Advertisement

Actin pp 105-112 | Cite as

Actin Regulation and Surface Catalysis

  • Lawrence E. Crawford
  • Robert W. Tucker
  • Alan W. Heldman
  • Pascal J. Goldschmidt-Clermont
Chapter
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 358)

Abstract

The motile behavior of non-muscle cells often differs between healthy and pathological conditions. Two disease processes, cancer and atherosclerosis, are associated with high morbidity and mortality in our society. The cells involved in both the pathogenesis of and me defense against these diseases undergo marked changes in the organization of their actin cytoskeletonl1,2. In response to a signal originating from the extracellular space, from surrounding cells, or as the result of a mutation, diseased cells initiate a process of motion away from their normal location. Local growth inhibitors are lost, and displaced cells undergo unchecked proliferation1. One example of such a phenomenon is the migration of fibroblasts and smooth muscle cells into the vascular intima and their proliferation in patients with atherosclerotic coronary artery disease2. Another example is the proliferation of metastatic cells distant from the site of primary tumor1.

Keywords

Actin Filament Actin Cytoskeleton Calcium Transient Actin Stress Fiber Actin Monomer 
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.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    Van Roy F, Mareel M, Tumor invasion: effects of cell adhesion and motility. Trends Cell Biol. 2: 163 (1992).PubMedCrossRefGoogle Scholar
  2. 2.
    Heldman AW, Furman MI, Gardner TM, Gips SJ, Crawford LE, Goldschmidt-Clermont PJ, Coronary artery disease and atherogenesis. in: Molecular Basis of Medicine, Dang CV and Feldman AM, eds., (1993) in press.Google Scholar
  3. 3.
    Cooper JA, The role of actin polymerization in cell motility. Annu Rev Physiol 53: 585 (1991).PubMedCrossRefGoogle Scholar
  4. 4.
    Howard K, Getting there? Curr Biol. 3: 103 (1993).Google Scholar
  5. 5.
    Luna EJ, Hitt AL, Cytoskeleton-plasma membrane interactions. Science 258: 955 (1992).PubMedCrossRefGoogle Scholar
  6. 6.
    Goldschmidt-Clermont PJ, Janmey PA, Profilin, a weak CAP for actin and RAS. Cell 66, 419 (1991).PubMedCrossRefGoogle Scholar
  7. 7.
    Friend CM, Catalysis on surfaces. Scientific American 268: 74 (1993).CrossRefGoogle Scholar
  8. 8.
    Yates JT, Surface chemistry. Chemical Engineering News 70: 22 (1992).CrossRefGoogle Scholar
  9. 9.
    Fukami K, Furuhashi K, Inagaki M, Endo T, Hatano S, Takenawa T, Requirement of phosphatidylinositol 4, 5 bisphosphate for α-actinin function. Nature 359: 150 (1992).PubMedCrossRefGoogle Scholar
  10. 10.
    Goldschmidt-Clermont PJ, Kim JW, Machesky LM, Rhee SG, Pollard TD, Regulation of phospholipase Cγ1 by profilin and tyrosine phosphorylation. Science 251: 1231 (1991).PubMedCrossRefGoogle Scholar
  11. 11.
    Finkel T, Theriot JA, Dise KR, Tomaselli GF, Goldschmidt-Clermont PJ, Actin superstructure promoted by profilin. Proc Natl Acad Sci USA (1993) in press.Google Scholar
  12. 12.
    Cantley LC, Auger KR, Carpenter C, Duckworth B, Graziani A, Kapeller R, Soltoff S, Oncogenes and signal transduction. Cell 64: 281 (1991).PubMedCrossRefGoogle Scholar
  13. 13.
    Goldschmidt-Clermont PJ, Machesky LM, Baldassare JJ, Pollard TD, The actin-binding protein profilin binds to PIP2 and inhibits its hydrolysis by phospholipase-C. Science 247: 1575 (1990).PubMedCrossRefGoogle Scholar
  14. 14.
