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Vim  -  vimentin

Rattus norvegicus

Synonyms: Vimentin
 
 
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Disease relevance of Vim

 

High impact information on Vim

  • Expression of IF proteins depends on the route of cell differentiation and five major subclasses of IF proteins have been distinguished: of these, cytokeratins are typical of epithelial cells whereas vimentin occurs in mesenchymally derived cells and some other non-epithelial cells [5].
  • Vimentin binds phosphorylated Erks (pErk), thus linking pErk to the dynein retrograde motor via direct binding of vimentin to importin beta [6].
  • Scanning and transmission electron microscopy showed that Ptpro(-/-) mice had an amoeboid rather than the typical octopoid structure seen in the wild-type mouse podocyte and that there were blunting and widening of the minor (foot) processes in association with altered distribution of the podocyte intermediate cytoskeletal protein vimentin [7].
  • Likewise, none of the PCNA or vimentin-positive cells expressed clusterin at detectable levels [8].
  • An increase in desmin and vimentin in mesangial regions was also noted [9].
 

Chemical compound and disease context of Vim

 

Biological context of Vim

 

Anatomical context of Vim

 

Associations of Vim with chemical compounds

  • Only in DMSO-supplemented cultures was vimentin expression of hepatocytes inhibited and no coexpression was observed in the presence of this factor [20].
  • Using a bank of defined antibody markers, we confirmed nestin's pattern of distribution to be different from that of cytokeratin, vimentin, GBC-1, GAP43, and carnosine [21].
  • Markers for astroglial progenitors were vimentin, nestin, zebrin II, and the astroglial-specific glutamate transporter subtype GLAST [22].
  • BACKGROUND: Immunocytochemical analysis of liver has revealed that fat-storing cells (FSC) are heterogeneous with regard to vitamin A content, staining for cytokeratins, desmin, and vimentin and the cytoskeletal protein alpha-smooth muscle actin [23].
  • Treatment of primary cultures of oligodendrocyte precursors with calyculin A, a potent inhibitor of protein phosphatases 1 and 2A, caused the phosphorylation of two intermediate filament components, nestin and vimentin [24].
 

Physical interactions of Vim

 

Enzymatic interactions of Vim

  • Comparative analysis of tryptic phosphopeptide maps also indicates that corresponding phosphopeptides emerged in vimentin from OA-treated cells and were phosphorylated by MAPKAPK-2 [26].
  • Two-dimensional phosphopeptide maps of vimentin indicated that a major phosphopeptide phosphorylated by the endogenous calmodulin-dependent kinase also appears to be the same as a major phosphopeptide phosphorylated by the exogenous Ca2+/calmodulin-dependent protein kinase II [27].
 

Co-localisations of Vim

  • Unlike in IF-containing cells, where plectin colocalized largely with the vimentin network, in the IF-negative subclone the protein was mainly associated with polymeric actin structures [28].
 

Regulatory relationships of Vim

 

Other interactions of Vim

 

