Skip to main content
PMC home page
The Journal of Cell Biology logoLink to The Journal of Cell Biology
. 1974 Oct 1;63(1):215–226. doi: 10.1083/jcb.63.1.215

POTASSIUM AND AMINO ACID TRANSPORT IN HUMAN LEUKOCYTES EXPOSED TO PHAGOCYTIC STIMULI

Philip B Dunham 1, Ira M Goldstein 1, Gerald Weissmann 1
PMCID: PMC2109341  PMID: 4424263

Abstract

Influxes of potassium and amino acids were measured in suspensions of human polymorphonuclear leukocytes (PMNs) under resting conditions and after various phagocytic stimuli. Both ouabain-sensitive (or pump) and ouabain-insensitive (or leak) influxes of K were determined. In 5 mM external K, mean total K influx was 0.69 nmol/106 cells x min, of which 52% was ouabain-sensitive. Ouabain binding was irreversible, and, as in erythrocytes, was inhibited by K. At external concentrations of 0.1 mM, influxes of lysine and leucine were entirely carrier-mediated, with means of 0.021 nmol/106 cells x min, and 0.019 nmol/106 cells x min, respectively. After incubation of PMNs with zymosan or latex particles, the K pump was reduced more than 60%, whereas amino acid influxes were inhibited only by 30%. PMNs were also exposed to cytochalasin B before challenge by particles: the drug prevented phagocytosis but not surface binding of zymosan, nor did it influence transport of K or amino acids. After pretreatment of PMNs with cytochalasin B, interaction of zymosan with their surface resulted in the same degree of inhibition of influxes of K and amino acids as when the cells were permitted to phagocytose the particles. In contrast, exposure of PMN to latex particles, which do not bind to cytochalasin B-treated cells, after pretreatment of cells with cytochalasin B did not result in inhibition of influxes. Treatment of cells with colchicine had no effect on either membrane transport or its inhibition after exposure to various phagocytic stimuli. These results indicate that the surface membranes of PMNs are functionally heterogeneous with respect to the association of transport sites for the different solutes. Moreover, loss of specific membrane functions from phagocytosing cells may result from the surface-at-tachment phase of particle-cell interactions, since the interactions of zymosan particles with PMNs in the absence of phagocytosis also inhibited transport of solutes.

