Abstract
Vimentin, a major constituent of the intermediate filament family of proteins, is ubiquitously expressed in normal mesenchymal cells and is known to maintain cellular integrity and provide resistance against stress. Vimentin is overexpressed in various epithelial cancers, including prostate cancer, gastrointestinal tumors, tumors of the central nervous system, breast cancer, malignant melanoma, and lung cancer. Vimentin’s overexpression in cancer correlates well with accelerated tumor growth, invasion, and poor prognosis; however, the role of vimentin in cancer progression remains obscure. In recent years, vimentin has been recognized as a marker for epithelial–mesenchymal transition (EMT). Although EMT is associated with several tumorigenic events, vimentin’s role in the underlying events mediating these processes remains unknown. By virtue of its overexpression in cancer and its association with tumor growth and metastasis, vimentin serves as an attractive potential target for cancer therapy; however, more research would be crucial to evaluate its specific role in cancer. Our recent discovery of a vimentin-binding mini-peptide has generated further impetus for vimentin-targeted tumor-specific therapy. Furthermore, research directed toward elucidating the role of vimentin in various signaling pathways would reveal new approaches for the development of therapeutic agents. This review summarizes the expression and functions of vimentin in various types of cancer and suggests some directions toward future cancer therapy utilizing vimentin as a potential molecular target.
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Hesse M, Magin TM, Weber K (2001) Genes for intermediate filament proteins and the draft sequence of the human genome: novel keratin genes and a surprisingly high number of pseudogenes related to keratin genes 8 and 18. J Cell Sci 114:2569–2575
Fuchs E, Weber K (1994) Intermediate filaments: structure, dynamics, function, and disease. Annu Rev Biochem 63:345–382
Niki T, Pekny M, Hellemans K, Bleser PD, Berg KV, Vaeyens F, Quartier E et al (1999) Class VI intermediate filament protein nestin is induced during activation of rat hepatic stellate cells. Hepatology 29:520–527
Green KJ, Bohringer M, Gocken T, Jones JC (2005) Intermediate filament associated proteins. Adv Protein Chem 70:143–202
Franke WW, Grund C, Kuhn C, Jackson BW, Illmensee K (1982) Formation of cytoskeletal elements during mouse embryogenesis. III. Primary mesenchymal cells and the first appearance of vimentin filaments. Differentiation 23:43–59
Larsson A, Wilhelmsson U, Pekna M, Pekny M (2004) Increased cell proliferation and neurogenesis in the hippocampal dentate gyrus of old GFAP(−/−)Vim(−/−) mice. Neurochem Res 29:2069–2073
Cochard P, Paulin D (1984) Initial expression of neurofilaments and vimentin in the central and peripheral nervous system of the mouse embryo in vivo. J Neurosci 4:2080–2094
de Souza PC, Katz SG (2001) Coexpression of cytokeratin and vimentin in mice trophoblastic giant cells. Tissue Cell 33:40–45
Ko SH, Suh SH, Kim BJ, Ahn YB, Song KH, Yoo SJ, Son HS et al (2004) Expression of the intermediate filament vimentin in proliferating duct cells as a marker of pancreatic precursor cells. Pancreas 28:121–128
Mahrle G, Bolling R, Osborn M, Weber K (1983) Intermediate filaments of the vimentin and prekeratin type in human epidermis. J Invest Dermatol 81:46–48
Carter V, Shenton BK, Jaques B, Turner D, Talbot D, Gupta A, Chapman CE et al (2005) Vimentin antibodies: a non-HLA antibody as a potential risk factor in renal transplantation. Transplant Proc 37:654–657
