Proline in vasoactive peptides: Consequences for peptide hydrolysis in the lung

American Journal of Physiology - Lung Cellular and Molecular Physiology

Volumn 276, Issue 2 20-2, 1999, Pages

  Merker, Marilyn P ^a   Audi, Said H ^b   Brantmeier, Becky M ^b   Nithipatikom, Kasem ^b   Goldman, Robert S ^b   Roerig, David L ^b   Dawson, Christopher A ^b  

^a CLEMENT J ZABLOCKI VETERANS AFFAIRS MEDICAL CENTER   (United States)

^b NONE

Author keywords

Bradykinin; Cis trans isomerase; Cyclophilin; High performance liquid chromatography; Lung peptidases; 6 glycine bradykinin

Indexed keywords

BRADYKININ; CYCLOPHILIN; PEPTIDASE; PEPTIDE; PROLINE;

ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; BIOASSAY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HYDROLYSIS; HYPOTHESIS; ISOMERISM; LUNG PERFUSION; MALE; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; RABBIT; RAT;

EID: 0033062004     PISSN: 10400605     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajplung.1999.276.2.l341     Document Type: Article

References (36)

1. Audi, S. H., J. H. Linehan, G. S. Krenz, C. A. Dawson, S. B. Ahlf, and D. L. Roerig. Estimation of the pulmonary capillary transport function in isolated rabbit lungs. J. Appl. Physiol. 78: 1004-1014, 1995.
2. Audi, S. H., D. P. Schuster, M. P. Merker, R. D. Bongard, J. H. Linehan, and C. A. Dawson. Pulmonary angiotensin converting enzyme ligand binding kinetics (Abstract). FASEB J. 10: A99, 1996.
3. Boppana, V. K., C. Miller-Stein, J. F. Politowski, and G. Rhodes. High-performance liquid chromatographic determination of peptides in biological fluids by automated pre-column fluorescence derivatization with fluorescamine. J. Chromatogr. 548: 319-327, 1991.
4. Campbell, D. J., A. Kladis, and A. M. Duncan. Bradykinin peptides in kidney, blood, and other tissues of the rat. Hypertension 21: 155-165, 1993.
5. Dawson, C. A., R. D. Bongard, D. A. Rickaby, J. H. Linehan, and D. L. Roerig. Effect of transit time on metabolism of a pulmonary endothelial enzyme substrate. Am. J. Physiol. 257 (Heart Circ. Physiol. 26): H853-H865, 1989.
6. Decarie, A., G. Drapeau, J. Closset, R. Couture, and A. Adam. Development of digoxigenin-labeled peptide: application to chemiluminoenzyme immunoassay of bradykinin in inflammed tissues. Peptides 15: 511-518, 1994.
7. Dupuis, J., C. A. Goresky, J. W. Ryan, J. L. Rouleau, and G. G. Bach. Pulmonary angiotensin-converting enzyme substrate hydrolysis during exercise. J. Appl. Physiol. 72: 1868-1886, 1992.
8. Endrich, M. M., and H. Gehring. The V3 loop of human immunodeficiency virus type-1 envelope protein is a high-affinity ligand for immunophilins present in human blood. Eur. J. Biochem. 252: 441-446, 1998.
9. Erdos, E. G., and R. A. Skidgel. The angiotensin I-converting enzyme. Lab. Invest. 56: 345-348, 1987.
10. Ferreira, S. H., and J. R. Vane. The disappearance of bradykinin and eledoisin in the circulation and vascular beds of the cat. Br. J. Pharmacol. Chemother. 30: 417-424, 1967.
11. Fischer, G. Peptidyl-prolyl cis/trans isomerases and their effectors. Angew. Chem. Int. Ed. Engl. 33: 1415-1436, 1994.
12. King, G. K., C. R. Middlehurst, and P. W. Kuchel. Direct NMR evidence that prolidase is specific for the trans isomer of imidopeptide substrates. Biochemistry 25: 1054-1062, 1986.
13. Landaw, E. M., and J. J. I. DiStefano. Multiexponential, multicompartmental, and noncompartmental modeling. II. Data analysis and statistical considerations. Am. J. Physiol. 246 (Regulatory Integrative Comp. Physiol. 15): R665-R677, 1984.
14. Lin, L. N., and J. F. Brandts. Evidence suggesting that some proteolytic enzymes may cleave only the trans form of the peptide bond. Biochemistry 18: 43-47, 1979.
15. Lin, L. N., and J. F. Brandts. Role of cis-trans isomerism of the peptide bond in protease specificity. Kinetic studies on small proline-containing peptides and on polyproline. Biochemistry 18: 5037-5042, 1979.