Full Text

The Full Text of this article is available as a PDF (845.7 KB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. BARON D. N., ROBERTS P. M. The sodium, potassium and water content of isolated normal human leucocytes. J Physiol. 1963 Feb;165:219–226. doi: 10.1113/jphysiol.1963.sp007053. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. BERLIN R. D., WOOD W. B., Jr STUDIES ON THE PATHOGENESIS OF FEVER. XII. ELECTROLYTIC FACTORYS INFLUENCING THE RELEASE OF ENDOGENOUS PYROGEN FROM POLYMORPHONUCLEAR LEUKOCYTES. J Exp Med. 1964 May 1;119:697–714. doi: 10.1084/jem.119.5.697. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Baron D. N., Ahmed S. A. Intracellular concentrations of water and of the principal electrolytes determined by analysis of isolated human leucocytes. Clin Sci. 1969 Aug;37(1):205–219. [PubMed] [Google Scholar]
  4. Berry R. W., Shelanski M. L. Interactions of tubulin with vinblastine and guanosine triphosphate. J Mol Biol. 1972 Oct 28;71(1):71–80. doi: 10.1016/0022-2836(72)90401-9. [DOI] [PubMed] [Google Scholar]
  5. Böyum A. Isolation of mononuclear cells and granulocytes from human blood. Isolation of monuclear cells by one centrifugation, and of granulocytes by combining centrifugation and sedimentation at 1 g. Scand J Clin Lab Invest Suppl. 1968;97:77–89. [PubMed] [Google Scholar]
  6. Cividalli G., Nathan D. G. Sodium and potassium concentration and transmembrane fluxes in leukocytes. Blood. 1974 Jun;43(6):861–869. [PubMed] [Google Scholar]
  7. Dunham P. B., Gunn R. B. Adenosine triphosphatase and active cation transport in red blood cell membranes. Arch Intern Med. 1972 Feb;129(2):241–247. [PubMed] [Google Scholar]
  8. Dunham P. B., Hoffman J. F. Active cation transport and ouabain binding in high potassium and low potassium red blood cells of sheep. J Gen Physiol. 1971 Jul;58(1):94–116. doi: 10.1085/jgp.58.1.94. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. GLYNN I. M. Sodium and potassium movements in human red cells. J Physiol. 1956 Nov 28;134(2):278–310. doi: 10.1113/jphysiol.1956.sp005643. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Hempling H. G. Heats of activation for the exosmotic flow of water across the membrane of leucocytes and leukemic cells. J Cell Physiol. 1973 Feb;81(1):1–9. doi: 10.1002/jcp.1040810102. [DOI] [PubMed] [Google Scholar]
  11. Henson P. M. Interaction of cells with immune complexes: adherence, release of constituents, and tissue injury. J Exp Med. 1971 Sep 1;134(3 Pt 2):114s–135s. [PubMed] [Google Scholar]
  12. Hoffman J. F., Kregenow F. M. The characterization of new energy dependent cation transport processes in red blood cells. Ann N Y Acad Sci. 1966 Jul 14;137(2):566–576. doi: 10.1111/j.1749-6632.1966.tb50182.x. [DOI] [PubMed] [Google Scholar]
  13. Johnston R. B., Jr, Newman S. L., Struth A. G. An abnormality of the alternate pathway of complement activation in sickle-cell disease. N Engl J Med. 1973 Apr 19;288(16):803–808. doi: 10.1056/NEJM197304192881601. [DOI] [PubMed] [Google Scholar]
  14. Lay W. H., Nussenzweig V. Receptors for complement of leukocytes. J Exp Med. 1968 Nov 1;128(5):991–1009. doi: 10.1084/jem.128.5.991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Lichtman M. A., Weed R. I. The monovalent cation content and adenosine triphosphatase activity of human normal and leukemic granulocytes and lymphocytes: relationship to cell volume and morphologic age. Blood. 1969 Nov;34(5):645–660. [PubMed] [Google Scholar]
  16. Oliver J. M., Ukena T. E., Berlin R. D. Effects of phagocytosis and colchicine on the distribution of lectin-binding sites on cell surfaces. Proc Natl Acad Sci U S A. 1974 Feb;71(2):394–398. doi: 10.1073/pnas.71.2.394. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Reaven E. P., Axline S. G. Subplasmalemmal microfilaments and microtubules in resting and phagocytizing cultivated macrophages. J Cell Biol. 1973 Oct;59(1):12–27. doi: 10.1083/jcb.59.1.12. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. SBARRA A. J., KARNOVSKY M. L. The biochemical basis of phagocytosis. I. Metabolic changes during the ingestion of particles by polymorphonuclear leukocytes. J Biol Chem. 1959 Jun;234(6):1355–1362. [PubMed] [Google Scholar]
  19. Sachs J. R. Ouabain-insensitive sodium movements in the human red blood cell. J Gen Physiol. 1971 Mar;57(3):259–282. doi: 10.1085/jgp.57.3.259. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Skeel R. T., Yankee R. A., Spivak W. A., Novikovs L., Henderson E. S. Leukocyte preservation. I. Phagocytic stimulation of the hexose monophosphate shunt as a measure of cell viability. J Lab Clin Med. 1969 Feb;73(2):327–337. [PubMed] [Google Scholar]
  21. Tsan M. F., Berlin R. D. Effect of phagocytosis on membrane transport of nonelectrolytes. J Exp Med. 1971 Oct 1;134(4):1016–1035. doi: 10.1084/jem.134.4.1016. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Ukena T. E., Berlin R. D. Effect of colchicine and vinblastine on the topographical separation of membrane functions. J Exp Med. 1972 Jul 1;136(1):1–7. doi: 10.1084/jem.136.1.1. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Van Oss C. J., Stinson M. W. Immunoglobulins as aspecific opsonins. I. The influence of polyclonal and monoclonal immunoglobulins on the in vitro phagocytosis of latex particles and Staphylococci by human neutrophils. J Reticuloendothel Soc. 1970 Nov;8(5):397–406. [PubMed] [Google Scholar]
  24. Weisenberg R. C., Borisy G. G., Taylor E. W. The colchicine-binding protein of mammalian brain and its relation to microtubules. Biochemistry. 1968 Dec;7(12):4466–4479. doi: 10.1021/bi00852a043. [DOI] [PubMed] [Google Scholar]
  25. Weissmann G., Zurier R. B., Spieler P. J., Goldstein I. M. Mechanisms of lysosomal enzyme release from leukocytes exposed to immune complexes and other particles. J Exp Med. 1971 Sep 1;134(3):149–165. [PMC free article] [PubMed] [Google Scholar]
  26. Winkelstein J. A., Shin H. S., Wood W. B., Jr Heat labile opsonins to Pneumococcus. 3. The participation of immunoglobulin and of the alternate pathway of C3 activation. J Immunol. 1972 Jun;108(6):1681–1689. [PubMed] [Google Scholar]
  27. Zigmond S. H., Hirsch J. G. Cytochalasin B: inhibition of D-2-deoxyglucose transport into leukocytes and fibroblasts. Science. 1972 Jun 30;176(4042):1432–1434. doi: 10.1126/science.176.4042.1432. [DOI] [PubMed] [Google Scholar]
  28. Zurier R. B., Hoffstein S., Weissmann G. Cytochalasin B: effect on lysosomal enzyme release from human leukocytes. Proc Natl Acad Sci U S A. 1973 Mar;70(3):844–848. doi: 10.1073/pnas.70.3.844. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from The Journal of Cell Biology are provided here courtesy of The Rockefeller University Press

RESOURCES