Murine Adseverin (D5), a Novel Member of the Gelsolin Family, and Murine Adseverin Are Induced by Interleukin-9 in T-Helper Lymphocytes

REFERENCES

• Amann, E., J. Brosius, and M. Ptashne 1983. Vectors bearing a hybrid trp-lac promoter useful for regulated expression of cloned genes in Escherichia coli. Gene 25: 167–178.
   PubMedGoogle Scholar
• Ampe, C., and J. Vandekerckhove 1987. The F-actin capping proteins of Physarum polycephalum: cap42(a) is very similar, if not identical, to fragmin and is structurally and functionally very homologous to gelsolin; cap42(b) is Physarum actin. EMBO J. 6: 4149–4157.
   PubMedGoogle Scholar
• Andre, E., F. Lottspeich, M. Schleicher, and A. Noegel 1988. Severin, gelsolin, and villin share a homologous sequence in regions presumed to contain F-actin severing domains. J. Biol. Chem. 263: 722–727.
   PubMedGoogle Scholar
• Ausubel, F., R. Brent, R. Kingston, D. Moore, J. Seidman, J. Smith, and K. Struhl 1993. Current protocols in molecular biology 1993. Greene and Wiley-Interscience, New York, N.Y.
   Google Scholar
• Bauw, G., M. De Loose, D. Inzé, M. Van Montagu, and J. Vandekerckhove 1987. Alterations in the phenotype of plant cells studied by NH2-terminal amino-acid-sequence analysis of proteins electroblotted from two-dimensional gel-separated total extracts. Proc. Natl. Acad. Sci. USA 84: 4806–4810.
   PubMedGoogle Scholar
• Brenner, S. L., and E. D. Korn 1983. On the mechanism of actin monomer-polymer subunit exchange at steady state. J. Biol. Chem. 258: 5013–5020.
   PubMed Web of Science ®Google Scholar
• Bryan, J. 1988. Gelsolin has three actin-binding sites. J. Cell Biol. 106: 1553–1562.
   PubMedGoogle Scholar
• Burtnick, L. D., E. D. Koepf, J. Grimes, E. Y. Jones, D. I. Stuart, P. J. McLaughin, and R. C. Robinson 1997. The crystal structure of plasma gelsolin; implication for actin severing, capping and nucleation. Cell 90: 661–670.
   PubMed Web of Science ®Google Scholar
• Dieffenbach, C. W., D. N. SenGupta, D. Krause, D. Sawzak, and R. H. Silverman 1989. Cloning of murine gelsolin and its regulation during differentiation of embryonal carcinoma cells. J. Biol. Chem. 264: 13281–13288.
   PubMed Web of Science ®Google Scholar
• Gettemans, J., Y. De Ville, E. Waelkens, and J. Vandekerckhove 1995. The actin-binding properties of the Physarum actin-fragmin complex. Regulation by calcium, phospholipids, and phosphorylation. J. Biol. Chem. 270: 2644–2651.
   PubMedGoogle Scholar
• Giebing, T., H. Hinssen, and J. D’Haese 1994. The complete sequence of a 40-kDa actin-modulating protein from the earthworm Lumbricus terrestris. Eur. J. Biochem. 225: 773–779.
   PubMedGoogle Scholar
• Gips, S. J., D. E. Kandzari, and P. J. Goldschmidt-Clermont 1994. Growth factor receptors, phospholipases, phospholipid kinases and actin reorganization. Semin. Cell Biol. 5: 201–208.
   PubMedGoogle Scholar
• Hesterkamp, T., A. G. Weeds, and H. G. Mannherz 1993. The actin monomers in the ternary gelsolin: 2 actin complexes are in an antiparallel orientation. Eur. J. Biochem. 218: 507–513.
   PubMedGoogle Scholar
• Hültner, L., C. Druez, J. Moeller, E. Schmitt, C. Uyttenhove, E. Rüde, P. Dörmer, and J. Van Snick 1990. Mast cell growth-enhancing activity (MEA) is structurally related and functionally identical to the novel mouse T cell growth factor P40/TCGFIII (interleukin 9). Eur. J. Immunol. 20: 1413–1416.
   PubMed Web of Science ®Google Scholar
• Janmey, P. A. 1994. Phosphoinositides and calcium as regulators of cellular actin assembly and disassembly. Annu. Rev. Physiol. 56: 169–191.
