The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

Links

 

Gene Review

VIL1  -  villin 1

Homo sapiens

Synonyms: D2S1471, VIL, Villin-1
 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

Disease relevance of VIL1

  • Villin expression during assembly of the brush border can be investigated using a human colon adenocarcinoma cell line HT29-18 [1].
  • Intestinal metaplasia in the stomach is defined by the presence of intestine-like cells expressing enterocyte-specific markers, such as villin [2].
  • Extensive in vitro proteolysis with Staphylococcus aureus V8 protease results in the production of a stable domain (apparent Mr 44000) which can be isolated due to its Ca2+-dependent interaction with G-actin bound to immobilized DNase-I, the standard procedure for the purification of villin [3].
  • We raised monoclonal antibodies to villin and used them to localize it in human ileum and colon and in 22 colonic neoplasms [4].
  • Presence of villin, a tissue-specific cytoskeletal protein, in sera of patients and an initial clinical evaluation of its value for the diagnosis and follow-up of colorectal cancers [5].
 

Psychiatry related information on VIL1

  • Although individual responses to VIL were variable, there was an over-all improvement of about 1 1/2 SD in neuropsychological test performance during VIL treatment [6].
 

High impact information on VIL1

  • The actin-binding protein villin induces microvillus growth and reorganization of the cytoskeleton in cells that do not normally produce this protein [7].
  • Transfection of mutagenized villin cDNAs into CV-1 cells was used to show that a conserved, COOH-terminally located cluster of charged amino acid residues (KKEK) is crucial for the morphogenic activity of villin in vivo [7].
  • Chemical cross-linking of actin to this peptide, the effects of amino acid substitutions in peptides, and the behavior of villin variants further corroborate the participation of the KKEK sequence in actin contacts [7].
  • Villin lacking one actin-binding domain (113 amino acids), located at its carboxyterminal end, did not induce growth if microvilli or stress fiber disruption [8].
  • The function of villin, an actin-binding protein, has been investigated by transfecting fibroblasts with cloned human cDNAs encoding wild-type villin or functional villin domains [8].
 

Chemical compound and disease context of VIL1

 

Biological context of VIL1

 

Anatomical context of VIL1

 

Associations of VIL1 with chemical compounds

 

Physical interactions of VIL1

  • The C-terminal actin-binding site in the ERM proteins and the actin-binding helix in the villin headpiece have a common amino acid motif [21].
  • We have employed a structure-based design to construct a small folding domain from the F-actin bundling protein villin that contains the amino acids necessary for the DNA binding of the basic leucine zipper protein GCN4 and have compared its DNA binding with GCN4 [22].
 

Enzymatic interactions of VIL1

 

Regulatory relationships of VIL1

  • The results show that all 40 (100%) colorectal adenocarcinomas expressed CDX2 and 39 (98%) expressed villin [12].
  • This inhibitor abolished the HGF-induced increase in villin levels before, but not after, confluence [25].
 

Other interactions of VIL1

  • The difficulties observed for LDHA and VIL1 are probably due to the fact that these genes belong to large gene families and therefore suggest that they may not be the most appropriate markers for a standardisation effort [26].
  • We observed inducible binding of Elk-1 and the SRF after 3 and 24 h of treatment with H. pylori, suggesting that the bacteria alone are sufficient to initiate a cascade of signaling events responsible for villin expression [2].
  • Some tubular formations showed signs of proximal maturation with the presence of CALLA, CD26, and even villin [27].
  • This result excludes fibronectin, villin, and desmin from being the causative genes for GFD in this large kindred [28].
  • In 99 individuals haplotype analysis was performed using 6 microsatellite markers spanning a > 56 cM interval in chromosome region 2q34, where fibronectin, villin, and desmin map in close proximity [28].
 

Analytical, diagnostic and therapeutic context of VIL1

  • In this work, specific PCR systems were developed for each of the marker genes except VIL1 (see results), from either existing bovine or human sequences, and a bovine BAC library was screened to obtain the corresponding BAC clones [26].
  • Functional dissection and molecular characterization of calcium-sensitive actin-capping and actin-depolymerizing sites in villin [29].
  • As shown by immunofluorescence and immunogold labelings, villin is targeted to the brush border area of differentiated HT29-18 cells but remains diffusely distributed in undifferentiated ones [30].
  • Microinjection of villin into cultured cells induces rapid and long-lasting changes in cell morphology but does not inhibit cytokinesis, cell motility, or membrane ruffling [31].
  • In addition an ELISA has been set up to measure villin accurately in total cell extracts [30].