Evans RM (1998) Vimentin: the conundrum of the intermediate filament gene family. Bioessays 20:79–86
Thiery JP (2002) Epithelial–mesenchymal transitions in tumour progression. Nat Rev Cancer 2:442–454
Chaffer CL, Brennan JP, Slavin JL, Blick T, Thompson EW, Williams ED (2006) Mesenchymal-to-epithelial transition facilitates bladder cancer metastasis: role of fibroblast growth factor receptor-2. Cancer Res 66:11271–11278
Ivaska J, Pallari HM, Nevo J, Eriksson JE (2007) Novel functions of vimentin in cell adhesion, migration, and signaling. Exp Cell Res 313:2050–2062
Colucci-Guyon E, Portier MM, Dunia I, Paulin D, Pournin S, Babinet C (1994) Mice lacking vimentin develop and reproduce without an obvious phenotype. Cell 79:679–694
Eckes B, Colucci-Guyon E, Smola H, Nodder S, Babinet C, Krieg T, Martin P (2000) Impaired wound healing in embryonic and adult mice lacking vimentin. J Cell Sci 113(Pt 13):2455–2462
Eckes B, Dogic D, Colucci-Guyon E, Wang N, Maniotis A, Ingber D, Merckling A et al (1998) Impaired mechanical stability, migration and contractile capacity in vimentin-deficient fibroblasts. J Cell Sci 111(Pt 13):1897–1907
Terzi F, Henrion D, Colucci-Guyon E, Federici P, Babinet C, Levy BI, Briand P et al (1997) Reduction of renal mass is lethal in mice lacking vimentin. Role of endothelin-nitric oxide imbalance. J Clin Invest 100:1520–1528
Schiffers PM, Henrion D, Boulanger CM, Colucci-Guyon E, Langa-Vuves F, van Essen H, Fazzi GE et al (2000) Altered flow-induced arterial remodeling in vimentin-deficient mice. Arterioscler Thromb Vasc Biol 20:611–616
Nieminen M, Henttinen T, Merinen M, Marttila-Ichihara F, Eriksson JE, Jalkanen S (2006) Vimentin function in lymphocyte adhesion and transcellular migration. Nat Cell Biol 8:156–162
Langa F, Kress C, Colucci-Guyon E, Khun H, Vandormael-Pournin S, Huerre M, Babinet C (2000) Teratocarcinomas induced by embryonic stem (ES) cells lacking vimentin: an approach to study the role of vimentin in tumorigenesis. J Cell Sci 113(Pt 19):3463–3472
Goldie KN, Wedig T, Mitra AK, Aebi U, Herrmann H, Hoenger A (2007) Dissecting the 3D structure of vimentin intermediate filaments by cryo-electron tomography. J Struct Biol 158:378–385
Fuchs E, Hanukoglu I (1983) Unraveling the structure of the intermediate filaments. Cell 34:332–334
Ku NO, Liao J, Chou CF, Omary MB (1996) Implications of intermediate filament protein phosphorylation. Cancer Metastasis Rev 15:429–444
Aziz A, Hess JF, Budamagunta MS, Voss JC, Fitzgerald PG Site-directed spin labeling and electron paramagnetic resonance determination of vimentin head domain structure. J Biol Chem 285:15278–15285
Eriksson JE, He T, Trejo-Skalli AV, Harmala-Brasken AS, Hellman J, Chou YH, Goldman RD (2004) Specific in vivo phosphorylation sites determine the assembly dynamics of vimentin intermediate filaments. J Cell Sci 117:919–932
Evans RM (1989) Phosphorylation of vimentin in mitotically selected cells. In vitro cyclic AMP-independent kinase and calcium-stimulated phosphatase activities. J Cell Biol 108:67–78
Huang TJ, Lee TT, Lee WC, Lai YK, Yu JS, Yang SD (1994) Autophosphorylation-dependent protein kinase phosphorylates Ser25, Ser38, Ser65, Ser71, and Ser411 in vimentin and thereby inhibits cytoskeletal intermediate filament assembly. J Protein Chem 13:517–525
Ando S, Tanabe K, Gonda Y, Sato C, Inagaki M (1989) Domain- and sequence-specific phosphorylation of vimentin induces disassembly of the filament structure. Biochemistry 28:2974–2979
