Cytoskeletal Networks and Osmotic Pressure in Relation to Cell Structure and Motility

  • Paul A. Janmey
  • C. Casey Cunningham
  • George F. Oster
  • Thomas P. Stossel
Part of the NATO ASI Series book series (volume 64)


The motility of many cell types proceeds sporadically, by a sequence of propulsive and contractile movements. These movements appear to be controlled by proteins acting upon the actin cytoskeletal network which induce gel-sol transformations in specific regions of the cytoplasm. However, the forces that actually drive these cytoplasmic motions remain obscure; indeed there may be several force generating systems which dominate different types of motile events. For example, directed locomotion may involve the same direct mechanochemical coupling as occurs within muscles, in conjunction with other forces such as membrane bending, gel swelling and elasticity, or osmotic and hydrostatic pressures. In this chapter we will review the elastic properties of cytoskeletal protein networks. It is these networks that provide elastic resistance to cell deformation, and whose rearrangement may allow directed motion in response to externally or internally generated forces.


Osmotic Pressure Actin Filament Actin Polymerization Actin Network Cytoskeletal Network 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Bray D, Money N, Harold F and Bamburg J (1991) Responses of growth cones to changes in osmolality of the surrounding medium. J Cell Sci 98:507–515PubMedGoogle Scholar
  2. Cortese JD, Schwab B 3rd, Frieden C and Elson EL (1989) Actin polymerization induces a shape change in actin-containing vesicles. Proc Natl Acad Sei USA 86:5773–7CrossRefGoogle Scholar
  3. Cunningham C, Stossel T and Kwiatkowski D (1991a) Enhanced motility in NIH 3T3 fibroblasts that overexpress gelsolin. Science 251:1233–1236PubMedCrossRefGoogle Scholar
  4. Cunningham, CC, et al. (1991b) manuscript submittedGoogle Scholar
  5. deGennes PG (1976) Dynamics of entangled polymer solutions. I. The Rouse model. Macromolecules 9:587–593CrossRefGoogle Scholar
  6. Elson EL (1988) Cellular mechanics as an indicator of cytoskeletal structure and function. Annu Rev Biophys Biophys Chem 17:397–430PubMedCrossRefGoogle Scholar
  7. Felder S and Elson E (1990) Mechanics of fibroblast locomotion: Quantitative analysis of forces and motions at the leading lamellas of fibroblasts. J Cell Biol 111:2513–2526PubMedCrossRefGoogle Scholar
  8. Gallez D and Coakley W (1986) Interfacial instability at cell membranes. Prog Biophys Molec Biol 48:155–199CrossRefGoogle Scholar
  9. Hartwig J and Kwiatkowski D (1991) Actin-binding proteins. Curr Op Cell Biol 3:87–97PubMedCrossRefGoogle Scholar
  10. Hartwig JH and Stossel TP (1981) The structure of actin-binding protein molecules in solution and interaction with actin filaments. J Mol Biol 145:563–581PubMedCrossRefGoogle Scholar
  11. Ito T, Zaner KS and Stossel TP (1987) Nonideality of volume flows and phase transitions of F-actin solutions in response to osmotic stress. Biophys J 51:745–53PubMedCrossRefGoogle Scholar
  12. Janmey P, Euteneuer U, Traub P and Schliwa M (1991) Viscoelastic properties of vimentin compared with other filamentous biopolymer networks. J Cell Biol 113:155–160PubMedCrossRefGoogle Scholar
  13. Janmey P (1991) A torsion pendulum for measurement of the viscoelastic properties of biopolymers and its application to actin networks. J Biochem Biophys Meth 22:41–53PubMedCrossRefGoogle Scholar
  14. Janmey PA, Hvidt S, Lamb J and Stossel TP (1990) ABP-actin gels resemble covalently crosslinked networks. Nature 345:89–92PubMedCrossRefGoogle Scholar
  15. Janmey PA, Hvidt S, Peetermans J, Lamb J, Ferry JD and Stossel TP (1988) Viscoelasticity of F-actin and F-actin/gelsolin complexes. Biochemistry 27:8218–27PubMedCrossRefGoogle Scholar
  16. Janmey PA, Peetermans J, Zaner KS, Stossel TP and Tanaka T (1986) Structure and mobility of actin filaments as measured by quasielastic light scattering, viscometry, and electron microscopy. J Biol Chem 261:8357–8362 Kokufata E, Zhang Y-Q and Tanaka T (1991) Saccharide-sensitive phase transition of a lectin-loaded gel. Nature 351:302–304Google Scholar
  17. Llerenas E and Cid M (1985) The molecular interaction between F-actin and lecithin in a phospholipid monolayer system. Bol Estud Med Biol Mex 33:33–39Google Scholar
  18. Mozzarelli A, Hofrichter J and Eaton W (1987) Delay time of hemoglobin S polymerization prevents most cells from sickling in vivo. Science 237:500–506PubMedCrossRefGoogle Scholar
  19. Odell, G. P. Janmey, G. Oster (1991). Actin polymerization and filopodial protrusion, (to appear)Google Scholar
  20. Oster G (1988) Biophysics of the leading lamella. Cell Motil. Cytoskel. 10:164–171CrossRefGoogle Scholar
  21. Oster, G., L. Cheng, H.-P.H. Moore A. Perelson (1989). Vesicle formation in the Golgi apparatus. J. Theo. Biol. 141:463–504.CrossRefGoogle Scholar
  22. Oster G, Perelson A and Tilney L (1982) A mechanical model for acrosomal extension in Thyone. J Math Biol 15:259–265CrossRefGoogle Scholar
  23. Oster G and Perleson A (1987) The physics of cell motility. J Cell Sci Suppl 8:35–54PubMedGoogle Scholar
  24. Pollard TD and Cooper JA (1986) Actin and actin-binding proteins. Ann Rev Biochem 55:987–1035PubMedCrossRefGoogle Scholar
  25. Stossel TP, Chaponnier C, Ezzell RM, Hartwig JH, Janmey PA, Kwiatkowski DJ, Lind SE, Smith DB, Southwick FS, Yin HL and Zaner KS (1985) Non-muscle actin-binding proteins. Ann Rev Cell Biol 1:353–402PubMedCrossRefGoogle Scholar
  26. Suzuki A, Yamazaki M and Ito T (1989) Osmoelastic coupling in biological structures: formation of parallel bundles of actin filaments in a crystalline-like structure caused by osmotic stress. Biochemistry 28:6513–8PubMedCrossRefGoogle Scholar
  27. Yin HL (1987) Gelsolin: calcium- and polyphosphoinositide-regulated actin-modulating protein. Bioessays 7:176–9PubMedCrossRefGoogle Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 1992

Authors and Affiliations

  • Paul A. Janmey
    • 1
  • C. Casey Cunningham
    • 1
  • George F. Oster
    • 1
    • 2
  • Thomas P. Stossel
    • 1
  1. 1.Department of MedicineHarvard Medical SchoolBostonUSA
  2. 2.Departments of Molecular & Cellular Biology, and EntomologyUniversity of CaliforniaBerkeleyUSA

Personalised recommendations