UNIVERSITY JENA   (Germany)

^b UNIVERSITY OF ROSTOCK   (Germany)

Author keywords

Angiotensin I converting enzyme; Bradykinin B1 and B2 receptors; Crosstalk; Polymorphonuclear leukocytes; Potentiation

Indexed keywords

BRADYKININ; DIPEPTIDYL CARBOXYPEPTIDASE; HORMONE RECEPTOR; ION CHANNEL;

CELL ACTIVATION; ENZYME DEGRADATION; ENZYME INHIBITION; HORMONE ACTION; HYPOTENSION; IMMUNOCOMPETENT CELL; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; REVIEW; SIGNAL TRANSDUCTION; SMOOTH MUSCLE;

EID: 33644858629     PISSN: 16154053     EISSN: 16154061     Source Type: Journal    
DOI: 10.1002/sita.200500061     Document Type: Review

References (119)

1. 2. J. Med. Chem. 36: 3481-3483.
2. Ladram, A., Montagne, J.J., Bulant, M., Nicolas, P. (1994) Analysis of structural requirements for TRH-potentiating peptide receptor binding by analogue design. Peptides 15: 429-433.
3. 125I]ANF binding to FRTL-5 rat thyroid cells by increasing ANF receptor affinity. Peptides 15: 1249-1253.
4. Rocha e Silva, M., Reis, M.L., Ferreira, S.H. (1976) Release of kinins from fresh plasma under varying experimental conditions. Biochem. Pharmacol. 16: 1665-1676.
5. Kato, H., Suzuki, T. (1969) Bradykinin-potentiating peptides from the venom of Agkistrodon halys blomhoffii. Experientia 25: 694-695.
6. Kato, H., Suzuki, T. (1971) Bradykinin-potentiating peptides from the venom of Agkistrodon halys blomhoffii. Isolation of five bradykinin potentiators and the amino acid sequences of two of them, potentiators B and C. Biochemistry 10: 972-980.
7. Ferreira, S.H. (1965) A Bradykinin-Potentiating Factor (Bpf) Present in the Venom of Bothrops jararaca. Br. J. Pharmacol. 24: 163-169.
8. Ferreira, S.H., Bartelt, D.C., Greene, L.J. (1970) Isolation of bradykinin-potentiating peptides from Bothrops jararaca venom. Biochemistry 9: 2583-2593.
9. Cushman, D.W., Pluscec, J., Williams, N.J., Weaver, E.R., Sabo, E.F., Kocy, O., Cheung, H.S., Ondetti, M.A. (1973) Inhibition of angiotensin- converting enzyme by analogs of peptides from Bothrops jararaca venom. Experientia 29: 1032-1035.
10. Ondetti, M.A., Williams, N.J., Sabo, E.F., Pluscec, J., Weaver, E.R., Kocy, O. (1971) Angiotensin-converting enzyme inhibitors from the venom of Bothrops jararaca. Isolation, elucidation of structure, and synthesis. Biochemistry 10: 4033-4039.
11. Cintra, A.C., Vieira, C.A., Giglio, J.R. (1990) Primary structure and biological activity of bradykinin potentiating peptides from Bothrops insularis snake venom. J. Protein Chem. 9: 221-227.
12. Ferreira, L.A., Henriques, O.B., Lebrun, I., Batista, M.B., Prezoto, B.C., Andreoni, A.S., Zelnik, R., Habermehl, G. (1992) A new bradykinin-potentiating peptide (peptide P) isolated from the venom of Bothrops jararacussu (jararacucu tapete, urutu dourado). Toxicon 30: 33-40.
13. Ferreira, L.A., Galle, A., Raida, M., Schrader, M., Lebrun, I., Habermehl, G. (1998) Isolation: analysis and properties of three bradykinin-potentiating peptides (BPP-II, BPP-III, and BPP-V) from Bothrops neuwiedi venom. J. Protein Chem. 17: 285-289.
14. Chi, C.W., Wang, S.Z., Xu, L.G., Wang, M.Y., Lo, S.S., Huang, W.D. (1985) Structure-function studies on the bradykinin potentiating peptide from Chinese snake venom (Agkistrodon halys Pallas). Peptides 6 Suppl. 3: 339-342.