Ando S, Tokui T, Yamauchi T, Sugiura H, Tanabe K, Inagaki M (1991) Evidence that Ser-82 is a unique phosphorylation site on vimentin for Ca2(+)-calmodulin-dependent protein kinase II. Biochem Biophys Res Commun 175:955–962
Nakamura Y, Hashimoto R, Amano M, Nagata K, Matsumoto N, Goto H, Fukusho E et al (2000) Localized phosphorylation of vimentin by rho-kinase in neuroblastoma N2a cells. Genes Cells 5:823–837
Cheng TJ, Tseng YF, Chang WM, Chang MD, Lai YK (2003) Retaining of the assembly capability of vimentin phosphorylated by mitogen-activated protein kinase-activated protein kinase-2. J Cell Biochem 89:589–602
Goto H, Tanabe K, Manser E, Lim L, Yasui Y, Inagaki M (2002) Phosphorylation and reorganization of vimentin by p21-activated kinase (PAK). Genes Cells 7:91–97
Goto H, Yasui Y, Kawajiri A, Nigg EA, Terada Y, Tatsuka M, Nagata K et al (2003) Aurora-B regulates the cleavage furrow-specific vimentin phosphorylation in the cytokinetic process. J Biol Chem 278:8526–8530
Turowski P, Myles T, Hemmings BA, Fernandez A, Lamb NJ (1999) Vimentin dephosphorylation by protein phosphatase 2A is modulated by the targeting subunit B55. Mol Biol Cell 10:1997–2015
van Venrooij WJ, Pruijn GJ (2000) Citrullination: a small change for a protein with great consequences for rheumatoid arthritis. Arthritis Res 2:249–251
Vossenaar ER, Radstake TR, van der Heijden A, van Mansum MA, Dieteren C, de Rooij DJ, Barrera P et al (2004) Expression and activity of citrullinating peptidylarginine deiminase enzymes in monocytes and macrophages. Ann Rheum Dis 63:373–381
Farach AM, Galileo DS (2008) O-GlcNAc modification of radial glial vimentin filaments in the developing chick brain. Brain Cell Biol 36:191–202
Liming Wang JZ, Banerjee Sipra, Barnes Laura, Sajja Venkateswara, Liu Yiding, Guo Baochuan, Yuping Du, Agarwal MukeshK, Wald DavidN, Wang Qin, Yang Jinbo (2010) Sumoylation of vimentin354 is associated with PIAS3 inhibition of Glioma cell migration. Oncotarget 1:620–627
Rittling SR, Baserga R (1987) Functional analysis and growth factor regulation of the human vimentin promoter. Mol Cell Biol 7:3908–3915
Lilienbaum A, Paulin D (1993) Activation of the human vimentin gene by the Tax human T-cell leukemia virus. I. Mechanisms of regulation by the NF-kappa B transcription factor. J Biol Chem 268:2180–2188
Rittling SR, Coutinho L, Amram T, Kolbe M (1989) AP-1/jun binding sites mediate serum inducibility of the human vimentin promoter. Nucleic Acids Res 17:1619–1633
Chen JH, Vercamer C, Li Z, Paulin D, Vandenbunder B, Stehelin D (1996) PEA3 transactivates vimentin promoter in mammary epithelial and tumor cells. Oncogene 13:1667–1675
Zhang X, Diab IH, Zehner ZE (2003) ZBP-89 represses vimentin gene transcription by interacting with the transcriptional activator, Sp1. Nucleic Acids Res 31:2900–2914
Wieczorek E, Lin Z, Perkins EB, Law DJ, Merchant JL, Zehner ZE (2000) The zinc finger repressor, ZBP-89, binds to the silencer element of the human vimentin gene and complexes with the transcriptional activator, Sp1. J Biol Chem 275:12879–12888
Gilles C, Polette M, Mestdagt M, Nawrocki-Raby B, Ruggeri P, Birembaut P, Foidart JM (2003) Transactivation of vimentin by beta-catenin in human breast cancer cells. Cancer Res 63:2658–2664
Min C, Eddy SF, Sherr DH, Sonenshein GE (2008) NF-kappaB and epithelial to mesenchymal transition of cancer. J Cell Biochem 104:733–744
Huber MA, Azoitei N, Baumann B, Grunert S, Sommer A, Pehamberger H, Kraut N et al (2004) NF-kappaB is essential for epithelial-mesenchymal transition and metastasis in a model of breast cancer progression. J Clin Invest 114:569–581
