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Gene Review

SCIN  -  scinderin

Homo sapiens

Synonyms: Adseverin, KIAA1905, Scinderin, adseverin
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Disease relevance of SCIN

  • In Staphylococcus aureus phages encoding immune evasion molecules (SAK, SCIN, CHIPS), which integrate specifically into the beta-haemolysin (Hlb) gene, are widely distributed [1].
  • Scale for chemotherapy-induced long-term neurotoxicity (SCIN): psychometrics, validation, and findings in a large sample of testicular cancer survivors [2].
  • METHODS: As part of a questionnaire survey 684 testicular cancer survivors (TCSs) filled in the SCIN, which assesses peripheral sensory neuropathy (paresthesias), Raynaud's phenomenon, and ototoxicity [2].

Psychiatry related information on SCIN

  • CONCLUSION: The SCIN shows good psychometric properties, and is recommended as a brief screening instrument for chemotheraphy-indeed neurotoxicity [2].

High impact information on SCIN

  • Nicotinic stimulation and high K(+)-depolarization of chromaffin cells cause disassembly of cortical filamentous actin networks and redistribution of scinderin, a Ca(2+)-dependent actin filament-severing protein [3].
  • Here we report that PMA, a PKC activator, caused scinderin redistribution, although with a slower onset than that induced by nicotine [3].
  • Activation of scinderin by Ca2+ may cause disassembly of actin filaments leaving cortical areas of low cytoplasmic viscosity which are the sites of exocytosis (Vitale, M. L., A. Rodríguez Del Castillo, L. Tchakarov, and J.-M. Trifaró. 1991. J. Cell. Biol. 113:1057-1067) [3].
  • Ca2+ and pH determine the interaction of chromaffin cell scinderin with phosphatidylserine and phosphatidylinositol 4,5,-biphosphate and its cellular distribution during nicotinic-receptor stimulation and protein kinase C activation [3].
  • Scinderin was not phosphorylated by the kinase and further experiments using the Na+/H+ antiport inhibitors and intracellular pH determinations, demonstrated that PKC-mediated scinderin redistribution was a consequence of an increase in intracellular pH [3].

Biological context of SCIN


Anatomical context of SCIN


Associations of SCIN with chemical compounds

  • Double staining immunocytochemical studies with antibodies against scinderin and rhodamine phalloidin, a probe for F-actin, also demonstrated the presence of scinderin in platelets [10].
  • EGTA eluates from the affinity columns contained scinderin as demonstrated by mono and two-dimensional polyacrylamide gel electrophoresis and immunoblotting with scinderin antibodies [10].
  • The individual cumulative cisplatin dose correlated significantly with all the SCIN items [2].
  • Moreover, it was shown that scinderin binds to phosphatidylserine and phosphatidylinositol 4,5-biphosphate liposomes in a Ca(2+)-dependent manner, an effect which was modulated by the pH [3].
  • Recombinant scinderin and peptides Sc-ABP1 and Sc-ABP2 were tested for their effects on Ca(2+)-induced serotonin release from digitonin permeabilized platelets [11].

Other interactions of SCIN

  • All proteins of the villin superfamily, which includes the actin-capping and -severing proteins such as gelsolin, scinderin, and severin, are calcium-regulated actin-modifying proteins [12].
  • The dynamics of cortical F-actin is controlled by two mechanisms: a) stimulation-induced Ca2+ entry and scinderin activation and b) protein kinase C (PKC) activation and MARCKS phosphorylation as demonstrated here by experiments with recombinant proteins, antisense olygodeoxynucleotides and vector mediated transient expressions [13].
  • More notably, we found that actin-related genes ephrin-A1 and scinderin were overexpressed in resistant target [14].

Analytical, diagnostic and therapeutic context of SCIN

  • The aim of this study was to explore the psychometric properties of a brief self-report scale for chemotherapy induced long-term neurotoxicity (the SCIN) [2].
  • Scinderin, which is structurally different from gelsolin (different pIs, amino acid composition, peptide maps, and so on), decreases the viscosity of actin gels as a result of its F-actin-severing properties, as demonstrated by electron microscopy [9].


