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. 1985 Feb 1;225(3):807–814. doi: 10.1042/bj2250807

Redistribution of membrane-bound and cytosolic action in rabbit polymorphonuclear leucocytes during phagocytosis.

D I Stewart, N Crawford
PMCID: PMC1144657  PMID: 2983683

Abstract

In the analysis of highly purified surface membrane from both resting and phagocytosing neutrophils an increase in the surface membrane associated actin has been demonstrated. This change at the cell periphery is associated with a coincident increase in the F-actin content of the cells following stimulation of the cells by exposure to opsonized Oil Red O droplets. The actin which is newly associated with the surface membrane of the phagocytosing cells was more susceptible to removal by detergent than the membrane-associated actin in resting cells and it was also noted that the F-actin associated with phagosomes was readily disrupted by detergent. A redistribution of the surface membrane glycoprotein 5'-nucleotidase was observed during phagocytosis, but no change in distribution of a 125I-labelled Lens culinaris lectin was observed during the entire phagocytic process.

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Selected References

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  1. Avruch J., Wallach D. F. Preparation and properties of plasma membrane and endoplasmic reticulum fragments from isolated rat fat cells. Biochim Biophys Acta. 1971 Apr 13;233(2):334–347. doi: 10.1016/0005-2736(71)90331-2. [DOI] [PubMed] [Google Scholar]
  2. Berlin R. D., Oliver J. M. Analogous ultrastructure and surface properties during capping and phagocytosis in leukocytes. J Cell Biol. 1978 Jun;77(3):789–804. doi: 10.1083/jcb.77.3.789. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Besterman J. M., Low R. B. Endocytosis: a review of mechanisms and plasma membrane dynamics. Biochem J. 1983 Jan 15;210(1):1–13. doi: 10.1042/bj2100001. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Blackburn M. J., Andrews T. M., Watts R. W. Measurement of DNA in isolated granulocytes by the ethidium technique. Anal Biochem. 1973 Jan;51(1):1–10. doi: 10.1016/0003-2697(73)90446-6. [DOI] [PubMed] [Google Scholar]
  5. Blikstad I., Markey F., Carlsson L., Persson T., Lindberg U. Selective assay of monomeric and filamentous actin in cell extracts, using inhibition of deoxyribonuclease I. Cell. 1978 Nov;15(3):935–943. doi: 10.1016/0092-8674(78)90277-5. [DOI] [PubMed] [Google Scholar]
  6. Boxer L. A., Hedley-Whyte E. T., Stossel T. P. Neutrophil action dysfunction and abnormal neutrophil behavior. N Engl J Med. 1974 Nov 21;291(21):1093–1099. doi: 10.1056/NEJM197411212912101. [DOI] [PubMed] [Google Scholar]
  7. Carraway K. L., Doss R. C., Huggins J. W., Chesnut R. W., Carraway C. A. Effects of cytoskeletal perturbant drugs on ecto 5'-nucleotidase, a concanavalin A receptor. J Cell Biol. 1979 Dec;83(3):529–543. doi: 10.1083/jcb.83.3.529. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Chaponnier C., Borgia R., Rungger-Brändle E., Weil R., Gabbiani G. An actin-destabilizing factor is present in human plasma. Experientia. 1979 Aug 15;35(8):1039–1041. doi: 10.1007/BF01949928. [DOI] [PubMed] [Google Scholar]
  9. Fernley H. N., Walker P. G. Kinetic behaviour of calf-intestinal alkaline phosphatase with 4-methylumbelliferyl phosphate. Biochem J. 1965 Oct;97(1):95–103. doi: 10.1042/bj0970095. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Gruenstein E., Rich A., Weihing R. R. Actin associated with membranes from 3T3 mouse fibroblast and HeLa cells. J Cell Biol. 1975 Jan;64(1):223–234. doi: 10.1083/jcb.64.1.223. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Harris H. E., Weeds A. G. Platelet actin: sub-cellular distribution and association with profilin. FEBS Lett. 1978 Jun 1;90(1):84–88. doi: 10.1016/0014-5793(78)80303-2. [DOI] [PubMed] [Google Scholar]
  12. Hällgren R., Sjöström P., Bill A. The uptake of IgG and IgM coated sheep erythrocytes in perfused rabbit liver. Immunology. 1978 Feb;34(2):347–351. [PMC free article] [PubMed] [Google Scholar]
  13. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  14. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  15. Lind S. E., Yin H. L., Stossel T. P. Human platelets contain gelsolin. A regulator of actin filament length. J Clin Invest. 1982 Jun;69(6):1384–1387. doi: 10.1172/JCI110578. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Mannherz H. G., Magener M. Concanavalin A inhibits the interaction of snake venom 5'-nucleotidase and actin. FEBS Lett. 1979 Jul 1;103(1):77–80. doi: 10.1016/0014-5793(79)81253-3. [DOI] [PubMed] [Google Scholar]
  17. Menashi S., Weintroub H., Crawford N. Characterization of human platelet surface and intracellular membranes isolated by free flow electrophoresis. J Biol Chem. 1981 Apr 25;256(8):4095–4101. [PubMed] [Google Scholar]
  18. Mescher M. F., Jose M. J., Balk S. P. Actin-containing matrix associated with the plasma membrane of murine tumour and lymphoid cells. Nature. 1981 Jan 15;289(5794):139–144. doi: 10.1038/289139a0. [DOI] [PubMed] [Google Scholar]
  19. Michell R. H., Pancake S. J., Noseworthy J., Karnovsky M. L. Measurement of rates of phagocytosis: the use of cellular monolayers. J Cell Biol. 1969 Jan;40(1):216–224. doi: 10.1083/jcb.40.1.216. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. 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]
  21. Silverstein S. C., Steinman R. M., Cohn Z. A. Endocytosis. Annu Rev Biochem. 1977;46:669–722. doi: 10.1146/annurev.bi.46.070177.003321. [DOI] [PubMed] [Google Scholar]
  22. Stewart D. I., Crawford N. The isolation of a purified plasma membrane fraction from rabbit peritoneal leucocytes by reversible adhesion to nylon fibres. FEBS Lett. 1981 Apr 20;126(2):175–179. doi: 10.1016/0014-5793(81)80235-9. [DOI] [PubMed] [Google Scholar]
  23. Stewart D. I., Emes C. H., Crawford N. Preparation of a highly purified surface membrane fraction from rabbit polymorphonuclear leucocytes by high-voltage free-flow electrophoresis. Biochim Biophys Acta. 1983 Aug 24;733(1):154–162. doi: 10.1016/0005-2736(83)90101-3. [DOI] [PubMed] [Google Scholar]
  24. Stossel T. P., Mason R. J., Hartwig J., Vaughan M. Quantitative studies of phagocytosis by polymorphonuclear leukocytes: use of emulsions to measure the initial rate of phagocytosis. J Clin Invest. 1972 Mar;51(3):615–624. doi: 10.1172/JCI106851. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Weeds A. Actin-binding proteins--regulators of cell architecture and motility. Nature. 1982 Apr 29;296(5860):811–816. doi: 10.1038/296811a0. [DOI] [PubMed] [Google Scholar]

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