Wu Y, Zhang X, Salmon M, Lin X, Zehner ZE (2007) TGFbeta1 regulation of vimentin gene expression during differentiation of the C2C12 skeletal myogenic cell line requires Smads, AP-1 and Sp1 family members. Biochim Biophys Acta 1773:427–439
Shirahata A, Sakata M, Sakuraba K, Goto T, Mizukami H, Saito M, Ishibashi K et al (2009) Vimentin methylation as a marker for advanced colorectal carcinoma. Anticancer Res 29:279–281
Zou H, Harrington JJ, Shire AM, Rego RL, Wang L, Campbell ME, Oberg AL et al (2007) Highly methylated genes in colorectal neoplasia: implications for screening. Cancer Epidemiol Biomarkers Prev 16:2686–2696
Wu Y, Zhang X, Salmon M, Zehner ZE (2007) The zinc finger repressor, ZBP-89, recruits histone deacetylase 1 to repress vimentin gene expression. Genes Cells 12:905–918
Traub P, Shoeman RL (1994) Intermediate filament proteins: cytoskeletal elements with gene-regulatory function? Int Rev Cytol 154:1–103
Hartig R, Shoeman RL, Janetzko A, Tolstonog G, Traub P (1998) DNA-mediated transport of the intermediate filament protein vimentin into the nucleus of cultured cells. J Cell Sci 111(Pt 24):3573–3584
Georgatos SD, Blobel G (1987) Lamin B constitutes an intermediate filament attachment site at the nuclear envelope. J Cell Biol 105:117–125
Mergui X, Puiffe ML, Valteau-Couanet D, Lipinski M, Benard J, Amor-Gueret M p21Waf1 expression is regulated by nuclear intermediate filament vimentin in neuroblastoma. BMC Cancer 10:473
Perides G, Harter C, Traub P (1987) Electrostatic and hydrophobic interactions of the intermediate filament protein vimentin and its amino terminus with lipid bilayers. J Biol Chem 262:13742–13749
Ise H, Kobayashi S, Goto M, Sato T, Kawakubo M, Takahashi M, Ikeda U et al (2010) Vimentin and desmin possess GlcNAc-binding lectin-like properties on cell surfaces. Glycobiology 20:843–864
Cutrera J, Dibra D, Xia X, Hasan A, Reed S, Li S Discovery of a Linear Peptide for Improving Tumor Targeting of Gene Products and Treatment of Distal Tumors by IL-12 Gene Therapy. Mol Ther
Bhattacharya R, Gonzalez AM, Debiase PJ, Trejo HE, Goldman RD, Flitney FW, Jones JC (2009) Recruitment of vimentin to the cell surface by beta3 integrin and plectin mediates adhesion strength. J Cell Sci 122:1390–1400
Ivaska J, Vuoriluoto K, Huovinen T, Izawa I, Inagaki M, Parker PJ (2005) PKCepsilon-mediated phosphorylation of vimentin controls integrin recycling and motility. EMBO J 24:3834–3845
Moisan E, Girard D (2006) Cell surface expression of intermediate filament proteins vimentin and lamin B1 in human neutrophil spontaneous apoptosis. J Leukoc Biol 79:489–498
Kurki P, Virtanen I (1984) The detection of human antibodies against cytoskeletal components. J Immunol Methods 67:209–223
Mor-Vaknin N, Punturieri A, Sitwala K, Markovitz DM (2003) Vimentin is secreted by activated macrophages. Nat Cell Biol 5:59–63
Garg A, Barnes PF, Porgador A, Roy S, Wu S, Nanda JS, Griffith DE et al (2006) Vimentin expressed on Mycobacterium tuberculosis-infected human monocytes is involved in binding to the NKp46 receptor. J Immunol 177:6192–6198
Srivastava BI, Srivastava MD (2006) Expression of natural cytotoxicity receptors NKp30, NKp44, and NKp46 mRNAs and proteins by human hematopoietic and non-hematopoietic cells. Leuk Res 30:37–46
Huet D, Bagot M, Loyaux D, Capdevielle J, Conraux L, Ferrara P, Bensussan A et al (2006) SC5 mAb represents a unique tool for the detection of extracellular vimentin as a specific marker of Sezary cells. J Immunol 176:652–659