16. Lin, L. N. and J. F. Brandts. Evidence showing that a proline-specific endopeptidase has an absolute requirement for a trans peptide bond immediately preceding the active bond. Biochemistry 22: 4480-4485, 1983.
17. 6 analog are substrates of cyclophilin: a fluorine-19 magnetization transfer study. Biochemistry 29: 10298-10302, 1990.
18. London, R. E., J. M. Stewart, and J. R. Cann. Probing the role of proline in peptide hormones. NMR studies of bradykinin and related peptides. Biochem. Pharmacol. 40: 41-48, 1990.
19. 1H nuclear magnetic resonance studies of bradykinin and selected peptide fragments. Biochemistry 17: 2270-2277, 1978.
20. 6]-bradykinin. Role of serine in reducing structural heterogeneity. J. Am. Chem. Soc. 101: 2455-2462, 1979.
21. Madden, J. A., C. A. Dawson, and D. R. Harder. Hypoxia induced activation in small isolated pulmonary arteries of the cat. J. Appl. Physiol. 59: 113-118, 1985.
22. Merker, M., and R. E. Handschumacher. Uptake and nature of the intracellular binding of cyclosporin A in a murine thymoma cell line, BW5147. J. Immunol. 132: 1-6, 1984.
23. Merker, M. P., I. M. Armitage, S. H. Audi, L. T. Kakalis, J. H. Linehan, J. R. Maehl, D. L. Roerig, and C. A. Dawson. Impact of angiotensin-converting enzyme substrate conformation on fractional hydrolysis in the lung. Am. J. Physiol. 270 (Lung Cell. Mol. Physiol. 14): L251-L259, 1996.
24. Merker, M. P., and C. A. Dawson. Cyclophilin facilitated bradykinin inactivation in the perfused rat lung. Biochem. Pharmacol. 50: 2085-2091, 1995.
25. Merker, M. P., C. A. Dawson, R. Bongard, D. Roerig, S. Haworth, and J. Linehan. Angiotensin-converting enzyme preferentially hydrolyzes the trans isomer of a proline-containing substrate. J. Appl. Physiol. 75: 1519-1524, 1993.
26. Milnor, W. R. Hemodynamics. Baltimore, MD: Williams and Wilkins, 1982.
27. Prechel, M. M., A. T. Orawski, L. L. Maggiora, and W. H. Simmons. Effect of a new aminopeptidase P inhibitor, apstatin, on bradykinin degradation in the rat lung. J. Pharmacol. Exp. Ther. 275: 1136-1142, 1995.
28. Regoli, D., and J. Barabe. Pharmacology of bradykinin and related kinins. Pharmacol. Rev. 32: 1-46, 1980.
29. Ryffel, B. Cyclosporin binding proteins. Identification, distribution, function and relation to FK binding proteins. Biochem. Pharmacol. 46: 1-12, 1993.
30. Schuster, D. P., T. J. McCarthy, M. J. Welch, S. Holmberg, P. Sandiford, and J. Markham. In vivo measurements of pulmonary angiotensin-converting enzyme kinetics. II. Implementation and application. J. Appl. Physiol. 78: 1169-1178, 1995.
31. Simmons, W. H., and A. T. Orawski. Membrane-bound amino-peptidase P from bovine lung. J. Biol. Chem. 267: 4897-4903, 1992.
32. Skoglof, A., I. Nilsson, S. Gustafsson, J. Deinum, and P. Gothe. Cis-trans isomerization of an angiotensin converting enzyme inhibitor. An enzyme kinetic and nuclear magnetic resonance study. Biochim. Biophys. Acta 1041: 22-30, 1990.
33. Stein, R. L. Mechanism of enzymatic and nonenzymatic prolyl cis-trans isomerization. In: Advances in Protein Chemistry. Accessory Folding Proteins, edited by G. Lorimer. San Diego, CA: Academic, 1993, p. 1-24.
34. Stewart, J. M. Chemistry and biological activity of peptides related to bradykinin. In: Bradykinin, Kallidin and Kallikrein, edited by E. G. Erdos. Berlin, Germany: Springer-Verlag, 1979, p. 227-265.
35. Terragno, N. A., and A. Terragno. Release of vasoactive substances by kinins. In: Bradykinin, Kallidin and Kallikrein, edited by E. G. Erdos. Berlin, Germany: Springer-Verlag, 1979, p. 401-421.
36. Udenfriend, S., S. Stein, P. Bohlen, W. Dairman, W. Leimgruber, and M. Weigele. Fluorescamine: a reagent for assay of amino acids, peptides, proteins, and primary amines in the picomole range. Science 178: 871-872, 1972.