Advertisement

Pulmonary Endothelial Surface Reductase Kinetics

  • Christopher A. Dawson
  • Robert D. Bongard
  • David L. Roerig
  • Marilyn P. Merker
  • Yoshiyuki Okamoto
  • Said H. Audi
  • Lars E. Olson
  • Gary S. Krenz
  • John H. Linehan

Abstract

The role of the endothelium as a metabolically active organ having a number of regulatory functions is well established. The in vivo evaluation of these functions tends to be a difficult problem, and much of the research in this area is being carried out using simpler systems such as cultured endothelial cells. The results from such studies provide increased motivation for understanding how the various endothelial functions operate in vivo. The multiple-indicator dilution method (MID) is an approach for studying in vivo endothelial cell biology. The lungs are unique with regard to in vivo application of the MID for the study of capillary permeation, cellular transport, and reaction kinetics in that access to a single inlet (e.g., a systemic vein or the pulmonary artery) and single outlet (e.g., a peripheral systemic artery) is more readily available than in any other organ, and the MID has been applied to the in vivo study of these functions of the pulmonary endothelium (13–16, 18, 21, 22). The MID method is suited for studying those processes that occur rapidly enough that their effects can be observed in the time frame of a single pass through the lungs. In general, capillary blood flow tends to be so high in comparison to the rates of endothelial cell utilization of typical substrates for intermediary metabolism that the MID is not applicable to such substrates. However, the pulmonary endothelium also carries out a number of metabolic functions that appear to be directed at modulating blood concentrations of certain substances rather than at the metabolic requirements of the endothelial cells themselves.

