Coordinate induction of the actin cytoskeletal regulatory proteins gelsolin, vasodilator-stimulated phosphoprotein, and profilin during capillary morphogenesis in vitro

Experimental Cell Research

Volumn 249, Issue 1, 1999, Pages 22-32

  Salazar, René ^a   Bell, Scott E ^a   Davis, George E ^a  

^a TEXAS A AND M HEALTH SCIENCE CENTER   (United States)

Author keywords

Capillary morphogenesis; Gelsolin; Profilin; VASP

Indexed keywords

ACTIN; PHOSPHOPROTEIN; PROFILIN;

ARTICLE; CYTOSKELETON; EXTRACELLULAR MATRIX; GENE EXPRESSION REGULATION; HUMAN; HUMAN CELL; PRIORITY JOURNAL; PROTEIN EXPRESSION; TISSUE REPAIR; VASODILATATION;

TRIXIS;

EID: 0033602716     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1006/excr.1999.4460     Document Type: Article

References (47)

1. Ankenbauer T., Kleinschmidt J. A., Vanderkerckhove J., Franke W. Proteins regulating actin assembly in oogenesis and early embryogenesis ofXenopus laevis: J. Cell Biol. 107:1988;1489-1498.
2. Kwiatkowski D. J. Predominant induction of gelsolin and actin-binding protein during myeloid differentiation. J. Biol. Chem. 263:1988;13857-13862.
3. Dieffenbach C. W., SenGupta D. N., Krause D., Sawzak D., Silverman R. H. Cloning of murine gelsolin and its regulation during differentiation of embryonal carcinoma cells. J. Biol. Chem. 264:1989;13281-13288.
4. Grinnell F. Wound repair, keratinocyte activation and integrin modulation. J. Cell Sci. 101:1992;1-5.
5. Schwartz S. B., Higgins P. J., Ayyappan K. R., Staiano-Coico L. Gelsolin expression in normal human keratinocytes is a function of induced differentiation. Adv. Exp. Med. Biol. 358:1994;169-181.
6. Watts R. G. Role of gelsolin in the formation and organization of triton-soluble F-actin during myeloid differentiation of HL-60 cells. Blood. 85:1995;2212-2221.
7. Scholz A., Hinssen H. Biphasic pattern of gelsolin expression and variations in gelsolin-actin interactions during myogenesis. Exp. Cell Res. 219:1995;384-391.
8. Arora P. D., McCulloch C. A. G. Dependence of fibroblast migration on actin severing activity of gelsolin. J. Biol. Chem. 217:1996;20516-20523.
9. Mooney D. J., Langer R., Ingber D. E. Cytoskeletal filament assembly and the control of cell spreading and function by extracellular matrix. J. Cell Sci. 108:1995;2311-2320.
10. Chen C. S., Mrksich M., Huang S., Whitesides G. M., Ingber D. E. Geometric control of life and death. Science. 276:1997;1425-1428.
11. Yin H. L., Stossel T. P. Control of cytoplasmic actin gel-sol transformation by gelsolin, a calcium-dependent regulatory protein. Nature. 281:1979;583-586.
12. Kwiatkowski D. J., Janmey P. A., Yin H. L. Identification of critical functional and regulatory domains in gelsolin. J. Cell Biol. 108:1989;1717-1726.
13. Kwiatkowski D. J., Stossel T. P., Orkin S. H., Mole J. E., Colten H. R., Yin H. L. Plasma and cytoplasmic gelsolins are encoded by a single gene and contain a duplicated actin-binding domain. Nature. 323:1986;455-458.
14. 2+. J. Biol. Chem. 255:1980;9494-9500.
15. Janmey P. A., Stossel T. P. Gelsolin-polyphosphoinositide interaction: Full expression of gelsolin-inhibiting function by polyphosphoinositides in vesicular form and inactivation by dilution, aggregation, or masking of the inositol head group. J. Biol. Chem. 264:1989;4825-4831.
16. Banyard M. R., Medveczyk C. J., Tellam R. L. Microfilament organization correlates with increased cellular content of gelsolin. Exp. Cell Res. 187:1990;180-183.
17. Tanaka M., Mullauer L., Ogiso Y., Fujita H., Moriya S., Furuuchi K., Harabayashi T., Shinohara N., Koyanagi T., Kuzumaki N. Gelsolin: A candidate for suppressor of human bladder cancer. Cancer Res. 55:1995;3228-3232.
18. Cunningham C. C., Stossel T. P., Kwiatkowski D. J. Enhanced motility in NIH3T3 fibroblasts that overexpress gelsolin. Science. 251:1991;1233-1236.
19. Azuma T., Witke W., Stossel T. T., Hartwig J. H., Kwiatkowski D. J. Gelsolin is a downstream effector of rac for fibroblast motility. EMBO J. 17:1998;1362-1370.
20. Reinhard M., Halbrugge M., Scheer U., Wiegand C., Jockusch B. M., Walter U. The 46/50 kDa phosphoprotein VASP purified from human platelets is a novel protein associated with actin filaments and focal contacts. EMBO J. 11:1992;2063-2070.
21. Reinhard M., Griehl K., Abel K., Haffner C., Jarchau T., Hoppe V., Jockusch B. M., Walter U. The proline-rich focal adhesion and microfilament protein VASP is a ligand for profilins. EMBO J. 14:1995;1583-1589.
