Skip to main content
PMC home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1989 Apr;86(8):2723–2727. doi: 10.1073/pnas.86.8.2723

Direct visualization of the interrelationship between intramembrane and extracellular structures.

J B Wade 1, R A Coleman 1
PMCID: PMC286990  PMID: 2495534

Abstract

The apical surface of the toad urinary bladder is covered by an interconnected mesh of glycocalyx, which appears to attach to the plasma membrane bilayer. To evaluate the interrelationship between these extracellular elements and intramembrane structures, a strategy was devised to produce composite replicas that allow the simultaneous visualization of intramembrane particles by freeze-fracture while the glycocalyx mesh is replicated by rotary shadowing of the extracellular surface after freeze-drying. Evaluation of these composite replicas by electron microscopy reveals that contacts occur between extracellular filamentous elements and intramembrane particles. This structural organization may be important for stabilizing intramembrane components and for anchoring extracellular elements to the membrane.

Full text

PDF
2723

Images in this article

2724Image
on p.2724
2724Image
on p.2724
2725Image
on p.2725
2725Image
on p.2725
2726Image
on p.2726
2726Image
on p.2726

Selected References

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

  1. Almers W., Stirling C. Distribution of transport proteins over animal cell membranes. J Membr Biol. 1984;77(3):169–186. doi: 10.1007/BF01870567. [DOI] [PubMed] [Google Scholar]
  2. Andersson Forsman C., Pinto da Silva P. Fracture-flip: new high-resolution images of cell surfaces after carbon stabilization of freeze-fractured membranes. J Cell Sci. 1988 Aug;90(Pt 4):531–541. doi: 10.1242/jcs.90.4.531. [DOI] [PubMed] [Google Scholar]
  3. Branton D. Fracture faces of frozen membranes. Proc Natl Acad Sci U S A. 1966 May;55(5):1048–1056. doi: 10.1073/pnas.55.5.1048. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Dragsten P. R., Blumenthal R., Handler J. S. Membrane asymmetry in epithelia: is the tight junction a barrier to diffusion in the plasma membrane? Nature. 1981 Dec 24;294(5843):718–722. doi: 10.1038/294718a0. [DOI] [PubMed] [Google Scholar]
  5. Dubois-Dalcq M., Reese T. S. Structural changes in the membrane of vero cells infected with a paramyxovirus. J Cell Biol. 1975 Dec;67(3):551–565. doi: 10.1083/jcb.67.3.551. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Elgsaeter A., Branton D. Intramembrane particle aggregation in erythrocyte ghosts. I. The effects of protein removal. J Cell Biol. 1974 Dec;63(3):1018–1036. doi: 10.1083/jcb.63.3.1018. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Fisher K. A., Yanagimoto K. C. Effect of membrane splitting on transmembrane polypeptides. J Cell Biol. 1986 Feb;102(2):551–559. doi: 10.1083/jcb.102.2.551. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Gluck S., Al-Awqati Q. Vasopressin increases water permeability in inducing pores. Nature. 1980 Apr 17;284(5757):631–632. doi: 10.1038/284631a0. [DOI] [PubMed] [Google Scholar]
  9. Golan D. E., Veatch W. Lateral mobility of band 3 in the human erythrocyte membrane studied by fluorescence photobleaching recovery: evidence for control by cytoskeletal interactions. Proc Natl Acad Sci U S A. 1980 May;77(5):2537–2541. doi: 10.1073/pnas.77.5.2537. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Hartwig J. H., Ausiello D. A., Brown D. Vasopressin-induced changes in the three-dimensional structure of toad bladder apical surface. Am J Physiol. 1987 Nov;253(5 Pt 1):C707–C720. doi: 10.1152/ajpcell.1987.253.5.C707. [DOI] [PubMed] [Google Scholar]
