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Gene Review

Scin  -  scinderin

Mus musculus

Synonyms: AW545522, Adseverin, Gelsolin-like protein, Scinderin, adseverin
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Disease relevance of Scin

  • We expressed both proteins in Escherichia coli and show that mouse adseverin displays the typical characteristics of all members of the gelsolin family with respect to actin binding (capping, severing, and nucleation) and its regulation by Ca2+ [1].

Psychiatry related information on Scin

  • To understand the distinct functions of the closely related actin-severing proteins adseverin and gelsolin, we examined the expression of these proteins in detail during mouse and human development using a new highly sensitive and specific set of antibody reagents [2].

High impact information on Scin

  • Eps8-family proteins do not show any similarity to gelsolin-like proteins [3].
  • Mouse adseverin (D5) was found only in blood cells and in cell lines derived from T-helper lymphocytes and mast cells, where it is weakly expressed [1].
  • We have developed antibodies directed toward the leucine rich repeat and gelsolin-like domains of the human and mouse homologues of flightless I that specifically recognize expressed and endogenous forms of the protein [4].
  • In mouse and human intestine adseverin was expressed in enterocytes with a gradient of increasing expression from the duodenum to the colon, and from the crypt to the villus [2].
  • The observations indicate high level expression of adseverin in specific cells of the kidney and colon, and suggest a previously unrecognized function of adseverin in epithelial cell function [2].

Biological context of Scin


Anatomical context of Scin


Associations of Scin with chemical compounds


Other interactions of Scin

  • A comparison between mouse strains with different TCDD responsiveness indicated that the induction of adseverin is dependent on the aryl hydrocarbon receptor, a transcription factor known to mediate most of TCDD's biological effects [7].

Analytical, diagnostic and therapeutic context of Scin

  • Immunohistochemistry on murine kidney sections revealed a predominantly differential localization of adseverin and gelsolin [2].
  • In a gel filtration experiment, we demonstrated that mouse adseverin forms a 1:2 complex with G actin which is stable only in the presence of Ca2+, while no stable complex was observed for mouse adseverin (D5) [1].
  • The use of fetal thymic organ cultures also indicates that TCDD-induced expression of adseverin is confined to the thymocytes [9].


  1. Murine adseverin (D5), a novel member of the gelsolin family, and murine adseverin are induced by interleukin-9 in T-helper lymphocytes. Robbens, J., Louahed, J., De Pestel, K., Van Colen, I., Ampe, C., Vandekerckhove, J., Renauld, J.C. Mol. Cell. Biol. (1998) [Pubmed]
  2. The actin-binding proteins adseverin and gelsolin are both highly expressed but differentially localized in kidney and intestine. Lueck, A., Brown, D., Kwiatkowski, D.J. J. Cell. Sci. (1998) [Pubmed]
  3. Eps8 controls actin-based motility by capping the barbed ends of actin filaments. Disanza, A., Carlier, M.F., Stradal, T.E., Didry, D., Frittoli, E., Confalonieri, S., Croce, A., Wehland, J., Di Fiore, P.P., Scita, G. Nat. Cell Biol. (2004) [Pubmed]
  4. The flightless I protein colocalizes with actin- and microtubule-based structures in motile Swiss 3T3 fibroblasts: evidence for the involvement of PI 3-kinase and Ras-related small GTPases. Davy, D.A., Campbell, H.D., Fountain, S., de Jong, D., Crouch, M.F. J. Cell. Sci. (2001) [Pubmed]
  5. Calcium regulation of gelsolin and adseverin: a natural test of the helix latch hypothesis. Lueck, A., Yin, H.L., Kwiatkowski, D.J., Allen, P.G. Biochemistry (2000) [Pubmed]
  6. Differential developmentally regulated expression of gelsolin family members in the mouse. Arai, M., Kwiatkowski, D.J. Dev. Dyn. (1999) [Pubmed]
  7. Immune-specific up-regulation of adseverin gene expression by 2,3,7,8-tetrachlorodibenzo-p-dioxin. Svensson, C., Lundberg, K. Mol. Pharmacol. (2001) [Pubmed]
  8. Scinderin-derived actin-binding peptides inhibit Ca(2+)- and GTPgammaS-dependent exocytosis in mouse pancreatic beta-cells. Bruun, T.Z., Høy, M., Gromada, J. Eur. J. Pharmacol. (2000) [Pubmed]
  9. Dioxin-induced adseverin expression in the mouse thymus is strictly regulated and dependent on the aryl hydrocarbon receptor. Svensson, C., Silverstone, A.E., Lai, Z.W., Lundberg, K. Biochem. Biophys. Res. Commun. (2002) [Pubmed]
  10. Direct visualization of bipolar myosin filaments in stress fibers of cultured fibroblasts. Svitkina, T.M., Surguchova, I.G., Verkhovsky, A.B., Gelfand, V.I., Moeremans, M., De Mey, J. Cell Motil. Cytoskeleton (1989) [Pubmed]
  11. Organization of stress fibers in cultured fibroblasts after extraction of actin with bovine brain gelsolin-like protein. Verkhovsky, A.B., Surgucheva, I.G., Svitkina, T.M., Tint, I.S., Gelfand, V.I. Exp. Cell Res. (1987) [Pubmed]
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