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. 1985 Jul;76(1):93–100. doi: 10.1172/JCI111983

Binding of diamine oxidase activity to rat and guinea pig microvascular endothelial cells. Comparisons with lipoprotein lipase binding.

A Robinson-White, S B Baylin, T Olivecrona, M A Beaven
PMCID: PMC423716  PMID: 3926823

Abstract

Microvascular endothelial cells from rat and guinea pig fat pads were shown to bind diamine oxidase (DAO) activity when incubated with soluble extracts of placenta (33 DAO U/mg of placenta) and a purified placental enzyme preparation (94 U/micrograms of protein). The extent of binding was dependent on the concentration of enzyme activity and tissue. Saturation of binding sites with 5,000 U of DAO/ml resulted in levels of bound activity (up to 11-13 U/mg of endothelial cells) in excess of that observed in all tissues except placenta. Scatchard plots suggested that there were at least two DAO binding sites (apparent Km 92 and 2,450 U/ml). Although the same cell preparations bound 125I-labeled lipoprotein lipase (LPL), the presence of LPL on the endothelial cell surface did not interfere with the binding of DAO activity except when cells were exposed to high concentrations of LPL. Alternatively, bound DAO activity was partially displaced (up to 33%) only with high concentrations (30 micrograms/ml) of LPL. DAO activity may thus be bound to at least two populations of sites, one of which may bind LPL. Both enzymes, however, were displaced by heparin (0.05-5 U/ml) and DAO binding was impaired by prior treatment of cells with proteolytic and glycosaminoglycandegrading enzymes. The demonstration of DAO binding to vascular endothelial cells provides a further example of the ability of these cells to bind enzymes at their surface and thereby act on biologically active substances in the circulation.