  11. Heuser J. E., Salpeter S. R. Organization of acetylcholine receptors in quick-frozen, deep-etched, and rotary-replicated Torpedo postsynaptic membrane. J Cell Biol. 1979 Jul;82(1):150–173. doi: 10.1083/jcb.82.1.150. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Hirokawa N., Heuser J. E. Quick-freeze, deep-etch visualization of the cytoskeleton beneath surface differentiations of intestinal epithelial cells. J Cell Biol. 1981 Nov;91(2 Pt 1):399–409. doi: 10.1083/jcb.91.2.399. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Hong K., Hubbell W. L. Preparation and properties of phospholipid bilayers containing rhodopsin. Proc Natl Acad Sci U S A. 1972 Sep;69(9):2617–2621. doi: 10.1073/pnas.69.9.2617. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Hynes R. O. Integrins: a family of cell surface receptors. Cell. 1987 Feb 27;48(4):549–554. doi: 10.1016/0092-8674(87)90233-9. [DOI] [PubMed] [Google Scholar]
  15. Jehl B., Bauer R., Dörge A., Rick R. The use of propane/isopentane mixtures for rapid freezing of biological specimens. J Microsc. 1981 Sep;123(Pt 3):307–309. doi: 10.1111/j.1365-2818.1981.tb02475.x. [DOI] [PubMed] [Google Scholar]
  16. Kachadorian W. A., Wade J. B., DiScala V. A. Vasopressin: induced structural change in toad bladder luminal membrane. Science. 1975 Oct 3;190(4209):67–69. doi: 10.1126/science.809840. [DOI] [PubMed] [Google Scholar]
  17. Koppel D. E., Sheetz M. P., Schindler M. Matrix control of protein diffusion in biological membranes. Proc Natl Acad Sci U S A. 1981 Jun;78(6):3576–3580. doi: 10.1073/pnas.78.6.3576. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Lewis S. A. A reinvestigation of the function of the mammalian urinary bladder. Am J Physiol. 1977 Mar;232(3):F187–F195. doi: 10.1152/ajprenal.1977.232.3.F187. [DOI] [PubMed] [Google Scholar]
  19. McCloskey M., Poo M. M. Protein diffusion in cell membranes: some biological implications. Int Rev Cytol. 1984;87:19–81. doi: 10.1016/s0074-7696(08)62439-0. [DOI] [PubMed] [Google Scholar]
  20. Miller K. R., Prescott C. S., Jacobs T. L., Lassignal N. L. Artifacts associated with quick-freezing and freeze-drying. J Ultrastruct Res. 1983 Feb;82(2):123–133. doi: 10.1016/s0022-5320(83)90047-3. [DOI] [PubMed] [Google Scholar]
  21. Parsons C. L., Stauffer C., Schmidt J. D. Bladder-surface glycosaminoglycans: an efficient mechanism of environmental adaptation. Science. 1980 May 9;208(4444):605–607. doi: 10.1126/science.6154316. [DOI] [PubMed] [Google Scholar]
  22. Patel V. P., Lodish H. F. A fibronectin matrix is required for differentiation of murine erythroleukemia cells into reticulocytes. J Cell Biol. 1987 Dec;105(6 Pt 2):3105–3118. doi: 10.1083/jcb.105.6.3105. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Pinto da Silva P., Branton D. Membrane splitting in freeze-ethching. Covalently bound ferritin as a membrane marker. J Cell Biol. 1970 Jun;45(3):598–605. doi: 10.1083/jcb.45.3.598. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Pinto da Silva P., Kan F. W. Label-fracture: a method for high resolution labeling of cell surfaces. J Cell Biol. 1984 Sep;99(3):1156–1161. doi: 10.1083/jcb.99.3.1156. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Rizki T. M., Rizki R. M. Basement membrane polarizes lectin binding sites of Drosophila larval fat body cells. Nature. 1983 May 26;303(5915):340–342. doi: 10.1038/303340a0. [DOI] [PubMed] [Google Scholar]
  26. Wade J. B., DiScala V. A., Karnovsky M. J. Membrane structural specialization of the toad urinary bladder revealed by the freeze-fracture technique. I. The granular cell. J Membr Biol. 1975 Jul 24;22(3-4):385–402. doi: 10.1007/BF01868182. [DOI] [PubMed] [Google Scholar]
  27. Wallace B. G. Aggregating factor from Torpedo electric organ induces patches containing acetylcholine receptors, acetylcholinesterase, and butyrylcholinesterase on cultured myotubes. J Cell Biol. 1986 Mar;102(3):783–794. doi: 10.1083/jcb.102.3.783. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Wier M. L., Edidin M. Effects of cell density and extracellular matrix on the lateral diffusion of major histocompatibility antigens in cultured fibroblasts. J Cell Biol. 1986 Jul;103(1):215–222. doi: 10.1083/jcb.103.1.215. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES