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Gene Review

GSN  -  gelsolin

Bos taurus

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Disease relevance of GSN


High impact information on GSN


Biological context of GSN


Anatomical context of GSN

  • Presence of scinderin and gelsolin, two Ca2+-dependent actin filament-severing proteins in the same tissue, suggests the possibility of synergistic functions by the two proteins in the control of cellular actin filament networks [11].
  • Scinderin is a structurally different protein from chromaffin cell gelsolin, another actin filament-severing protein described [11].
  • This finding has prompted us to examine effects of the gelsolin complex and the free gelsolin on activities of the above PLC isoforms from platelet cytosol [8].
  • The limited digestion of gelsolin from serum and bovine aorta smooth muscle by two different proteases, chymotrypsin and trypsin, proceeded much faster in the presence of Ca2+ than in its absence with the production of three main fragments of about 40K, 32K, and 21K [12].
  • These results suggest that destruction of the stress fibers by endogenous gelsolin, which leads to inhibition of cell contraction, may occur if the cytoplasmic Ca2+ is maintained at high concentrations for a few minutes [13].

Associations of GSN with chemical compounds


Other interactions of GSN

  • 2) Adseverin belonged to the gelsolin family of proteins, which consists of six homologous segments [16].
  • The COOH terminus exhibits a striking similarity to villin and gelsolin, particularly in regions known to bind F-actin [2].
  • In addition, several low-abundance proteins including fibrinogen beta-chain, chitinase 3-like 1, alpha-antitrypsin, complement C3 alpha-chain, gelsolin and apolipoprotein H were observed only in colostrum [17].
  • The relation between the passive tension and extension of connectin (titin) was obtained for a myofibril from which thin filaments had been completely removed with gelsolin under contracting conditions; this showed a concave curve, consistent with the previous results obtained in single fibers [15].
  • Fluorescent derivatives of phosphatidyl inositol (PtdIns)-(4,5)-P2 were synthesized and used to test the effects of the PtdIns-(4, 5)-P2-regulated proteins gelsolin, tau, cofilin, and profilin on labeled PtdIns-(4,5)-P2 that was either in micellar form or mixed with phosphatidylcholine (PtdCho) in bilayer vesicles [18].

Analytical, diagnostic and therapeutic context of GSN


  1. Gelsolin activates DNase I in vitro and cystic fibrosis sputum. Davoodian, K., Ritchings, B.W., Ramphal, R., Bubb, M.R. Biochemistry (1997) [Pubmed]
  2. Supervillin (p205): A novel membrane-associated, F-actin-binding protein in the villin/gelsolin superfamily. Pestonjamasp, K.N., Pope, R.K., Wulfkuhle, J.D., Luna, E.J. J. Cell Biol. (1997) [Pubmed]
  3. Cortical filamentous actin disassembly and scinderin redistribution during chromaffin cell stimulation precede exocytosis, a phenomenon not exhibited by gelsolin. Vitale, M.L., Rodríguez Del Castillo, A., Tchakarov, L., Trifaró, J.M. J. Cell Biol. (1991) [Pubmed]
  4. Elastic filaments in skeletal muscle revealed by selective removal of thin filaments with plasma gelsolin. Funatsu, T., Higuchi, H., Ishiwata, S. J. Cell Biol. (1990) [Pubmed]
  5. Regulation of the actin cycle in vivo by actin filament severing. McGrath, J.L., Osborn, E.A., Tardy, Y.S., Dewey, C.F., Hartwig, J.H. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
  6. Dependence of fibroblast migration on actin severing activity of gelsolin. Arora, P.D., McCulloch, C.A. J. Biol. Chem. (1996) [Pubmed]
  7. Phosphatidylinositol 4,5-bisphosphate (PIP2)-enhanced G protein-coupled receptor kinase (GRK) activity. Location, structure, and regulation of the PIP2 binding site distinguishes the GRK subfamilies. Pitcher, J.A., Fredericks, Z.L., Stone, W.C., Premont, R.T., Stoffel, R.H., Koch, W.J., Lefkowitz, R.J. J. Biol. Chem. (1996) [Pubmed]
  8. Effects of gelsolin on human platelet cytosolic phosphoinositide-phospholipase C isozymes. Banno, Y., Nakashima, T., Kumada, T., Ebisawa, K., Nonomura, Y., Nozawa, Y. J. Biol. Chem. (1992) [Pubmed]
  9. Comparison between the gelsolin and adseverin domain structure. Sakurai, T., Kurokawa, H., Nonomura, Y. J. Biol. Chem. (1991) [Pubmed]
  10. The Ca2(+)-dependent actin filament-severing activity of 74-kDa protein (adseverin) resides in its NH2-terminal half. Sakurai, T., Kurokawa, H., Nonomura, Y. J. Biol. Chem. (1991) [Pubmed]
  11. Chromaffin cell scinderin, a novel calcium-dependent actin filament-severing protein. Rodriguez Del Castillo, A., Lemaire, S., Tchakarov, L., Jeyapragasan, M., Doucet, J.P., Vitale, M.L., Trifaró, J.M. EMBO J. (1990) [Pubmed]
  12. Characterization of the Ca2+-induced conformational changes in gelsolin and identification of interaction regions between actin and gelsolin. Rouayrenc, J.F., Fattoum, A., Méjean, C., Kassab, R. Biochemistry (1986) [Pubmed]
  13. Smooth muscle gelsolin and a Ca2+-sensitive contractile cell model. Kanno, K., Sasaki, Y. J. Cell. Physiol. (1989) [Pubmed]
  14. Inhibition of actin regulatory activity of the 74-kDa protein from bovine adrenal medulla (adseverin) by some phospholipids. Maekawa, S., Sakai, H. J. Biol. Chem. (1990) [Pubmed]
  15. Microscopic analysis of the elastic properties of nebulin in skeletal myofibrils. Yasuda, K., Anazawa, T., Ishiwata, S. Biophys. J. (1995) [Pubmed]
  16. Differential expression of bovine adseverin in adrenal gland revealed by in situ hybridization. Cloning of a cDNA for adseverin. Nakamura, S., Sakurai, T., Nonomura, Y. J. Biol. Chem. (1994) [Pubmed]
  17. Identification of low-abundance proteins of bovine colostral and mature milk using two-dimensional electrophoresis followed by microsequencing and mass spectrometry. Yamada, M., Murakami, K., Wallingford, J.C., Yuki, Y. Electrophoresis (2002) [Pubmed]
  18. Fluorescent phosphoinositide derivatives reveal specific binding of gelsolin and other actin regulatory proteins to mixed lipid bilayers. Tuominen, E.K., Holopainen, J.M., Chen, J., Prestwich, G.D., Bachiller, P.R., Kinnunen, P.K., Janmey, P.A. Eur. J. Biochem. (1999) [Pubmed]
  19. Purification of native myosin filaments from muscle. Hidalgo, C., Padrón, R., Horowitz, R., Zhao, F.Q., Craig, R. Biophys. J. (2001) [Pubmed]
  20. Interaction of myosin subfragment 1 with forms of monomeric actin. Ballweber, E., Kiessling, P., Manstein, D., Mannherz, H.G. Biochemistry (2003) [Pubmed]
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