Sun S, Poon RT, Lee NP, Yeung C, Chan KL, Ng IO, Day PJ et al (2010) Proteomics of hepatocellular carcinoma: serum vimentin as a surrogate marker for small tumors (< or = 2 cm). J Proteome Res 9:1923–1930
Uchida A, Colot M, Micksche M (1984) Suppression of natural killer cell activity by adherent effusion cells of cancer patients. Suppression of motility, binding capacity and lethal hit of NK cells. Br J Cancer 49:17–23
Ashiru O, Boutet P, Fernandez-Messina L, Aguera-Gonzalez S, Skepper JN, Vales-Gomez M, Reyburn HT (2010) Natural killer cell cytotoxicity is suppressed by exposure to the human NKG2D ligand MICA*008 that is shed by tumor cells in exosomes. Cancer Res 70:481–489
Roghanian A, Jones DC, Pattisapu JV, Wolfe J, Young NT, Behnam B (2010) Filament-associated TSGA10 protein is expressed in professional antigen presenting cells and interacts with vimentin. Cell Immunol 265:120–126
Sukumaran B, Mastronunzio JE, Narasimhan S, Fankhauser S, Uchil PD, Levy R, Graham M et al (2011) Anaplasma phagocytophilum AptA modulates Erk1/2 signalling. Cell Microbiol 13:47–61
Phua DC, Humbert PO, Hunziker W (2009) Vimentin regulates scribble activity by protecting it from proteasomal degradation. Mol Biol Cell 20:2841–2855
Walter M, Chen FW, Tamari F, Wang R, Ioannou YA (2009) Endosomal lipid accumulation in NPC1 leads to inhibition of PKC, hypophosphorylation of vimentin and Rab9 entrapment. Biol Cell 101:141–152
Santilman V, Baran J, Anand-Apte B, Evans RM, Parat MO (2007) Caveolin-1 polarization in transmigrating endothelial cells requires binding to intermediate filaments. Angiogenesis 10:297–305
Svitkina TM, Verkhovsky AB, Borisy GG (1996) Plectin sidearms mediate interaction of intermediate filaments with microtubules and other components of the cytoskeleton. J Cell Biol 135:991–1007
Lieska N, Shao D, Kriho V, Yang HY (1991) Expression and distribution of cytoskeletal IFAP-300 kD as an index of lens cell differentiation. Curr Eye Res 10:1165–1174
Cheng TJ, Lai YK (1994) Transient increase in vimentin phosphorylation and vimentin-HSC70 association in 9L rat brain tumor cells experiencing heat-shock. J Cell Biochem 54:100–109
Brown KD, Binder LI (1992) Identification of the intermediate filament-associated protein gyronemin as filamin. Implications for a novel mechanism of cytoskeletal interaction. J Cell Sci 102(Pt 1):19–30
Song S, Hanson MJ, Liu BF, Chylack LT, Liang JJ (2008) Protein–protein interactions between lens vimentin and alphaB-crystallin using FRET acceptor photobleaching. Mol Vis 14:1282–1287
MacMillan-Crow LA, Lincoln TM (1994) High-affinity binding and localization of the cyclic GMP-dependent protein kinase with the intermediate filament protein vimentin. Biochemistry 33:8035–8043
Ciesielski-Treska J, Ulrich G, Chasserot-Golaz S, Aunis D (1995) Immunocytochemical localization of protein kinases Yes and Src in amoeboid microglia in culture: association of Yes kinase with vimentin intermediate filaments. Eur J Cell Biol 68:369–376
Stappenbeck TS, Bornslaeger EA, Corcoran CM, Luu HH, Virata ML, Green KJ (1993) Functional analysis of desmoplakin domains: specification of the interaction with keratin versus vimentin intermediate filament networks. J Cell Biol 123:691–705
van den Heuvel AP, de Vries-Smits AM, van Weeren PC, Dijkers PF, de Bruyn KM, Riedl JA, Burgering BM (2002) Binding of protein kinase B to the plakin family member periplakin. J Cell Sci 115:3957–3966
