Skip to main content
PMC home page
The Journal of Cell Biology logoLink to The Journal of Cell Biology
. 1981 Nov 1;91(2):524–530. doi: 10.1083/jcb.91.2.524

Effects of cytochalasin B on membrane-associated microfilaments in a cell-free system

PMCID: PMC2111989  PMID: 7198127

Abstract

The mode of action of cytochalasin B was examined in vitro using bile canaliculus-enriched plasma membrane fractions isolated from rat liver. The pericanalicular microfilaments, which are mainly actin filaments and which are normally attached to the canalicular membranes, were dissociated from the membranes by cytochalasin B treatment. A microfilamentous network was found in the supernate of the cytochalasin B treatment. A microfilamentous network was found in the supernate of the cytochalasin-treated specimens and a number of polypeptides, of which a polypeptide corresponding in molecular weight to actin was a notable member. These results suggest that actin filaments become detached from the canaliculus membranes by cytochalasin B.

Full Text

The Full Text of this article is available as a PDF (470.7 KB).

Selected References

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

  1. Berlin R. D., Oliver J. M., Ukena T. E., Yin H. H. The cell surface. N Engl J Med. 1975 Mar 6;292(10):515–520. doi: 10.1056/NEJM197503062921007. [DOI] [PubMed] [Google Scholar]
  2. Brenner S. L., Korn E. D. Substoichiometric concentrations of cytochalasin D inhibit actin polymerization. Additional evidence for an F-actin treadmill. J Biol Chem. 1979 Oct 25;254(20):9982–9985. [PubMed] [Google Scholar]
  3. Brown S. S., Spudich J. A. Cytochalasin inhibits the rate of elongation of actin filament fragments. J Cell Biol. 1979 Dec;83(3):657–662. doi: 10.1083/jcb.83.3.657. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Clarke M., Spudich J. A. Nonmuscle contractile proteins: the role of actin and myosin in cell motility and shape determination. Annu Rev Biochem. 1977;46:797–822. doi: 10.1146/annurev.bi.46.070177.004053. [DOI] [PubMed] [Google Scholar]
  5. Edelman G. M., Yahara I., Wang J. L. Receptor mobility and receptor-cytoplasmic interactions in lymphocytes. Proc Natl Acad Sci U S A. 1973 May;70(5):1442–1446. doi: 10.1073/pnas.70.5.1442. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Fisher M. M., Bloxam D. L., Oda M., Phillips M. J., Yousef I. M. Characterization of rat liver cell plasma membranes. Proc Soc Exp Biol Med. 1975 Oct;150(1):177–184. doi: 10.3181/00379727-150-38998. [DOI] [PubMed] [Google Scholar]
  7. French S. W., Davies P. L. Ultrastructural localization of actin-like filaments in rat hepatocytes. Gastroenterology. 1975 Apr;68(4 Pt 1):765–774. [PubMed] [Google Scholar]
  8. Gabbiani G., Montesano R., Tuchweber B., Salas M., Orci L. Phalloidin-induced hyperplasia of actin filaments in rat hepatocytes. Lab Invest. 1975 Nov;33(5):562–569. [PubMed] [Google Scholar]
  9. Govindan V. M., Wieland T. Isolation and identification of an actin from rat liver. FEBS Lett. 1975 Nov 1;59(1):117–119. doi: 10.1016/0014-5793(75)80354-1. [DOI] [PubMed] [Google Scholar]
  10. Hartwig J. H., Stossel T. P. Cytochalasin B and the structure of actin gels. J Mol Biol. 1979 Nov 5;134(3):539–553. doi: 10.1016/0022-2836(79)90366-8. [DOI] [PubMed] [Google Scholar]