Keywords

Methylene Blue Rabbit Lung American Physiological Society Reference Indicator Pulmonary Endothelium 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    Auclair, C., E. Voisin, and H. Banoun. Superoxide dismutase-inhibitable NBT and cytochrome C reduction as probe of superoxide anion production: A reapraisal. In: Oxy Radicals and Their Scavenger Systems, Molecular Aspects, edited by G. Cohen and R.A. Greenwald. New York: Elsevier Science Publishing Co., Inc., Vol. I, 1983, pp. 312–315.Google Scholar
  2. 2.
    Audi, S.H., C.A. Dawson, J.H. Linehan, G.S. Krenz, S.B. Ahlf, and D.L. Roerig. An interpretation of 14C-urea and 14C-primidone extraction in isolated rabbit lungs. Ann Biomed. Eng. 24:337–351, 1996.PubMedCrossRefGoogle Scholar
  3. 3.
    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(3): 1004–1014, 1995.PubMedGoogle Scholar
  4. 4.
    Baggiolini, M., F. Boulay, J.A. Badwey, and J.T. Curnutte. Activation of neutrophil leukocytes: Chemoattractant receptors and respiratory burst. FASEB J. 7:1004–1010, 1993.PubMedGoogle Scholar
  5. 5.
    Bongard, R.D., G.S. Krenz, J.H. Linehan, D.L. Roerig, M.P. Merker, J.L. Widell, and C.A. Dawson. Reduction and accumulation of methylene blue by the lung. J. Appl. Physiol. 77:1480–1491, 1994.PubMedGoogle Scholar
  6. 6.
    Bongard, R.D., M.P. Merker, R. Shundo, Y. Okamoto, D.L. Roerig, J.H. Linehan, and C.A. Dawson. Reduction of thiazine dyes by bovine pulmonary arterial endothelial cells in culture. Am. J. Physiol. 269 (Lung Cell. Mol. Physiol. 13): L78–L84, 1995.PubMedGoogle Scholar
  7. 7.
    Britigan, B.E., T.L. Roeder, and D.M. Shasby. Insight into the nature and site of oxygen-centered free radical generation by endothelial cell monolayers using a novel spin trapping technique. Blood 79:699–707, 1992.PubMedGoogle Scholar
  8. 8.
    Crane, F.L., H. Low, and M.G. Clark. Plasma membrane redox enzymes. In: The Enzymes of Biological Membranes, Second Edition, edited by A.N. Martonosi. New York, London: Plenum Press, Vol. 4, 1985, pp. 465–510.Google Scholar
  9. 9.
    Crane, F.L., I.L. Sun, R. Barr, and H. Low. Electron and proton transport across the plasma membrane. J. Bioenerget. Biomem. 23:773–803, 1991.CrossRefGoogle Scholar
  10. 10.
    Crane, F.L., I.L. Sun, M.G. Clark, C. Grebing, and H. Low. Transplasma-membrane redox systems in growth and development. Biochim. Biophys. Acta. 811:233–264, 1985.PubMedGoogle Scholar
  11. 11.
    Crone, C. The permeability of capillaries in various organs as determined by the use of the indicator diffusion method. Acta Physiol. Scand. 58:292–305, 1963.PubMedCrossRefGoogle Scholar
  12. 12.
    Cross, A.R., O.T.G. Jones, A.M. Harper, and A.W. Segal. Oxidation-reduction properties of the cytochrome b found in the plasma-membrane fraction of human neutrophils. Biochem. Int. 194:599–606, 1981.Google Scholar
  13. 13.
    Dawson, C.A., C.W. Christiansen, D.A. Rickaby, J.H. Linehan, and M.R. Johnston. Lung damage and pulmonary uptake of serotonin in intact dogs. J. Appl. Physiol. 58:1761–1766, 1985, 1985.PubMedGoogle Scholar
  14. 14.
    Dawson, C.A. and J.H. Linehan. Biogenic amines. In: Lung Biology in Health and Disease, edited by D. Massaro. New York: Marcel Dekker, Inc., Vol. 41—Lung Cell Biology, 1989, pp. 1091–1139.Google Scholar
  15. 15.
    Dawson, C.A., D.L. Roerig, and J.H. Linehan. Evaluation of endothelial injury in the human lung. Chest 10:13–24, 1989.Google Scholar
  16. 16.
    Dupuis, J., C. Goresky, and D.J. Stewart. Pulmonary removal and production of endothelin in the anesthetized dog. J. Appl. Physiol. 76:694–700, 1994.PubMedGoogle Scholar
  17. 17.
    Gillis, C.N. Pharmacological aspects of metabolic processes in the pulmonary microcirculation. Ann. Rev. Pharmacol. Toxicol. 26:183–200, 1986.CrossRefGoogle Scholar
  18. 18.
    Gillis, C.N. Pulmonary extraction of PGE1 in the adult respiratory distress syndrome. Am. Rev. Respir. Dis. 137:1–2, 1988.PubMedCrossRefGoogle Scholar
  19. 19.