15. Ferreira, L.A., Mollring, T., Lebrun, F.L., Raida, M., Znottka, R., Habermehl, G.G. (1995) Structure and effects of a kinin potentiating fraction F (AppF) isolated from Agkistrodon piscivorus piscivorus venom. Toxicon 33: 1313-1319.
16. L'vov, V.M., Yukel'son, L.Y. (1995) Bradykinin-potentiating Peptides from Echis multisquamatus venom. Khim. Prir. Soedin. 1: 435-440.
17. Ferreira, L.A., Alves, E.W., Henriques, O.B. (1993) Peptide T, a novel bradykinin potentiator isolated from Tityus serrulatus scorpion venom. Toxicon 31: 941-947.
18. Meki, A.R., Nassar, A.Y., Rochat, H. (1995) A bradykinin-potentiating peptide (peptide K12) isolated from the venom of Egyptian scorpion Buthus occitanus. Peptides 16: 1359-1365.
19. Zeng, X.C., Li, W.X., Peng, F., Zhu, Z.H. (2000) Cloning and characterization of a novel cDNA sequence encoding the precursor of a novel venom peptide (BmKbpp) related to a bradykinin-potentiating peptide from Chinese scorpion Buthus martensii Karsch. IUBMB Life 49: 207-210.
20. Sosnina, N.A., Golubenko, Z., Akhunov, A.A., Kugaevskaia, E.V., Eliseeva Iu, E., Orekhovich, V.N. (1990) Bradykinin-potentiating peptides from the spider Latrodectus tredecimguttatus-inhibitors of carboxycathepsin and of a preparation of karakurt venom kininase. Dokl. Akad. Nauk. SSSR 315: 236-239.
21. Akchunov, A.A., Golubenko, Z., Sosnina, N. (1992) Isolation and characterization of biological properties of inhibitors angiotensin-1-converting enzyme from the spider venom Latrodectus tredecimguttatus. Agents Actions Suppl. 38 (Pt 1): 469-474.
22. Ferreira, L.A., Alves, W.E., Lucas, M.S., Habermehl, G.G. (1996) Isolation and characterization of a bradykinin potentiating peptide (BPP-S) isolated from Scaptocosa raptoria venom. Toxicon 34: 599-603.
23. Yamafuji, K., Taniguchi, Y., Sakamoto, E. (1996) The thiol enzyme from rat spleen that produces bradykinin potentiating peptide from rat plasma. Immunopharmacology 32: 157-159.
24. Sakamoto, E., Sakao, Y., Taniguchi, Y., Yamafuji, K. (1999) Cathepsin Y (a novel thiol enzyme) produces kinin potentiating peptide from the component protein of rat plasma. Immunopharmacology 45: 207-214.
25. Rodrigues, M.S., Schaffel, R., Assreuy, J. (1992) Comparative study on the mechanism of bradykinin potentiation induced by bradykinin-potentiating peptide 9a, enalaprilat and kinin-potentiating peptide. Eur. J. Pharmacol. 216: 357-362.
26. 9α) on kinin-induced rat paw edema. Agents Actions 32: 182-187.
27. Assreuy, J., Almeida, A.A., Guimaraes, J.A. (1989) Pharmacological properties of a new kinin-potentiating peptide generated from human serum proteins. Eur. J. Pharmacol. 168: 231-237.
28. Piot, J.M., Zhao, Q., Guillochon, D., Ricart, G., Thomas, D. (1992) Isolation and characterization of a bradykinin-potentiating peptide from a bovine peptic hemoglobin hydrolysate. FEBS Lett. 299: 75-79.
29. Ivanov, V.T., Karelin, A.A., Philippova, M.M., Nazimov, I.V., Pletnev, V.Z. (1997) Hemoglobin as a source of endogenous bioactive peptides: The concept of tissue-specific peptide pool. Biopolymers (Peptide Science) 43: 171-188.
30. Zhao, Q., Garreau, I., Sannier, F., Piot, J.M. (1997) Opioid peptides derived from hemoglobin: hemorphins. Biopolymers (Peptide Science) 43: 75-98.