   PubMed Web of Science ®Google Scholar
• Janmey, P. A., and T. P. Stossel 1987. Modulation of gelsolin function by phosphatidylinositol 4,5-bisphosphate. Nature 325: 362–364.
   PubMed Web of Science ®Google Scholar
• Janmey, P. A., J. Lamb, P. G. Allen, and P. T. Matsudaira 1992. Phosphoinositide-binding peptides derived from the sequences of gelsolin and villin. J. Biol. Chem. 267: 11818–11823.
   PubMed Web of Science ®Google Scholar
• Kraus-Friedman, N. 1994. Signal transduction and calcium: a suggested role for the cytoskeleton in inositol 1,4,5-triphosphate action. Cell Motil. Cytoskelet. 28: 279–284.
   PubMedGoogle Scholar
• Kwiatkowski, D. J., T. P. Stossel, S. H. Orkin, J. E. Mole, H. R. Colten, and H. L. Yin 1986. Plasma and cytoplasmic gelsolins are encoded by a single gene and contain a duplicated actin-binding domain. Nature 227: 455–458.
   Google Scholar
• Kwiatkowski, D. J., P. A. Janmey, and H. L. Yin 1989. Identification of critical functional and regulatory domains in gelsolin. J. Cell Biol. 108: 1717–1726.
   PubMedGoogle Scholar
• Liou, G. I., and S. Matragon 1992. A simple method to homogenize multiple tissue samples in small sizes without cross contamination. BioTechniques 13: 719.
   PubMedGoogle Scholar
• Louahed, Y., N. Kermouni, J. Van Snick, and J. C. Renauld 1995. IL-9 induces expression of granzymes and high-affinity IgE receptor in murine T helper clones. J. Immunol. 154: 5061–5070.
   PubMed Web of Science ®Google Scholar
• Lück, A., J. D’Haese, and H. Hinssen 1995. A gelsolin-related protein from lobster muscle: cloning, sequence analysis and expression. Biochem. J. 305: 767–775.
   PubMedGoogle Scholar
• MacLean-Fletcher, S., and T. Pollard 1980. Viscometric analysis of the gelation of Acanthamoeba extracts and purification of two gelation factors. J. Cell Biol. 85: 414–428.
   PubMed Web of Science ®Google Scholar
• Maekawa, S., and H. Sakai 1990. Inhibition of actin regulatory activity of the 74-kDa protein from bovine adrenal medulla (adseverin) by some phospholipids. J. Biol. Chem. 265: 10940–10942.
   PubMedGoogle Scholar
• Marcu, M. G., L. Zhang, A. Elzagallaai, and J. M. Trifaro 1998. Localization by segmental deletion analysis and functional characterization of a third actin-binding site in domain 5 of scinderin. J. Biol. Chem. 273: 3661–3668.
   PubMedGoogle Scholar
• Müllauer, L., H. Fujita, A. Ishizaki, and N. Kuzumaki 1993. Tumor-suppressive function of mutated gelsolin in ras-transformed cells. Oncogene 8: 2531–2536.
   PubMed Web of Science ®Google Scholar
• Nakamura, S., T. Sakurai, and Y. Nonomura 1994. Differential expression of bovine adseverin in adrenal gland revealed by in situ hybridization. Cloning of a cDNA for adseverin. J. Biol. Chem. 269: 5890–5896.
   PubMedGoogle Scholar
• Paunio, T., H. Kangas, N. Kalkkinen, M. Haltia, J. Palo, and L. Peltonen 1994. Toward understanding the pathogenic mechanisms in gelsolin-related amyloidosis: in vitro expression reveals an abnormal gelsolin fragment. Hum. Mol. Genet. 12: 2223–2229.
   Google Scholar
• Pope, B., S. Maclver, and A. Weeds 1995. Localization of the calcium-sensitive actin monomer binding site in gelsolin to segment 4 and identification of calcium binding sites. Biochemistry 34: 1583–1588.
   PubMedGoogle Scholar
• Rodriguez Del Castillo, A., S. Lemaire, L. Tchakarov, M. Jeyapragrasan, J. P. Doucet, M. L. Vitale, and J. M. Trifaro 1990. Chromaffin cell scinderin, a novel calcium-dependent actin filament-severing protein. EMBO J. 9: 43–52.