  1. Extensive phage dynamics in Staphylococcus aureus contributes to adaptation to the human host during infection. Goerke, C., Wirtz, C., Flückiger, U., Wolz, C. Mol. Microbiol. (2006) [Pubmed]
  2. Scale for chemotherapy-induced long-term neurotoxicity (SCIN): psychometrics, validation, and findings in a large sample of testicular cancer survivors. Oldenburg, J., Fosså, S.D., Dahl, A.A. Quality of life research : an international journal of quality of life aspects of treatment, care and rehabilitation. (2006) [Pubmed]
  3. Ca2+ and pH determine the interaction of chromaffin cell scinderin with phosphatidylserine and phosphatidylinositol 4,5,-biphosphate and its cellular distribution during nicotinic-receptor stimulation and protein kinase C activation. Rodríguez Del Castillo, A., Vitale, M.L., Trifaró, J.M. J. Cell Biol. (1992) [Pubmed]
  4. Expression of scinderin in megakaryoblastic leukemia cells induces differentiation, maturation, and apoptosis with release of plateletlike particles and inhibits proliferation and tumorigenesis. Zunino, R., Li, Q., Rosé, S.D., Romero-Benítez, M.M., Lejen, T., Brandan, N.C., Trifaró, J.M. Blood (2001) [Pubmed]
  5. Two pathways control chromaffin cell cortical F-actin dynamics during exocytosis. Trifaró, J., Rosé, S.D., Lejen, T., Elzagallaai, A. Biochimie (2000) [Pubmed]
  6. Scinderin, a Ca2+-dependent actin filament severing protein that controls cortical actin network dynamics during secretion. Trifaró, J.M., Rosé, S.D., Marcu, M.G. Neurochem. Res. (2000) [Pubmed]
  7. The role of different Scinderin domains in the control of F-actin cytoskeleton during exocytosis. Lejen, T., Pene, T.D., Rosé, S.D., Trifaró, J.M. Ann. N. Y. Acad. Sci. (2002) [Pubmed]
  8. Localization by segmental deletion analysis and functional characterization of a third actin-binding site in domain 5 of scinderin. Marcu, M.G., Zhang, L., Elzagallaai, A., Trifaró, J.M. J. Biol. Chem. (1998) [Pubmed]
  9. Dynamic changes in chromaffin cell cytoskeleton as prelude to exocytosis. Trifaró, J.M., Rodríguez del Castillo, A., Vitale, M.L. Mol. Neurobiol. (1992) [Pubmed]
  10. Human platelets contain scinderin, a Ca(2+)-dependent actin filament-severing protein. Rodríguez Del Castillo, A., Vitale, M.L., Tchakarov, L., Trifaró, J.M. Thromb. Haemost. (1992) [Pubmed]
  11. Recombinant scinderin, an F-actin severing protein, increases calcium-induced release of serotonin from permeabilized platelets, an effect blocked by two scinderin-derived actin-binding peptides and phosphatidylinositol 4,5-bisphosphate. Marcu, M.G., Zhang, L., Nau-Staudt, K., Trifaró, J.M. Blood (1996) [Pubmed]
  12. Functional dissection and molecular characterization of calcium-sensitive actin-capping and actin-depolymerizing sites in villin. Kumar, N., Tomar, A., Parrill, A.L., Khurana, S. J. Biol. Chem. (2004) [Pubmed]
  13. Pathways that control cortical F-actin dynamics during secretion. Trifaró, J.M., Lejen, T., Rosé, S.D., Pene, T.D., Barkar, N.D., Seward, E.P. Neurochem. Res. (2002) [Pubmed]
  14. Identification of target actin content and polymerization status as a mechanism of tumor resistance after cytolytic T lymphocyte pressure. Abouzahr, S., Bismuth, G., Gaudin, C., Caroll, O., Van Endert, P., Jalil, A., Dausset, J., Vergnon, I., Richon, C., Kauffmann, A., Galon, J., Raposo, G., Mami-Chouaib, F., Chouaib, S. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
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