31. Lignot, B., Froidevaux, R., Nedjar-Arroume, N., Guillochon, D. (1999) Solvent effect on kinetics of appearance of neokyotorphin, VV-haemorphin-4 and a bradykinin-potentiating peptide in the course of peptic hydrolysis of bovine haemoglobin. Biotechnol. Appl. Biochem. 30 (Pt 3): 201-207.
32. Henriques, O.B., de Deus, R.B., Santos, R.A. (1987) Bradykinin potentiating peptides isolated from alpha-casein tryptic hydrolysate. Biochem. Pharmacol. 36: 182-184.
33. Lebrun, I., Lebrun, F.L., Henriques, O.B., Carmona, A.K., Juliano, L., Camargo, A.C. (1995) Isolation and characterization of a new bradykinin potentiating octapeptide from gamma-casein. Can. J. Physiol. Pharmacol. 73: 85-91.
34. Matsui, T., Li, C.H., Osajima, Y. (1999) Preparation and characterization of novel bioactive peptides responsible for angiotensin I-converting enzyme inhibition from wheat germ. J. Pept. Sci. 5: 289-297.
35. Paula, R.D., Lima, C.V., Britto, R.R., Campagnole-Santos, M.J., Khosla, M.C., Santos, RA (1999) Potentiation of the hypotensive effect of bradykinin by angiotensin-(1-7)-related peptides. Peptides 20: 493-500.
36. Chaturvedi, D., Huelar, E., Gunthorpe, M., Gofman, M., Krapf, D.S., Apostol, E., Lewis, W.S. (1993) Bradykinin analogs as inhibitors of angiotensin-converting enzyme. Pept. Res. 6: 308-312.
37. Schumann, C., Seyfarth, L., Greiner, G., Paegelow, I., Reissmann, S. (2002) Synthesis and biological activities of new side chain and backbone cyclic bradykinin analogues. J. Pept. Res. 60: 128-140.
38. Cirstea, M. (1965) Potentiation of some bradykinin effects by thiol compounds. Br. J. Pharmacol. Chemother. 25: 405-410.
39. Auerswald, W., Doleschel, W. (1967) On the potentiation of kinins by sulfhydrylic compounds. Arch. Int. Pharmacodyn. Ther. 168: 188-198.
40. Hall, D.W., Bonta, I.L. (1974) Potentiation of the biphasic bradykinin response of the guinea-pig ileum. Arch. Int. Pharmacodyn. Ther. 207: 361-372.
41. Higuchi, S., Murayama, N., Saguchi, K., Ohi, H., Fujita, Y., Camargo, A.C., Ogawa, T., Deshimaru, M., Ohno, M. (1999) Bradykinin-potentiating peptides and C-type natriuretic peptides from snake venom. Immunopharmacology 44: 129-135.
42. Hayashi, M.A., Murbach, A.F., Ianzer, D., Portaro, F.C., Prezoto, B.C., Fernandes, B.L., Silveira, P.F., Silva, C.A., Pires, R.S., Britto, L.R., Dive, V., Camargo, A.C. (2003) The C-type natriuretic peptide precursor of snake brain contains highly specific inhibitors of the angiotensin-converting enzyme. J. Neurochem. 85: 969-977.
43. Ianzer, D., Konno, K., Marques-Porto, R., Vieira Portaro, F.C., Stocklin, R., Martins de Camargo, A.C., Pimenta, D.C. (2004) Identification of five new bradykinin potentiating peptides (BPPs) from Bothrops jararaca crude venom by using electrospray ionization tandem mass spectrometry after a two-step liquid chromatography. Peptides 25: 1085-1092.
44. Gavras, I., Gavras, H. (2002) Metabolic effects of angiotensin-converting enzyme inhibition: the role of bradykinin. Curr. Opin. Endocrinol. Diabetes 9: 323-328.
45. Kudoh, A., Dietze, G.J., Rabito, S.F. (2000) Insulin enhances the bradykinin response in L8 rat skeletal myoblasts. Diabetes 49: 190-194.
46. Kudoh, A., Kudoh, E., Katagai, H., Takazawa, T. (2002) Insulin potentiates bradykinin-induced inositol 1,4,5-triphosphate in neonatal rat cardiomyocytes. J. Cardiovasc. Pharmacol. 39: 621-627.