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Selected References

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  1. Atkins F. L., Beaven M. A. Ornithine decarboxylase and histaminase (diamine oxidase) activities in rat thymus and their relationship to the thymus lymphocyte. Biochem Pharmacol. 1975 Apr 1;24(7):763–768. doi: 10.1016/0006-2952(75)90117-3. [DOI] [PubMed] [Google Scholar]
  2. Baylin S. B., Beaven M. A., Krauss R. M., Keiser H. R. Response of plasma histaminase activity to small doses of heparin in normal subjects and patients with hyperlipoproteinemia. J Clin Invest. 1973 Aug;52(8):1985–1993. doi: 10.1172/JCI107383. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Baylin S. B. Histaminase (diamine oxidase) activity in human tumors: an expression of a mature genome. Proc Natl Acad Sci U S A. 1977 Mar;74(3):883–887. doi: 10.1073/pnas.74.3.883. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Baylin S. B., Margolis S. Purification of histaminase (diamine oxidase) from human pregnancy plasma by affinity chromatography. Biochim Biophys Acta. 1975 Aug 26;397(2):294–306. doi: 10.1016/0005-2744(75)90119-9. [DOI] [PubMed] [Google Scholar]
  5. Beaven M. A., Marshall J. R., Baylin S. B., Sjoerdsma A. Changes in plasma histaminase activity during normal early human pregnancy and pregnancy disorders. Am J Obstet Gynecol. 1975 Nov 15;123(6):605–609. doi: 10.1016/0002-9378(75)90882-0. [DOI] [PubMed] [Google Scholar]
  6. Beaven M. A., Robinson-White A., Roderick N. B., Kauffman G. L. The demonstration of histamine release in clinical conditions: a review of past and present assay procedures. Klin Wochenschr. 1982 Sep 1;60(17):873–881. doi: 10.1007/BF01716943. [DOI] [PubMed] [Google Scholar]
  7. Beaven M. A., Shaff R. E. Study of the relationship of histaminase and diamine oxidase activities in various rat tissues and plasma by sensitive isotopic assay procedures. Biochem Pharmacol. 1975 May 1;24(9):979–984. doi: 10.1016/0006-2952(75)90431-1. [DOI] [PubMed] [Google Scholar]
  8. Bengtsson G., Olivecrona T., Hök M., Riesenfeld J., Lindahl U. Interaction of lipoprotein lipase with native and modified heparin-like polysaccharides. Biochem J. 1980 Sep 1;189(3):625–633. doi: 10.1042/bj1890625. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Bengtsson G., Olivecrona T. Interaction of lipoprotein lipase with heparin-Sepharose. Evaluation of conditions for affinity binding. Biochem J. 1977 Oct 1;167(1):109–119. doi: 10.1042/bj1670109. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Bengtsson G., Olivecrona T. Lipoprotein lipase: some effects of activator proteins. Eur J Biochem. 1980 May;106(2):549–555. doi: 10.1111/j.1432-1033.1980.tb04602.x. [DOI] [PubMed] [Google Scholar]
  11. Buffoni F. Histaminase and related amine oxidases. Pharmacol Rev. 1966 Dec;18(4):1163–1199. [PubMed] [Google Scholar]
  12. Buonassisi V., Root M. Enzymatic degradation of heparin-related mucopolysaccharides from the surface of endothelial cell cultures. Biochim Biophys Acta. 1975 Mar 14;385(1):1–10. doi: 10.1016/0304-4165(75)90067-7. [DOI] [PubMed] [Google Scholar]
  13. Cheng C. F., Oosta G. M., Bensadoun A., Rosenberg R. D. Binding of lipoprotein lipase to endothelial cells in culture. J Biol Chem. 1981 Dec 25;256(24):12893–12898. [PubMed] [Google Scholar]
  14. Dahlbäck O., Hansson R., Tibbling G., Tryding N. The effect of heparin on diamine oxidase and lipoprotein lipase in human lymph and blood plasma. Scand J Clin Lab Invest. 1968;21(1):17–25. doi: 10.3109/00365516809076972. [DOI] [PubMed] [Google Scholar]
  15. Fielding C. J., Higgins J. M. Lipoprotein lipase: comparative properties of the membrane-supported and solubilized enzyme species. Biochemistry. 1974 Oct 8;13(21):4324–4330. doi: 10.1021/bi00718a013. [DOI] [PubMed] [Google Scholar]
  16. Giertz H., Hahn F. Mechanism of histaminase liberation in guinea pig anaphylaxis. Int Arch Allergy Appl Immunol. 1969;36(1):41–44. doi: 10.1159/000230719. [DOI] [PubMed] [Google Scholar]
  17. Hansson R., Holmberg C. G., Tibbling G., Tryding N., Westling H., Wetterqvist H. Heparin-induced diamine oxidase increase in human blood plasma. Acta Med Scand. 1966 Nov;180(5):533–536. doi: 10.1111/j.0954-6820.1966.tb02866.x. [DOI] [PubMed] [Google Scholar]
  18. Hansson R., Thysell H. Heparin-induced increase of diamine oxidase in lymph and blood plasma of rat, guinea-pig and rabbit. Acta Physiol Scand. 1971 Feb;81(2):208–214. doi: 10.1111/j.1748-1716.1971.tb04893.x. [DOI] [PubMed] [Google Scholar]