    Machesky LM, Goldschmidt-Clermont PJ, Pollard TD, The affinities of human platelet and Acanthamoeba profilin isoforms for polyphosphoinositides account for their relative abilities to inhibit phospholipase C. Cell Regul 1: 937–950 (1990).PubMedGoogle Scholar
  15. 15.
    Engel J, Fasold H, Hulla FW, Waechter F, Wegner A, The polymerization reaction of muscle actin. Mol Cell Biochem 18: 3 (1977).PubMedCrossRefGoogle Scholar
  16. 16.
    Wegner A, Head to tail polymerization of actin. J Mol Biol. 108: 139–150, 1976.PubMedCrossRefGoogle Scholar
  17. 17.
    Janmey PA, Hvidt S, Oster GF, Lamb J, Stossel TP, Hartwig JH, Effect of ATP on actin filament stiffness. Nature 347: 95 (1990).PubMedCrossRefGoogle Scholar
  18. 18.
    Pollard TD, Goldberg I, Schwarz WH, Nucleotide exchange, structure, and mechanical properties of filaments assembled from ATP-actin and ADP-actin. J Biol Chem 267: 20339 (1992).PubMedGoogle Scholar
  19. 19.
    Theriot JA, Mitchison TJ, Actin microfilaments dynamics in locomoting cells. Nature 352: 126 (1991).PubMedCrossRefGoogle Scholar
  20. 20.
    Theriot JA, Mitchison TJ, The nucleation-release model of actin filament dynamics in cell motility. Trends Cell Biol. 2: 219 (1992).PubMedCrossRefGoogle Scholar
  21. 21.
    Mockrin SC, Korn ED, Acanthamoeba profilin interacts with G-actin to increase the rate of exchange of actin-bound adenosine 5’-triphosphate. Biochemistry 19: 5359 (1980).PubMedCrossRefGoogle Scholar
  22. 22.
    Goldschmidt-Clermont PJ, Furman MI, Wachsstock D, Safer D, Nachmias VT, Pollard TD, The control of actin nucleotide exchange by thymosinb4 and profilin. A potential regulatory mechanism for actin polymerization in cells. Mol Biol Cell 3: 1015 (1992).PubMedGoogle Scholar
  23. 23.
    Carlier M-F, Role of nucleotide hydrolysis in the dynamics of actin filaments and microtubules. Int Rev Cytol 115: 139 (1989).PubMedCrossRefGoogle Scholar
  24. 24.
    Cooper JA, Effects of cytochalasin and phalloidin on actin. J Cell Biol. 105: 1473 (1987).PubMedCrossRefGoogle Scholar
  25. 25.
    Ridley AJ, Hall A, The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell 70: 389 (1992).PubMedCrossRefGoogle Scholar
  26. 26.
    Ridley AJ, Paterson HF, Johnston CL, Diekmann D, Hall A, The small GTP-binding protein rac regulates growth factor-induced membrane ruffling. Cell 70: 401 (1992).PubMedCrossRefGoogle Scholar
  27. 27.
    Bourne HR, Sanders DA, McCormick F, The GTPase superfamily: a conserved switch for diverse cell functions. Nature 348: 125 (1990).PubMedCrossRefGoogle Scholar
  28. 28.
    Bourne HR, Sanders DA, McCormick F, The GTPase superfamily: conserved structure and molecular mechanism. Nature 349: 117 (1991)Google Scholar
  29. 29.
    Goldschmidt-Clermont PJ, Mendelsohn ME, Gibbs JB, Rac and Rho in control. Curr Biol. 2: 669 (1992).PubMedCrossRefGoogle Scholar
  30. 30.
    Acknowledgements: This research was supported in part by a grant from Syntex, by a grant from the Bernard Foundation and by the American heart Association (G-I-A, Maryland Affiliate, Inc.). PJG-C was selected as a Syntex Scholar in 1992.Google Scholar

Copyright information

© Springer Science+Business Media New York 1994

Authors and Affiliations

  • Lawrence E. Crawford
    • 1
  • Robert W. Tucker
    • 2
    • 3
  • Alan W. Heldman
    • 1
  • Pascal J. Goldschmidt-Clermont
    • 1
    • 3
  1. 1.Cardiology Division, Department of MedicineJohns Hopkins University School of MedicineBaltimoreUSA
  2. 2.Oncology DepartmentJohns Hopkins University School of MedicineBaltimoreUSA
  3. 3.Department of Cell Biology and AnatomyJohns Hopkins University School of MedicineBaltimoreUSA

Personalised recommendations