47. Minshall, R.D., Nedumgottil, S.J., Igic, R., Erdös, E.G., Rabito, S.F. (2000) Potentiation of the effects of bradykinin on its receptor in the isolated guinea pig ileum. Peptides 21: 1257-1264.
48. Dendorfer, A., Reissmann, S., Wolfrum, S., Raasch, W., Dominiak, P. (2001) Potentiation of kinin analogues by ramiprilat is exclusively related to their degradation. Hypertension 38: 142-146.
49. 2 receptor? Immunopharmacology 33: 93-94.
50. Norman, M.U., Lew, R.A., Smith, A.I., Hickey, M.J. (2003) Metalloendopeptidases EC 3.4.24.15/16 regulate bradykinin activity in the cerebral microvasculature. Am. J. Phystol. Heart. Circ. Physiol. 284: H1942-1948.
51. Tom, B., de Vries, R., Saxena, P.R., Danser, A.H. (2001) Bradykinin potentiation by angiotensin-(1-7) and ACE inhibitors correlates with ACE C- and N-domain blockade. Hypertension 38: 95-99.
52. 2 receptors and angiotensin I-converting enzyme in CHO cells. Circ. Res. 81: 848-856.
53. 2 receptor. Hypertension 33: 835-843.
54. 1 receptor by ACE inhibitors. Int. Immunophormacol. 2: 1787-1793.
55. 2 receptor. Hypertension 39: 619-623.
56. Jaeger, P., Ferguson, R.K., Brunner, H.R., Kirchertz, E.J., Gavras, H. (1978) Mechanism of blood pressure reduction by teprotide (SQ 20881) in rats. Kidney Int. 13: 289-296.
57. Boels, K., Schaller, H.C. (2003) Identification and characterization of GPR100 as a novel human G-protein-coupled bradykinin receptor. Br. J. Pharmacol. 140: 932-938.
58. Meini, S., Bellucci, F., Cucchi, P., Giulani, S., Quartara, L., Giolitti, A., Zappitelli, S., Rotondaro, L., Boels, K., Maggi, C.A. (2004) Bradykinin and GPR100 receptors: a paradigm for receptor signal transduction pharmacology. Br. J. Pharmacol. 143: 938-941.
59. 2 kinin receptors. Br. J. Pharmacol. 143: 931-932.
60. Chan, D., Gera, L., Stewart, J., Helfrich, B., Verella-Garcia, M., Johnson, G., Baron, A., Yang, J., Puck, T., Bunn, P., Jr. (2002) Bradykinin antagonist dimer, CU201, inhibits the growth of human lung cancer cell lines by a "biased agonist" mechanism. Proc. Natl. Acad. Sci. U.S.A. 99: 4608-4613.
61. AbdAlla, S., Lother, H., Quitterer, U. (2000) AT1-receptor heterodimers show enhanced G-protein activation and altered receptor sequestration. Nature 407: 94-98.
62. Paegelow, I., Reissmann, S., Arold, H. (1976) The effect of bradykinin potentiating factors (BPF) on bradykinin in vitro. Acta Biol. Med. Ger. 35(2): 235-244.
63. Ferry, X., Brehin, S., Kamel, R., Landry, Y. (2002) G protein-dependent activation of mast cell by peptides and basic secretagogues. Peptides 23: 1507-1515.
64. i-like proteins, a receptor-independent effect of kinins in mast cells. Mol. Pharmocol. 38: 816-822.
65. Klinker, J.F., Hageluken, A., Grunbaum, L., Seifert, R. (1995) Direct and indirect receptor-independent G-protein activation by cationic-amphiphilic substances. Exp. Dermatol. 4: 231-239.
66. Odagaki, Y., Nishi, N., Nakagawa, S., Koyama, T. (1999) Activation of G proteins by neuropeptide Y and gamma-aminobutyric acid(B) receptor agonists in rat cerebral cortical membranes through distinct modes of action. J. Pharmacol. Exp. Ther. 291: 1250-1256.