22. Reinhard M., Jouvenal K., Tripier D., Walter U. Identification, purification, and characterization of zyxin-related protein that binds the focal adhesion and microfilament protein VASP (vasodilator-stimulated phosphoprotein). Proc. Natl. Acad. Sci. USA. 92:1995;7956-7960.
23. Brindle N. P. J., Holt M. R., Davies J. E., Price C. J., Critchley D. R. The focal-adhesion vasodilator-stimulated phosphoprotein (VASP) binds to the proline-rich domain in vinculin. Biochem. J. 318:1996;753-757.
24. Sohn R. H., Goldschmidt P. J. Profilin: At the crossroads of signal transduction and the actin cytoskeleton. BioEssays. 16:1994;465-472.
25. Schafer D. A., Cooper J. A. Control of actin assembly at filament ends. Annu. Rev. Cell Dev. Biol. 11:1995;497-518.
26. Watanabe N., Madaule P., Reid T., Ishizaki T., Watanabe G., Kakizuka A., Saito Y., Nakao K., Jockusch B. M., Narumiya S. P140mDia, a mammalian homolog ofDrosophila. EMBO J. 16:1997;3044-3056.
27. Vernon R. B., Sage E. H. Between molecules and morphology. Am. J. Pathol. 147:1995;873-883.
28. Senger D. R. Molecular framework for angiogenesis - A complex web of interactions between extravasated plasma proteins and endothelial cell proteins induced by angiogenic cytokines. Am. J. Pathol. 149:1996;1-7.
29. Davis G. E., Camarillo C. An alpha-2-beta-1 integrin-dependent pinocytotic mechanism involving intracellular vacuole formation and coalescence regulates capillary lumen and tube formation in three-dimensional collagen matrix. Exp. Cell Res. 224:1996;39-51.
30. Moldovan N. I., Milliken E. E., Irani K., Chen J., Sohn R. H., Finkel T., Goldschmidt-Clermont P. J. Regulation of endothelial cell adhesion by profilin. Curr. Biol. 7:1997;24-30.
31. Chaponnier C., Janmey P. A., Yin H. L. The actin filament-severing domain of plasma gelsolin. J. Cell Biol. 103:1986;1473-1481.
32. Bornstein M. B. Reconstituted rat-tail collagen used as a substrate for tissue cultures on coverslips in Maximov slides and roller tubes. Lab. Invest. 7:1958;134-137.
33. Chomczynski P., Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162:1987;156-159.
34. Sambrook J., Fritsch E. F., Maniatis T. Analysis and cloning of eukaryotic genomic DNA. Molecular Cloning: A Laboratory Manual. 1989;Cold Spring Harbor Laboratory Press, Cold Spring Harbor.
35. Maciag T., Cerundolo J., Lisley S., Kelley P. R., Forand R. An endothelial cell growth factor from bovine hypothalamus: Identification and partial characterization. Proc. Natl. Acad. Sci. USA. 76:1979;5674-5678.
36. Lipton B. H., Bensch K. G., Karasek M. A. Microvessel endothelial cell transdifferentiation: Phenotypic characterization. Differentiation. 46:1991;117-133.
37. Witke W., Sharpe A. H., Hartwig J. H., Azuma T., Stossel T. P., Kwiatkowski D. J. Hemostatic, inflammatory, and fibroblast responses are blunted in mice lacking gelsolin. Cell. 81:1995;41-51.
38. Kothakota S., Azuma T., Reinhard C., Klippel A., Tang J., Chu K., McGarry T. J., Kirschner M. W., Koths K., Kwiatkowski D. J., Williams L. T. Caspase-3-generated fragment of gelsolin: Effector of morphological change in apoptosis. Science. 278:1997;294-298.
39. Ohtsu M., Sakai N., Fujita H., Kashiwagi M., Gasa S., Shimizu S., Eguchi Y., Tsujimoto Y., Sakiyama Y., Kobayashi K., Kuzumaki N. Inhibition of apoptosis by the actin-regulatory protein gelsolin. EMBO J. 16:1997;4650-4656.
40. Folkman J., Haudenschild C. Angiogenesis in vitro. Nature. 288:1980;551-556.
41. Draijer R., Vaandrager A. B., Nolte C., de Jonge H. R., Walter U., van Hinsbergh V. W. M. Expression of cGMP-dependent protein kinase I and phosphorylation of its substrate, vasodilator-stimulated phosphoprotein, in human endothelial cells of different origin. Circ. Res. 77:1995;897-905.
42. Markert T., Krenn V., Leebman J., Walter U. High expression of the focal adhesion- and microfilament-associated protein VASP in vascular smooth muscle and endothelial cells of the intact human vessel wall. Basic Res. Cardiol. 9:1996;337-343.
43. Ridley A. J., Hall A. The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell. 70:1992;389-399.
44. Ankenbauer T., Kleinschmidt J. A., Walsh M. J., Weiner O. H., Franke W. W. Identification of a widespread nuclear actin binding protein. Nature. 342:1989;822-825.
45. Gant T. M., Wilson K. L. Nuclear assembly. Annu. Rev. Cell Dev. Biol. 13:1997;669-695.
46. Boulikas T. Nuclear localization signals (NLS). Crit. Rev. Eukaryotic Gene Exp. 3:1993;193-227.
47. Onoda K., Yu F. X., Yin H. L. GCap39 is a nuclear and cytoplasmic protein. Cell Motil. Cytoskeleton. 26:1993;227-238.