Analytical, diagnostic and therapeutic context of Vim

References

  1. Induction of Hsp27 and Hsp32 stress proteins and vimentin in glial cells of the rat hippocampus following hyperthermia. Bechtold, D.A., Brown, I.R. Neurochem. Res. (2003) [Pubmed]
  2. Embryonic intermediate filaments, nestin and vimentin, expression in the spinal cords of rats with experimental autoimmune encephalomyelitis. Shin, T.K., Lee, Y.D., Sim, K.B. J. Vet. Sci. (2003) [Pubmed]
  3. Effect of vimentin on reactive gliosis: in vitro and in vivo analysis. Lin, J., Cai, W. J. Neurotrauma (2004) [Pubmed]
  4. Differentiation of malignant oral rat keratinocytes reflects changes in EGF and TGF-beta receptor expression but not growth factor dependence. Game, S.M., Stone, A., Matthews, J.B., Scully, C., Prime, S.S. Carcinogenesis (1991) [Pubmed]
  5. Cessation of cytokeratin expression in a rat hepatoma cell line lacking differentiated functions. Venetianer, A., Schiller, D.L., Magin, T., Franke, W.W. Nature (1983) [Pubmed]
  6. Vimentin-dependent spatial translocation of an activated MAP kinase in injured nerve. Perlson, E., Hanz, S., Ben-Yaakov, K., Segal-Ruder, Y., Seger, R., Fainzilber, M. Neuron (2005) [Pubmed]
  7. Altered podocyte structure in GLEPP1 (Ptpro)-deficient mice associated with hypertension and low glomerular filtration rate. Wharram, B.L., Goyal, M., Gillespie, P.J., Wiggins, J.E., Kershaw, D.B., Holzman, L.B., Dysko, R.C., Saunders, T.L., Samuelson, L.C., Wiggins, R.C. J. Clin. Invest. (2000) [Pubmed]
  8. Localization of proliferating cell nuclear antigen, vimentin, c-Fos, and clusterin in the postischemic kidney. Evidence for a heterogenous genetic response among nephron segments, and a large pool of mitotically active and dedifferentiated cells. Witzgall, R., Brown, D., Schwarz, C., Bonventre, J.V. J. Clin. Invest. (1994) [Pubmed]
  9. Expression of smooth muscle cell phenotype by rat mesangial cells in immune complex nephritis. Alpha-smooth muscle actin is a marker of mesangial cell proliferation. Johnson, R.J., Iida, H., Alpers, C.E., Majesky, M.W., Schwartz, S.M., Pritzi, P., Gordon, K., Gown, A.M. J. Clin. Invest. (1991) [Pubmed]
  10. Cardiac renin-angiotensin system in the hypertrophied heart. Iwai, N., Shimoike, H., Kinoshita, M. Circulation (1995) [Pubmed]
  11. Cytoplasmic retention of mutant tsp53 is dependent on an intermediate filament protein (vimentin) scaffold. Klotzsche, O., Etzrodt, D., Hohenberg, H., Bohn, W., Deppert, W. Oncogene (1998) [Pubmed]
  12. Transdifferentiation of cultured tubular cells induced by hypoxia. Manotham, K., Tanaka, T., Matsumoto, M., Ohse, T., Inagi, R., Miyata, T., Kurokawa, K., Fujita, T., Ingelfinger, J.R., Nangaku, M. Kidney Int. (2004) [Pubmed]
  13. Expression of vimentin and glial fibrillary acidic protein in ethylnitrosourea-induced rat gliomas and glioma cell lines. Reifenberger, G., Bilzer, T., Seitz, R.J., Wechsler, W. Acta Neuropathol. (1989) [Pubmed]
  14. Calcium cataract: a model for optical anisotropy fluctuations. Bettelheim, F.A., Qin, C., Zigler, J.S. Exp. Eye Res. (1995) [Pubmed]
  15. Propionic acid induces cytoskeletal alterations in cultured astrocytes from rat cerebral cortex. de Almeida, L.M., Funchal, C., Gottfried, C., Wajner, M., Pessoa-Pureur, R. Metabolic brain disease. (2006) [Pubmed]
  16. Microscopic Characterization of Follicular Structures in Letrozole-induced Polycystic Ovarian Syndrome in the Rat. Baravalle, C., Salvetti, N.R., Mira, G.A., Pezzone, N., Ortega, H.H. Arch. Med. Res. (2006) [Pubmed]
  17. Differential expression of vimentin in rat prostatic tumors. Bussemakers, M.J., Verhaegh, G.W., van Bokhoven, A., Debruyne, F.M., Schalken, J.A. Biochem. Biophys. Res. Commun. (1992) [Pubmed]
  18. Simvastatin attenuates renal inflammation, tubular transdifferentiation and interstitial fibrosis in rats with unilateral ureteral obstruction. Vieira, J.M., Mantovani, E., Rodrigues, L.T., Dellê, H., Noronha, I.L., Fujihara, C.K., Zatz, R. Nephrol. Dial. Transplant. (2005) [Pubmed]
  19. Activation of embryonic intermediate filaments contributes to glial scar formation after spinal cord injury in rats. Kim, D.H., Heo, S.D., Ahn, M.J., Sim, K.B., Shin, T.K. J. Vet. Sci. (2003) [Pubmed]