67. Zhu, J., Toews, M.L., MacDonald, R.G., Hexum, T.D. (1994) Neuropeptide Y promotes GTP photo-incorporation into a 55 kDa protein. Eur. J. Pharmacol. 268: 279-291.
68. o by mastoparan, related amphiphilic peptides, and hydrophobic amines. Mechanism and structural determinants of activity. J. Biol. Chem. 265: 14176-14186.
69. Gies, J.P., Landry, Y., Mousli, M. (1993) Receptor-independent activation of mast cells by bradykinin and related peptides. Trends Neurosci 16: 498-499.
70. Wei, L., Alhenc-Gelas, F., Corvol, P., Clauser, E. (1991) The two homologous domains of human angiotensin I-converting enzyme are both catalytically active. J. Biol. Chem. 266: 9002-9008.
71. Deddish, P.A., Marcic, B., Jackman, H.L., Wang, H.Z., Skidgel, R.A., Erdös, E.G. (1998) N-domain-specific substrate and C-domain inhibitors of angiotensin-converting enzyme: angiotensin-(1-7) and keto-ACE. Hypertension 31: 912-917.
72. Cotton, J., Hayashi, M.A., Cuniasse, P., Vazeux, G., Ianzer, D., De Camargo, A.C., Dive, V. (2002) Selective inhibition of the C-domain of angiotensin I converting enzyme by bradykinin potentiating peptides. Biochemistry 41: 6065-6071.
73. Natesh, R., Schwager, S.L.U., Sturrock, E.D., Acharya, K.R. (2003). Crystal structure of the human angiotensin-converting enzyme-lisinopril complex. Nature 421: 551-554.
74. Ehlers, M.R.W., Fox, E.A., Strydom, D.J., Riordan, J.F. (1989) Molecular cloning of the human testicular angiotensin-converting enzyme. Proc. Natl. Acad. Sci. U.S.A. 86: 7741-7745.
75. Warner, F.J., Guy, J.L., Lambert, D.W., Hooper, N.M., Turner, A.J. (2003) Angiotensin converting enzyme-2 (ACE2) and its possible roles in hypertension, diabetes and cardiac function. LIPS 10: 377-385.
76. Li, W., Moore, M.J., Vasilieva, N., Sui, J., Wong, S.K., Berne, M.A., Somasundaran, M., Sullivan, J.L., Luzuriaga, K., Greenough, T.C., Choe, H., Farzan, M. (2003) Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus. Nature 426: 450-454.
77. Hecker, M., Blaukat, A., Bara, A.T., Müller-Esterl, W., Busse, R. (1997) ACE inhibitor potentiation of bradykinin-induced venoconstriction. Br. J. Pharmacol. 121: 1475-1481.
78. Ufkes, J.G., Aarsen, P.N., van der Meer, C. (1977) The mechanism of action of two bradykinin-potentiating peptides on isolated smooth muscle. Eur. J. Pharmacol. 44: 89-97.
79. Ufkes, J.G., Visser, B.J., Heuver, G., Van der Meer, C. (1978) Structure-activity relationships of bradykinin potentiating peptides. Eur. J. Pharmacol. 50: 119-122.
80. 9 alpha (teprotide). Pharmazie 40 (5): 314-317. (German)
81. 2 bradykinin receptor by ACE inhibitors. J. Biol. Chem. 275: 16110-16118.
82. Filatova, M.P., Krit, N.A., Beschastnaya, N.V., Blokhina, A.V., Kozlova, N.I., Pavlikhina, L.V., Eliseeva, Yu.E., Orekhovich, V.N., Reissmann, S., Paegelow, I. (1985) Synthesis and biological activity of analogs of peptidyl dipeptidase nonapeptide inhibitor. Bioorg. Khim. 11(1): 21-30.
83. Reissmann, S., Filatova, M.P. (1987) Synthesis and biological activity of analogues of the Bradykinin potentiating nonapeptide with substitution of the proline residues. Z. Chem. 27(4): 147-148.
84. th FEBS congress, Part B. Eds. Ovchinnikov, Yu. A., VNU science press, Utrecht (Neth), pp. 449-455.