  19. Hansson R., Tryding N., Törnqvist A. Diamine oxidase (histaminase) in human pregnancy. The activity of the enzyme in lymph and in blood plasma and the effect of heparin on the latter. Acta Obstet Gynecol Scand. 1969;48(1):8–18. doi: 10.3109/00016346909156622. [DOI] [PubMed] [Google Scholar]
  20. Heimark R. L., Schwartz S. M. Binding of coagulation factors IX and X to the endothelial cell surface. Biochem Biophys Res Commun. 1983 Mar 16;111(2):723–731. doi: 10.1016/0006-291x(83)90365-0. [DOI] [PubMed] [Google Scholar]
  21. Hoyer L. W., De los Santos R. P., Hoyer J. R. Antihemophilic factor antigen. Localization in endothelial cells by immunofluorescent microscopy. J Clin Invest. 1973 Nov;52(11):2737–2744. doi: 10.1172/JCI107469. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Jaffe E. A., Hoyer L. W., Nachman R. L. Synthesis of antihemophilic factor antigen by cultured human endothelial cells. J Clin Invest. 1973 Nov;52(11):2757–2764. doi: 10.1172/JCI107471. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Knott G. D. Mlab--a mathematical modeling tool. Comput Programs Biomed. 1979 Dec;10(3):271–280. doi: 10.1016/0010-468x(79)90075-8. [DOI] [PubMed] [Google Scholar]
  24. Lionetti F. J., Hunt S. M., Lin P. S., Kurtz S. R., Valeri C. R. Preservation of human granulocytes. II. Characteristics of granulocytes obtained by counterflow centrifugation. Transfusion. 1977 Sep-Oct;17(5):465–472. doi: 10.1046/j.1537-2995.1977.17578014585.x. [DOI] [PubMed] [Google Scholar]
  25. Lux G. D., Marton L. J., Baylin S. B. Ornithine decarboxylase is important in intestinal mucosal maturation and recovery from injury in rats. Science. 1980 Oct 10;210(4466):195–198. doi: 10.1126/science.6774420. [DOI] [PubMed] [Google Scholar]
  26. Maudsley D. V., Kobayashi Y. Biosynthesis and metabolism of putrescine in the rat placenta. Biochem Pharmacol. 1977 Jan 15;26(2):121–124. doi: 10.1016/0006-2952(77)90382-3. [DOI] [PubMed] [Google Scholar]
  27. Olivecrona T., Bengtsson G., Marklund S. E., Lindahl U., Hök M. Heparin-lipoprotein lipase interactions. Fed Proc. 1977 Jan;36(1):60–65. [PubMed] [Google Scholar]
  28. Robinson-White A., Beaven M. A. Presence of histamine and histamine-metabolizing enzyme in rat and guinea-pig microvascular endothelial cells. J Pharmacol Exp Ther. 1982 Nov;223(2):440–445. [PubMed] [Google Scholar]
  29. Ryan U. S., Ryan J. W., Whitaker C., Chiu A. Localization of angiotensin converting enzyme (kininase II). II. Immunocytochemistry and immunofluorescence. Tissue Cell. 1976;8(1):125–145. doi: 10.1016/0040-8166(76)90025-2. [DOI] [PubMed] [Google Scholar]
  30. SCHAYER R. W. The metabolism of histamine in various species. Br J Pharmacol Chemother. 1956 Dec;11(4):472–473. doi: 10.1111/j.1476-5381.1956.tb00020.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Shakir K. M., Margolis S., Baylin S. B. Localization of histamine (diamine oxidase) in rat small intestinal mucosa: site of release by heparin. Biochem Pharmacol. 1977 Dec 15;26(24):2343–2347. doi: 10.1016/0006-2952(77)90438-5. [DOI] [PubMed] [Google Scholar]
  32. Shimada K., Gill P. J., Silbert J. E., Douglas W. H., Fanburg B. L. Involvement of cell surface heparin sulfate in the binding of lipoprotein lipase to cultured bovine endothelial cells. J Clin Invest. 1981 Oct;68(4):995–1002. doi: 10.1172/JCI110354. [DOI] [PMC free article] [PubMed] [Google Scholar]
  33. Southren A. L., Calanog A. M., Mishr S., Weingold A. B. Effect of cycloheximide on production of diamine oxidase by the human placenta. J Appl Physiol. 1970 Nov;29(5):684–686. doi: 10.1152/jappl.1970.29.5.684. [DOI] [PubMed] [Google Scholar]
  34. Southren A. L., Weingold A. B., Kobayashi Y., Sherman D. H., Grimaldi R., Gold E. M. Plasma diamine oxidase in pregnancy complicated by diabetes mellitus. Am J Obstet Gynecol. 1968 Aug 1;101(7):899–908. doi: 10.1016/0002-9378(68)90271-8. [DOI] [PubMed] [Google Scholar]
  35. Tryding N., Willert B. Determination of plasma diamine oxidase (histaminase) in clinical practice. A comparison between a biological method and a radiochemical micromethod. Scand J Clin Lab Invest. 1968;22(1):29–32. doi: 10.3109/00365516809160732. [DOI] [PubMed] [Google Scholar]
  36. Wallinder L., Peterson J., Olivecrona T., Bengtsson-Olivecrona G. Hepatic and extrahepatic uptake of intravenously injected lipoprotein lipase. Biochim Biophys Acta. 1984 Oct 4;795(3):513–524. doi: 10.1016/0005-2760(84)90181-4. [DOI] [PubMed] [Google Scholar]
  37. ZELLER E. A. IDENTITY OF HISTAMINASE AND DIAMINE OXIDASE. Fed Proc. 1965 May-Jun;24:766–768. [PubMed] [Google Scholar]

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