References

  1. A human villin cDNA clone to investigate the differentiation of intestinal and kidney cells in vivo and in culture. Pringault, E., Arpin, M., Garcia, A., Finidori, J., Louvard, D. EMBO J. (1986) [Pubmed]
  2. Helicobacter-induced intestinal metaplasia in the stomach correlates with Elk-1 and serum response factor induction of villin. Rieder, G., Tessier, A.J., Qiao, X.T., Madison, B., Gumucio, D.L., Merchant, J.L. J. Biol. Chem. (2005) [Pubmed]
  3. Isolation of a domain of villin retaining calcium-dependent interaction with G-actin, but devoid of F-actin fragmenting activity. Hesterberg, L.K., Weber, K. Eur. J. Biochem. (1986) [Pubmed]
  4. Localization of villin, a cytoskeletal protein specific to microvilli, in human ileum and colon and in colonic neoplasms. West, A.B., Isaac, C.A., Carboni, J.M., Morrow, J.S., Mooseker, M.S., Barwick, K.W. Gastroenterology (1988) [Pubmed]
  5. Presence of villin, a tissue-specific cytoskeletal protein, in sera of patients and an initial clinical evaluation of its value for the diagnosis and follow-up of colorectal cancers. Dudouet, B., Jacob, L., Beuzeboc, P., Magdelenat, H., Robine, S., Chapuis, Y., Christoforov, B., Cremer, G.A., Pouillard, P., Bonnichon, P. Cancer Res. (1990) [Pubmed]
  6. Preliminary support for the oral administration of valine, isoleucine and leucine for phenylketonuria. Jordan, M.K., Brunner, R.L., Hunt, M.M., Berry, H.K. Developmental medicine and child neurology. (1985) [Pubmed]
  7. An actin-binding site containing a conserved motif of charged amino acid residues is essential for the morphogenic effect of villin. Friederich, E., Vancompernolle, K., Huet, C., Goethals, M., Finidori, J., Vandekerckhove, J., Louvard, D. Cell (1992) [Pubmed]
  8. Villin induces microvilli growth and actin redistribution in transfected fibroblasts. Friederich, E., Huet, C., Arpin, M., Louvard, D. Cell (1989) [Pubmed]
  9. Atypical bile duct adenoma, clear cell type: a previously undescribed tumor of the liver. Albores-Saavedra, J., Hoang, M.P., Murakata, L.A., Sinkre, P., Yaziji, H. Am. J. Surg. Pathol. (2001) [Pubmed]
  10. Reduction of cerebrospinal fluid phenylalanine after oral administration of valine, isoleucine, and leucine. Berry, H.K., Bofinger, M.K., Hunt, M.M., Phillips, P.J., Guilfoile, M.B. Pediatr. Res. (1982) [Pubmed]
  11. Heparin inhibition of antibody-dependent complement-mediated lysis. Wesolowski, J., Ault, K., Houghton, R., Parkman, R. Exp. Hematol. (1984) [Pubmed]
  12. Value of CDX2, villin, and alpha-methylacyl coenzyme A racemase immunostains in the distinction between primary adenocarcinoma of the bladder and secondary colorectal adenocarcinoma. Suh, N., Yang, X.J., Tretiakova, M.S., Humphrey, P.A., Wang, H.L. Mod. Pathol. (2005) [Pubmed]
  13. Immunolocalization of integrins in the normal and neoplastic colonic epithelium. Koukoulis, G.K., Virtanen, I., Moll, R., Quaranta, V., Gould, V.E. Virchows Arch., B, Cell Pathol. (1993) [Pubmed]
  14. Sequence of human villin: a large duplicated domain homologous with other actin-severing proteins and a unique small carboxy-terminal domain related to villin specificity. Arpin, M., Pringault, E., Finidori, J., Garcia, A., Jeltsch, J.M., Vandekerckhove, J., Louvard, D. J. Cell Biol. (1988) [Pubmed]
  15. Structure of the human villin gene. Pringault, E., Robine, S., Louvard, D. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  16. Villin is a major protein of the microvillus cytoskeleton which binds both G and F actin in a calcium-dependent manner. Bretscher, A., Weber, K. Cell (1980) [Pubmed]
