Skip to main content
NCBI home page
Biophysical Journal logoLink to Biophysical Journal
. 1992 May;61(5):1301–1305. doi: 10.1016/S0006-3495(92)81938-0

Regulation of water flow by actin-binding protein-induced actin gelatin.

T Ito 1, A Suzuki 1, T P Stossel 1
PMCID: PMC1260393  PMID: 1318095

Abstract

Actin filaments inhibit osmotically driven water flow (Ito, T., K.S. Zaner, and T.P. Stossel. 1987. Biophys. J. 51: 745-753). Here we show that the actin gelation protein, actin-binding protein (ABP), impedes both osmotic shrinkage and swelling of an actin filament solution and reduces markedly the concentration of actin filaments required for this inhibition. These effects depend on actin filament immobilization, because the ABP concentration that causes initial impairment of water flow by actin filaments corresponds to the gel point measured viscometrically and because gelsolin, which noncovalently severs actin filaments, solates actin gels and restores water flow in a solution of actin cross-linked by ABP. Since ABP gels actin filaments in the periphery of many eukaryotic cells, such actin networks may contribute to physiological cell volume regulation.

Full text

PDF
1301

Selected References

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

  1. Brotschi E. A., Hartwig J. H., Stossel T. P. The gelation of actin by actin-binding protein. J Biol Chem. 1978 Dec 25;253(24):8988–8993. [PubMed] [Google Scholar]
  2. Chaponnier C., Janmey P. A., Yin H. L. The actin filament-severing domain of plasma gelsolin. J Cell Biol. 1986 Oct;103(4):1473–1481. doi: 10.1083/jcb.103.4.1473. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Gorlin J. B., Yamin R., Egan S., Stewart M., Stossel T. P., Kwiatkowski D. J., Hartwig J. H. Human endothelial actin-binding protein (ABP-280, nonmuscle filamin): a molecular leaf spring. J Cell Biol. 1990 Sep;111(3):1089–1105. doi: 10.1083/jcb.111.3.1089. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Hartwig J. H., Shevlin P. The architecture of actin filaments and the ultrastructural location of actin-binding protein in the periphery of lung macrophages. J Cell Biol. 1986 Sep;103(3):1007–1020. doi: 10.1083/jcb.103.3.1007. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Hartwig J. H., Stossel T. P. Structure of macrophage actin-binding protein molecules in solution and interacting with actin filaments. J Mol Biol. 1981 Jan 25;145(3):563–581. doi: 10.1016/0022-2836(81)90545-3. [DOI] [PubMed] [Google Scholar]
  6. Hock R. S., Davis G., Speicher D. W. Purification of human smooth muscle filamin and characterization of structural domains and functional sites. Biochemistry. 1990 Oct 9;29(40):9441–9451. doi: 10.1021/bi00492a019. [DOI] [PubMed] [Google Scholar]
  7. Hoffmann E. K., Simonsen L. O. Membrane mechanisms in volume and pH regulation in vertebrate cells. Physiol Rev. 1989 Apr;69(2):315–382. doi: 10.1152/physrev.1989.69.2.315. [DOI] [PubMed] [Google Scholar]
  8. Ito T., Zaner K. S., Stossel T. P. Nonideality of volume flows and phase transitions of F-actin solutions in response to osmotic stress. Biophys J. 1987 May;51(5):745–753. doi: 10.1016/S0006-3495(87)83401-X. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Janmey P. A., Hvidt S., Lamb J., Stossel T. P. Resemblance of actin-binding protein/actin gels to covalently crosslinked networks. Nature. 1990 May 3;345(6270):89–92. doi: 10.1038/345089a0. [DOI] [PubMed] [Google Scholar]
  10. Janmey P. A., Stossel T. P. Kinetics of actin monomer exchange at the slow growing ends of actin filaments and their relation to the elongation of filaments shortened by gelsolin. J Muscle Res Cell Motil. 1986 Oct;7(5):446–454. doi: 10.1007/BF01753587. [DOI] [PubMed] [Google Scholar]
  11. MacLean-Fletcher S. D., Pollard T. D. Viscometric analysis of the gelation of Acanthamoeba extracts and purification of two gelation factors. J Cell Biol. 1980 May;85(2):414–428. doi: 10.1083/jcb.85.2.414. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Oster G. F., Perelson A. S. The physics of cell motility. J Cell Sci Suppl. 1987;8:35–54. doi: 10.1242/jcs.1987.supplement_8.3. [DOI] [PubMed] [Google Scholar]
  13. Tanaka T. Gels. Sci Am. 1981 Jan;244(1):124-36, 138. doi: 10.1038/scientificamerican0181-124. [DOI] [PubMed] [Google Scholar]
  14. Yin H. L., Zaner K. S., Stossel T. P. Ca2+ control of actin gelation. Interaction of gelsolin with actin filaments and regulation of actin gelation. J Biol Chem. 1980 Oct 10;255(19):9494–9500. [PubMed] [Google Scholar]

Articles from Biophysical Journal are provided here courtesy of The Biophysical Society

RESOURCES