  20. Growth and differentiation factors inhibit the migratory phenotype of cultured neonatal rat hepatocytes induced by HGF/SF. Pagan, R., Martín, I., Llobera, M., Vilaró, S. Exp. Cell Res. (1997) [Pubmed]
  21. Expression of the intermediate filament protein nestin by sustentacular cells in mature olfactory neuroepithelium. Doyle, K.L., Khan, M., Cunningham, A.M. J. Comp. Neurol. (2001) [Pubmed]
  22. Progenitors in the postnatal cerebellar white matter are antigenically heterogeneous. Milosevic, A., Goldman, J.E. J. Comp. Neurol. (2002) [Pubmed]
  23. Liver fat-storing cell clones obtained from a CCl4-cirrhotic rat are heterogeneous with regard to proliferation, expression of extracellular matrix components, interleukin-6, and connexin 43. Greenwel, P., Rubin, J., Schwartz, M., Hertzberg, E.L., Rojkind, M. Lab. Invest. (1993) [Pubmed]
  24. Phosphorylation and disruption of intermediate filament proteins in oligodendrocyte precursor cultures treated with calyculin A. Almazan, G., Afar, D.E., Bell, J.C. J. Neurosci. Res. (1993) [Pubmed]
  25. Cytoskeleton-associated plectin: in situ localization, in vitro reconstitution, and binding to immobilized intermediate filament proteins. Foisner, R., Leichtfried, F.E., Herrmann, H., Small, J.V., Lawson, D., Wiche, G. J. Cell Biol. (1988) [Pubmed]
  26. Identification of mitogen-activated protein kinase-activated protein kinase-2 as a vimentin kinase activated by okadaic acid in 9L rat brain tumor cells. Cheng, T.J., Lai, Y.K. J. Cell. Biochem. (1998) [Pubmed]
  27. Ca2+/calmodulin-dependent protein phosphorylation associated with the cytoskeleton of quiescent rat fibroblast (3Y1) cells. Terasawa, M., Tokumitsu, H., Kobayashi, R., Hidaka, H. J. Biochem. (1991) [Pubmed]
  28. Distribution and ultrastructure of plectin arrays in subclones of rat glioma C6 cells differing in intermediate filament protein (vimentin) expression. Foisner, R., Bohn, W., Mannweiler, K., Wiche, G. J. Struct. Biol. (1995) [Pubmed]
  29. Nestin promotes the phosphorylation-dependent disassembly of vimentin intermediate filaments during mitosis. Chou, Y.H., Khuon, S., Herrmann, H., Goldman, R.D. Mol. Biol. Cell (2003) [Pubmed]
  30. Rac1 regulates heat shock responses by reorganization of vimentin filaments: identification using MALDI-TOF MS. Lee, S.Y., Song, E.J., Kim, H.J., Kang, H.J., Kim, J.H., Lee, K.J. Cell Death Differ. (2001) [Pubmed]
  31. Vimentin filaments follow the preexisting cytokeratin network during epithelial-mesenchymal transition of cultured neonatal rat hepatocytes. Pagan, R., Martín, I., Alonso, A., Llobera, M., Vilaró, S. Exp. Cell Res. (1996) [Pubmed]
  32. Upregulation of metabotropic glutamate receptor subtype mGluR3 and mGluR5 in reactive astrocytes in a rat model of mesial temporal lobe epilepsy. Aronica, E., van Vliet, E.A., Mayboroda, O.A., Troost, D., da Silva, F.H., Gorter, J.A. Eur. J. Neurosci. (2000) [Pubmed]
  33. A high molecular weight intermediate filament-associated protein in BHK-21 cells is nestin, a type VI intermediate filament protein. Limited co-assembly in vitro to form heteropolymers with type III vimentin and type IV alpha-internexin. Steinert, P.M., Chou, Y.H., Prahlad, V., Parry, D.A., Marekov, L.N., Wu, K.C., Jang, S.I., Goldman, R.D. J. Biol. Chem. (1999) [Pubmed]
  34. Nestin-immunoreactive cells in rat pituitary are neither hormonal nor typical folliculo-stellate cells. Krylyshkina, O., Chen, J., Mebis, L., Denef, C., Vankelecom, H. Endocrinology (2005) [Pubmed]
  35. Plectin sidearms mediate interaction of intermediate filaments with microtubules and other components of the cytoskeleton. Svitkina, T.M., Verkhovsky, A.B., Borisy, G.G. J. Cell Biol. (1996) [Pubmed]
  36. Class VI intermediate filament protein nestin is induced during activation of rat hepatic stellate cells. Niki, T., Pekny, M., Hellemans, K., Bleser, P.D., Berg, K.V., Vaeyens, F., Quartier, E., Schuit, F., Geerts, A. Hepatology (1999) [Pubmed]
  37. Migratory capacity of the cell line RN33B and the host glial cell response after subretinal transplantation to normal adult rats. Wojciechowski, A.B., Englund, U., Lundberg, C., Warfvinge, K. Glia (2004) [Pubmed]
  38. Ultrastructure of intermediate filaments of nestin- and vimentin-immunoreactive astrocytes in organotypic slice cultures of hippocampus. Miyaguchi, K. J. Struct. Biol. (1997) [Pubmed]
 
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