  17. Tropomyosin distinguishes between the two actin-binding sites of villin and affects actin-binding properties of other brush border proteins. Burgess, D.R., Broschat, K.O., Hayden, J.M. J. Cell Biol. (1987) [Pubmed]
  18. Regulation of cell motility by tyrosine phosphorylated villin. Tomar, A., Wang, Y., Kumar, N., George, S., Ceacareanu, B., Hassid, A., Chapman, K.E., Aryal, A.M., Waters, C.M., Khurana, S. Mol. Biol. Cell (2004) [Pubmed]
  19. Dynamic effects of acid on Barrett's esophagus. An ex vivo proliferation and differentiation model. Fitzgerald, R.C., Omary, M.B., Triadafilopoulos, G. J. Clin. Invest. (1996) [Pubmed]
  20. Dihydrofolate reductase gene amplification-associated shift of differentiation in methotrexate-adapted HT-29 cells. Lesuffleur, T., Barbat, A., Luccioni, C., Beaumatin, J., Clair, M., Kornowski, A., Dussaulx, E., Dutrillaux, B., Zweibaum, A. J. Cell Biol. (1991) [Pubmed]
  21. Structure-function relationships in the ezrin family and the effect of tumor-associated point mutations in neurofibromatosis 2 protein. Turunen, O., Sainio, M., Jääskeläinen, J., Carpén, O., Vaheri, A. Biochim. Biophys. Acta (1998) [Pubmed]
  22. Structure-based design of a leucine zipper protein with new DNA contacting region. Morii, T., Sato, S., Hagihara, M., Mori, Y., Imoto, K., Makino, K. Biochemistry (2002) [Pubmed]
  23. Regulation of actin dynamics by tyrosine phosphorylation: identification of tyrosine phosphorylation sites within the actin-severing domain of villin. Zhai, L., Kumar, N., Panebra, A., Zhao, P., Parrill, A.L., Khurana, S. Biochemistry (2002) [Pubmed]
  24. Regulation of phospholipase C-gamma(1) by the actin-regulatory protein villin. Panebra, A., Ma, S.X., Zhai, L.W., Wang, X.T., Rhee, S.G., Khurana, S. Am. J. Physiol., Cell Physiol. (2001) [Pubmed]
  25. HGF upregulates and modifies subcellular distribution of proteins in colon cancer cell enterocytic differentiation. Kermorgant, S., Dessirier, V., Lewin, M.J., Lehy, T. Am. J. Physiol. Gastrointest. Liver Physiol. (2001) [Pubmed]
  26. Development and assignment of bovine-specific PCR systems for the Texas nomenclature marker genes and isolation of homologous BAC probes. Gautier, M., Laurent, P., Hayes, H., Eggen, A. Genet. Sel. Evol. (2001) [Pubmed]
  27. Cell differentiation in Wilms' tumor (nephroblastoma): an immunohistochemical study. Droz, D., Rousseau-Merck, M.F., Jaubert, F., Diebold, N., Nezelof, C., Adafer, E., Mouly, H. Hum. Pathol. (1990) [Pubmed]
  28. Glomerulopathy associated with predominant fibronectin deposits: exclusion of the genes for fibronectin, villin and desmin as causative genes. Hildebrandt, F., Strahm, B., Prochoroff, A., Cybulla, M., Gemperle, O., Krapf, R., Brandis, M. Am. J. Med. Genet. (1996) [Pubmed]
  29. 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]
  30. Changes in villin synthesis and subcellular distribution during intestinal differentiation of HT29-18 clones. Dudouet, B., Robine, S., Huet, C., Sahuquillo-Merino, C., Blair, L., Coudrier, E., Louvard, D. J. Cell Biol. (1987) [Pubmed]
  31. Microinjection of villin into cultured cells induces rapid and long-lasting changes in cell morphology but does not inhibit cytokinesis, cell motility, or membrane ruffling. Franck, Z., Footer, M., Bretscher, A. J. Cell Biol. (1990) [Pubmed]
 
WikiGenes - Universities