85. 9. In Proceedings of the Third Symposium Optical Spectroscopy, Teubner Texte zur Physik Band 4, B.G. Teubner Verlagsgesellschaft, Leipzig (DDR).
86. 9α. Peptides 26: 1235-1247.
87. 2 receptor. Eur. J. Pharmacol. 346: 291-298.
88. Ibarra-Rubio, M.E., Pena, J.C., Pedraza-Chaverri, J. (1989) Kinetic and inhibitory characteristics of serum angiotensin-converting enzyme from nine mammalian species. Comp. Biochem. Physiol. 92B: 399-403.
89. Hellberg, S., Sjostrom, M., Wold, S. (1986) The prediction of bradykinin potentiating potency of pentapeptides. An example of a peptide quantitative structure-activity relationship. Acta Chem. Scand. B 40: 135-140.
90. Norinder, U. (1991) Theoretical amino acid descriptors. Application to bradykinin potentiating peptides. Peptides 12: 1223-1227.
91. Lin, Z., Wu, Y., Quan, X., Zhou, Y., Ni, B., Wan, Y. (2003) Use of a novel electrotopological descriptor for the prediction of biological activity of peptide analogues. LIPS 9 (6): 273-281.
92. Cushman, D.W., Cheung, H.S., Sabo, E.F., Ondetti, M.A. (1977) Design of potent competitive inhibitors of angiotensin-converting enzyme. Carboxyalkanoyl and mercaptoalkanoyl amino acids. Biochemistry 16: 5484-5491.
93. Patchett, A.A., Harris, E., Tristram, E.W., Wyvratt, M.J., Wu, M.T., Taub, D., Peterson, E.R., Ikeler, T.J., ten Broeke, J., Payne, L.G., Ondeyka, D.L., Thorsett, E.D., Greenlee, W.J., Lohr, N.S., Hoffsommer, R.D., Joshua, H., Ruyle, W.V., Rothrock, J.W., Aster, S.D., Maycock, A.L., Robinson, P.M., Hirschmann, R., Sweet, C.S., Ulm, E.H., Gross, D.M., Vassil, T.C., Stone, C.A. (1980) A new class of angiotensin-converting enzyme inhibitors. Nature 288: 280-283.
94. Teetz, V., Geiger, R., Henning, R., Urbach, H. (1984) Synthesis of a highly active angiotensin converting enzyme inhibitor: 2-[N-[(S)-1- ethoxycarbonyl-3-phenylpropyl]-L-alanyl]-(1S,3S,5S)-2- azabicyclo[3.3.0]octane- 3-carboxylic acid (Hoe 498). Arzneimittelforschung 34: 1399-1401.
95. Klutchko, S., Blankley, C.J., Fleming, R.W., Hinkley, J.M., Werner, A.E., Nordin, I., Holmes, A., Hoefle, M.L., Cohen, D.M., Essenburg, A.D., et al. (1986) Synthesis of novel angiotensin converting enzyme inhibitor quinapril and related compounds. A divergence of structure-activity relationships for non-sulfhydryl and sulfhydryl types. J. Med. Chem. 29: 1953-1961.
96. Brunner, D.B., Desponds, G., Biollaz, J., Keller, I., Ferber, F., Gavras, H., Brunner, H.R., Schelling, J.L. (1981) Effect of a new angiotensin converting enzyme inhibitor MK 421 and its lysine analogue on the components of the renin system in healthy subjects. Br. J. Clin. Pharmacol. 11: 461-467.
97. 1 receptor? Am. J. Physiol. Heart Circ. Physiol. 285: H277-282.
98. 2 receptor in the rabbit jugular vein: modulation of contractile response to bradykinin. Can. J. Physiol. Pharmacol. 80: 153-163.
99. Ongali, B., Buck Hde, S., Cloutier, F., Legault, F., Regoli, D., Lambert, C., Thibault, G., Couture, R. (2003) Chronic effects of angiotensin-converting enzyme inhibition on kinin receptor binding sites in the rat spinal cord. Am. J. Physiol. Heart Circ. Physiol. 284: H1949-1958.
100. Koehne, P., Schaper, C., Graf, K., Kunkel, G. (1998) Neutral endopeptidase 24.11: its physiologic and possibly pathophysiologic role in inflammation with special effect on respiratory inflammation. Allergy 53: 1023-1042.