   PubMed Web of Science ®Google Scholar
• Sakurai, T., H. Kurokawa, and Y. Nonomura 1991. Comparison between the gelsolin and adseverin domain structure. J. Biol. Chem. 166: 15979–15983.
   Google Scholar
• Schmitt, E., R. van Brandwijk, J. Van Snick, B. Siebold, and E. Rüde 1989. TCGF III/P40 is produced by naive murine CD4+ T cells but is not a general T cell growth factor. Eur. J. Immunol. 19: 2167–2170.
   PubMed Web of Science ®Google Scholar
• Spudich, J. A., and S. Watt 1971. The regulation of rabbit skeletal muscle contraction. J. Biol. Chem. 246: 4866–4871.
   PubMed Web of Science ®Google Scholar
• Sun, H. Q., D. C. Wooten, P. A. Janmey, and H. L. Yin 1994. The actin side-binding domain of gelsolin also caps actin filaments. Implications for actin filament severing. J. Biol. Chem. 269: 9473–9479.
   PubMedGoogle Scholar
• Tanaka, M., L. Mullauer, Y. Ogiso, H. Fujita, S. Moriya, K. Furuuchi, T. Harabayashi, N. Shinohara, T. Koyanagi, and N. Kuzumaki 1995. Gelsolin: a candidate for suppressor of human bladder cancer. Cancer Res. 55: 3228–3232.
   PubMed Web of Science ®Google Scholar
• Tchakarov, L., M. L. Vitale, M. Jeyapragrasan, A. Rodriguez Del Castillo, and J. M. Trifaro 1990. Expression of scinderin, an actin filament-severing protein, in different tissues. FEBS Lett. 268: 209–212.
   PubMedGoogle Scholar
• T’Jampens, D., K. Meerschaert, B. Constantin, J. Bailey, L. J. Cook, V. De Corte, H. De Mol, M. Goethals, J. Van Damme, J. Vanderkerckhove, and J. Gettemans 1997. Molecular cloning, over-expression, developmental regulation and immunolocalization of fragmin P, a gelsolin-related actin-binding protein from Physarum polycephalum plasmodia. J. Cell Sci. 110: 1215–1226.
   PubMedGoogle Scholar
• Uyttenhove, C., J. Simpson, and J. Van Snick 1988. Functional and structural characterization of P40, a mouse glycoprotein with T-cell growth factor activity. Proc. Natl. Acad. Sci. USA 85: 6934–6938.
   PubMed Web of Science ®Google Scholar
• Way, M., and A. G. Weeds 1988. Nucleotide sequence of pig plasma gelsolin. Comparison of protein sequence with human gelsolin and other actin-severing proteins shows strong homologies and evidence for large internal repeats. J. Mol. Biol. 203: 1127–1133.
   PubMed Web of Science ®Google Scholar
• Way, M., J. Gooch, B. Pope, and A. G. Weeds 1989. Expression of human plasma gelsolin in Escherichia coli and dissection of actin binding sites by segmental deletion mutagenesis. J. Cell Biol. 109: 593–605.
   PubMedGoogle Scholar
• Witke, W., A. H. Sharpe, J. H. Hartwig, T. Aruma, T. Stossel, and D. I. Kwiatkowski 1995. Hemostatic, inflammatory, and fibroblast responses are blunted in mice lacking gelsolin. Nature 81: 41–51.
   Google Scholar
• Yamamoto, K., J. D. Pardee, J. Reidler, L. Stryer, and J. A. Spudich 1982. Mechanism of interaction of Dictyostelium severin with actin filaments. J. Cell Biol. 95: 711–719.
   PubMedGoogle Scholar
• Yin, H. L., and T. P. Stossel 1979. Control of cytoplasmic actin gel-sol transformation by gelsolin, a calcium-dependent regulatory protein. Nature 281: 583–586.
   PubMed Web of Science ®Google Scholar
• Yin, H. L., and T. P. Stossel 1980. Purification and structural properties of gelsolin, a Ca2+-activated regulatory protein of macrophages. J. Biol. Chem. 255: 9490–9493.
   PubMedGoogle Scholar
• Yu, F. X., H. Q. Sun, P. A. Janmey, and H. Yin 1992. Identification of a polyphosphoinositide-binding sequence in an actin monomer-binding domain of gelsolin. J. Biol. Chem. 267: 14616–14621.
   PubMed Web of Science ®Google Scholar