    Goldenberg, H. Plasma membrane redox activities. Biochim. Biophys. Acta 694:203–223, 1982.PubMedGoogle Scholar
  20. 20.
    Goldenberg, H., F.L. Crane, and J. Morre. NADH oxidoreductase of mouse liver plasma membranes. J. Biol. Chem. 254:2491–2498, 1979.PubMedGoogle Scholar
  21. 21.
    Goresky, C.A., J.W. Warnica, J.H. Gurgess, and B.E. Nadeau. Effect of exercise on dilution estimates of extravascular lung water and on the carbon monoxide diffusing capacity in normal adults. Circulation 37:379–389, 1975.Google Scholar
  22. 22.
    Harris, T.R., R.J. Roselli, C.R. Maurer, R.E. Parker, and N.A. Pou. Comparison of labeled propanediol and urea as markers of lung vascular injury. J. Appl. Physiol. 62:1852–1859, 1987.PubMedGoogle Scholar
  23. 23.
    Kennedy, T.P., N.V. Rao, C. Hopkins, L. Pennington, E. Tolley, and J.R. Hoidal. Role of reactive oxygen species in reperfusion injury of the rabbit lung. J. Clin. Invest. 83:1326–1335, 1989.PubMedCrossRefGoogle Scholar
  24. 24.
    Low, H., F.L. Crane, E.J. Patrick, G.S. Patten, and M.G. Clark. Properties and regulation of trans-plasma membrane redox system of perfused rat heart. Biochim. Biophys. Acta 804:253–260, 1984.PubMedCrossRefGoogle Scholar
  25. 25.
    Merker, M., B. Bongard, J. Linehan, Y. Okamoto, D. Vyprachticky, B.M. Brantmeier, D.L. Roerig and C. Dawson. Pulmonary endothelial thiazine uptake: Separation of cell surface reduction from intracellular reoxidation. Am. J. Physiol. 272 (Lung Cell. Mol. Physiol. 16): L673–L680 (in press), 1997.PubMedGoogle Scholar
  26. 26.
    Morre, D.J., M. Davidson, C. Geilen, J. Lawrence, G. Flesher, R. Crowe, and F.L. Crane. NADH oxidase activity of rat liver plasma membrane activated by guanine nucleotides. Biochem. Int. 292:647–653, 1993.Google Scholar
  27. 27.
    Navas, P., J.M. Villalba, and F. Cordoba. Ascorbate function at the plasma membrane. Biochim. Biophys. Acta 1197:1–13, 1994.PubMedGoogle Scholar
  28. 28.
    Olson, L.E., R.D. Bongard, C.A. Dawson, and J.H. Linehan. On-line detection of reduction and sequestration of thiazine dyes by the lung. FASEB J. 8:A916, 1994.Google Scholar
  29. 29.
    Ravel, P. and F. Lederer. Affinity-labeling of an NADPH-binding site on the heavy subunit of flavocytrochrome b558 in particulate NADPH oxidase from activated human neutrophils. Biochem. Biophys. Res. Commun. 196:543–552, 1993.PubMedCrossRefGoogle Scholar
  30. 30.
    Segal, A.W. and A. Abo. The biochemical basis of the NADPH oxidase of phagocytes. Trends Biochem. Sci. 18:43–47, 1993.PubMedCrossRefGoogle Scholar
  31. 31.
    Sun, I.L., E.E. Sun, F.L. Crane, D.J. Morre, A. Lindgren, and H. Low. Requirement for coenzyme Q in plasma membrane electron transport. Proc. Natl. Acad. Sci. 89:11126–11130, 1992.PubMedCrossRefGoogle Scholar
  32. 32.
    Toole-Simms, W., I.L. Sun, D.J. Morre, and F.L. Crane. Transplasma membrane electron and proton transport is inhibited by chloroquine. Biochemistry 4:761–769, 1990.Google Scholar
  33. 33.
    Villalba, J.M., A. Canalejo, M.I. Buron, F. Cordoba, and P. Navas. Thiol groups are involved in NADH-ascorbate free radical reductase activity of rat liver plasma membrane. Biochem. Biophys. Res. Commun. 192:707–713, 1993.PubMedCrossRefGoogle Scholar
  34. 34.
    Zulueta, J.J., F.-S. Yu, I.A. Hertig, and V.J. Thannickal. Release of hydrogen peroxide in response to hypoxia-reoxygenation: Role of an NAD(P)H oxidase-like enzyme in endothelial cell plasma membrane. Am. J. Respir. Cell Mol. Biol. 12:41–49, 1995.PubMedCrossRefGoogle Scholar
  35. 35.
    Zurbriggen, R. and J.L. Dreyer. An NADH-diaphorase is located at the cell plasma membrane in a mouse neuroblastoma cell line NB41A3. Biochim. Biophys. Acta 1183:513–520, 1994.PubMedCrossRefGoogle Scholar

Copyright information

© Springer-Verlag New York Inc. 1998

Authors and Affiliations

  • Christopher A. Dawson
  • Robert D. Bongard
  • David L. Roerig
  • Marilyn P. Merker
  • Yoshiyuki Okamoto
  • Said H. Audi
  • Lars E. Olson
  • Gary S. Krenz
  • John H. Linehan

There are no affiliations available

Personalised recommendations