  11. Hartwig J. H., Stossel T. P. Interactions of actin, myosin, and an actin-binding protein of rabbit pulmonary macrophages. III. Effects of cytochalasin B. J Cell Biol. 1976 Oct;71(1):295–303. doi: 10.1083/jcb.71.1.295. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Holborow E. J., Trenchev P. S., Dorling J., Webb J. Demostration of smooth muscle contractile protein antigens in liver and epithelial cells. Ann N Y Acad Sci. 1975 Jun 30;254:489–504. doi: 10.1111/j.1749-6632.1975.tb29196.x. [DOI] [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. Lin D. C., Lin S. Actin polymerization induced by a motility-related high-affinity cytochalasin binding complex from human erythrocyte membrane. Proc Natl Acad Sci U S A. 1979 May;76(5):2345–2349. doi: 10.1073/pnas.76.5.2345. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Lin D. C., Tobin K. D., Grumet M., Lin S. Cytochalasins inhibit nuclei-induced actin polymerization by blocking filament elongation. J Cell Biol. 1980 Feb;84(2):455–460. doi: 10.1083/jcb.84.2.455. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. MacLean-Fletcher S., Pollard T. D. Mechanism of action of cytochalasin B on actin. Cell. 1980 Jun;20(2):329–341. doi: 10.1016/0092-8674(80)90619-4. [DOI] [PubMed] [Google Scholar]
  17. Manasek F. J., Burnside B., Stroman J. The sensitivity of developing cardiac myofibrils to cytochalasin-B (electron microscopy-polarized light-Z-bands-heartbeat). Proc Natl Acad Sci U S A. 1972 Feb;69(2):308–312. doi: 10.1073/pnas.69.2.308. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Miranda A. F., Godman G. C., Deitch A. D., Tanenbaum S. W. Action of cytochalasin D on cells of established lines. I. Early events. J Cell Biol. 1974 May;61(2):481–500. doi: 10.1083/jcb.61.2.481. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Oda M., Price V. M., Fisher M. M., Phillips M. J. Ultrastructure of bile canaliculi, with special reference to the surface coat and the pericanalicular web. Lab Invest. 1974 Oct;31(4):314–323. [PubMed] [Google Scholar]
  20. Oshio C., Phillips M. J. Contractility of bile canaliculi: implications for liver function. Science. 1981 May 29;212(4498):1041–1042. doi: 10.1126/science.7015506. [DOI] [PubMed] [Google Scholar]
  21. Phillips M. J., Oda M., Mak E., Fisher M. M., Jeejeebhoy K. N. Microfilament dysfunction as a possible cause of intrahepatic cholestasis. Gastroenterology. 1975 Jul;69(1):48–58. [PubMed] [Google Scholar]
  22. Pollard T. D. Cytoskeletal functions of cytoplasmic contractile proteins. J Supramol Struct. 1976;5(3):317–334. doi: 10.1002/jss.400050306. [DOI] [PubMed] [Google Scholar]
  23. Pollard T. D., Weihing R. R. Actin and myosin and cell movement. CRC Crit Rev Biochem. 1974 Jan;2(1):1–65. doi: 10.3109/10409237409105443. [DOI] [PubMed] [Google Scholar]
  24. Song C. S., Rubin W., Rifkind A. B., Kappas A. Plasma membranes of the rat liver. Isolation and enzymatic characterization of a fraction rich in bile canaliculi. J Cell Biol. 1969 Apr;41(1):124–132. doi: 10.1083/jcb.41.1.124. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Spooner B. S., Yamada K. M., Wessells N. K. Microfilaments and cell locomotion. J Cell Biol. 1971 Jun;49(3):595–613. doi: 10.1083/jcb.49.3.595. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Spudich J. A., Watt S. The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin. J Biol Chem. 1971 Aug 10;246(15):4866–4871. [PubMed] [Google Scholar]
  27. Steck T. L. The organization of proteins in the human red blood cell membrane. A review. J Cell Biol. 1974 Jul;62(1):1–19. doi: 10.1083/jcb.62.1.1. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Weihing R. R. Cytochalasin B inhibits actin-related gelation of HeLa cell extracts. J Cell Biol. 1976 Oct;71(1):303–307. doi: 10.1083/jcb.71.1.303. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Yousef I. M., Murray R. K. Studies on the preparation of rat liver plasma membrane fractions and on their polypeptide patterns. Can J Biochem. 1978 Jul;56(7):713–721. doi: 10.1139/o78-107. [DOI] [PubMed] [Google Scholar]

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

RESOURCES