101. Skidgel, RA., Erdös, E.G. (2004) Angiotensin converting enzyme (ACE) and neprilysin hydrolyze neuropeptides: a brief history, the beginning and follow-ups to early studies. Peptides 25: 521-525.
102. Molina, H.M., Carmona, A.K., Kouyoumdjian, M., Borges, D.R., Juliano, L. (1996) Liver bradykinin-inactivating-endopeptidase is similar to the metalloendopeptidase (EC 3.4.24.15). Immunopharmacology 32: 176-179.
103. Ryan, J.W., Papapetropoulos, A., Ju, H., Denslow, N.D., Antonov, A., Virmani, R., Kolodgie, F.D., Gerrity, R.G., Catravas, J.D. (1996) Aminopeptidase P is disposed on human endothelial cells. Immunopharmacology 32: 149-152.
104. Papapetropoulos, A., Ryan, J.W., Antonov, A., Virmani, R., Kolodgie, F.D., Gerrity, R.G., Catravas, J.D. (1996) Human aortic endothelial cell aminopeptidase N. Immunopharmacology 32: 153-156.
105. Skidgel, RA., McGwire, G.B., Li, X.Y. (1996) Membrane anchoring and release of carboxypeptidase M: implications for extracellular hydrolysis of peptide hormones. Immunopharmacology 32: 48-52.
106. th American Peptide Symposium. Eds. Fields, G.B., Tam, J.P., Barany, G., Kluwer Academic Publishers, Dordrecht (Neth), pp. 429-430.
107. Maggiora, L.L., Orawski, A.T., Simmons, W.H. (1999) Apstatin analogue inhibitors of aminopeptidase P, a bradykinin-degrading enzyme. J. Med. Chem. 42: 2394-2402.
108. 2 receptor from human fibroblasts. J. Biol. Chem. 271: 32366-32374.
109. 2 receptor requires phosphorylation of three serine and two threonine residues at its carboxyl tail. J. Biol. Chem. 274: 12738-12747.
110. 2 bradykinin receptor. J. Biol. Chem. 279: 31268-31276.
111. Duchene, J., Schanstra, J.P., Pecher, C., Pizard, A., Susini, C., Esteve, J.P., Bascands, J.L., Girolami, J.P. (2002) A novel protein-protein interaction between a G protein-coupled receptor and the phosphatase SHP-2 is involved in bradykinin-induced inhibition of cell proliferation. J. Biol. Chem. 277: 40375-40383.
112. 2 bradykinin receptor complex with enhanced signaling capacity. J. Biol. Chem. 279: 22102-22107.
113. Klinker, J.F., Seifert, R. (1995) Receptor independent activation of G proteins. Pharm. Unserer Zeit 24: 250-263. (German)
114. 2 receptor in agonist-induced receptor dimerization. J. Biol. Chem. 274: 26079-26084.
115. Marcic, B.M., Erdös, E.G. (2000) Protein kinase C and phosphatase inhibitors block the ability of angiotensin I-converting enzyme inhibitors to resensitize the receptor to bradykinin without altering the primary effects of bradykinin. J. Pharmacol. Exp. Ther. 294: 605-612.
116. 2+ influx by Ras and GAP1 in fibroblast cells. Immunopharmacology 45: 7-11.
117. Paegelow, I., Trzeczak, S., Bockmann, S., Vietinghoff, G. (2002) Migratory responses of polymorphonuclear leukocytes to kinin peptides. Pharmacology 66: 153-161.
118. Dendorfer, A., Wagemann, M., Reissmann, S., Dominiak, P. (1999) Structural requirements for B2-agonists with improved degradation stability. Immunopharmacology 45: 199-205.
119. Asano, M., Hatori, C., Sawai, H., Johki, S., Inamura, N., Kayakiri, H., Satoh, S., Abe, Y., Inoue, T., Sawada, Y., Mizutani, T., Oku, T., Nakahara, K. (1998) Pharmacological characterization of a nonpeptide bradykinin B2 receptor antagonist, FR165649, and agonist, FR190997. Br. J. Pharmacol. 124: 441-446.