Cary RB, Klymkowsky MW, Evans RM, Domingo A, Dent JA, Backhus LE (1994) Vimentin’s tail interacts with actin-containing structures in vivo. J Cell Sci 107(Pt 6):1609–1622
Kanlaya R, Pattanakitsakul SN, Sinchaikul S, Chen ST, Thongboonkerd V (2010) Vimentin interacts with heterogeneous nuclear ribonucleoproteins and dengue nonstructural protein 1 and is important for viral replication and release. Mol Biosyst 6:795–806
Russell RL, Cao D, Zhang D, Handschumacher RE, Pizzorno G (2001) Uridine phosphorylase association with vimentin. Intracellular distribution and localization. J Biol Chem 276:13302–13307
Gao Y, Sztul E (2001) A novel interaction of the Golgi complex with the vimentin intermediate filament cytoskeleton. J Cell Biol 152:877–894
Perlson E, Michaelevski I, Kowalsman N, Ben-Yaakov K, Shaked M, Seger R, Eisenstein M et al (2006) Vimentin binding to phosphorylated Erk sterically hinders enzymatic dephosphorylation of the kinase. J Mol Biol 364:938–944
Zhu QS, Rosenblatt K, Huang KL, Lahat G, Brobey R, Bolshakov S, Nguyen T et al (2011) Vimentin is a novel AKT1 target mediating motility and invasion. Oncogene 30:457–470
Tzivion G, Luo ZJ, Avruch J (2000) Calyculin A-induced vimentin phosphorylation sequesters 14-3-3 and displaces other 14-3-3 partners in vivo. J Biol Chem 275:29772–29778
Lian N, Wang W, Li L, Elefteriou F, Yang X (2009) Vimentin inhibits ATF4-mediated osteocalcin transcription and osteoblast differentiation. J Biol Chem 284:30518–30525
Vuoriluoto K, Haugen H, Kiviluoto S, Mpindi JP, Nevo J, Gjerdrum C, Tiron C et al (2011) Vimentin regulates EMT induction by Slug and oncogenic H-Ras and migration by governing Axl expression in breast cancer. Oncogene 30(12):1436–1448
Barberis L, Pasquali C, Bertschy-Meier D, Cuccurullo A, Costa C, Ambrogio C, Vilbois F et al (2009) Leukocyte transmigration is modulated by chemokine-mediated PI3Kgamma-dependent phosphorylation of vimentin. Eur J Immunol 39:1136–1146
Zhao Y, Yan Q, Long X, Chen X, Wang Y (2008) Vimentin affects the mobility and invasiveness of prostate cancer cells. Cell Biochem Funct 26:571–577
Lang SH, Hyde C, Reid IN, Hitchcock IS, Hart CA, Bryden AA, Villette JM et al (2002) Enhanced expression of vimentin in motile prostate cell lines and in poorly differentiated and metastatic prostate carcinoma. Prostate 52:253–263
Singh S, Sadacharan S, Su S, Belldegrun A, Persad S, Singh G (2003) Overexpression of vimentin: role in the invasive phenotype in an androgen-independent model of prostate cancer. Cancer Res 63:2306–2311
Zhang X, Fournier MV, Ware JL, Bissell MJ, Yacoub A, Zehner ZE (2009) Inhibition of vimentin or beta1 integrin reverts morphology of prostate tumor cells grown in laminin-rich extracellular matrix gels and reduces tumor growth in vivo. Mol Cancer Ther 8:499–508
Wei J, Xu G, Wu M, Zhang Y, Li Q, Liu P, Zhu T et al (2008) Overexpression of vimentin contributes to prostate cancer invasion and metastasis via src regulation. Anticancer Res 28:327–334
Hafeez BB, Zhong W, Weichert J, Dreckschmidt NE, Jamal MS, Verma AK (2011) Genetic ablation of PKC epsilon inhibits prostate cancer development and metastasis in transgenic mouse model of prostate adenocarcinoma. Cancer Res 71:2318–2327
Wu M, Bai X, Xu G, Wei J, Zhu T, Zhang Y, Li Q et al (2007) Proteome analysis of human androgen-independent prostate cancer cell lines: variable metastatic potentials correlated with vimentin expression. Proteomics 7:1973–1983
Sethi S, Macoska J, Chen W, Sarkar FH (2010) Molecular signature of epithelial–mesenchymal transition (EMT) in human prostate cancer bone metastasis. Am J Transl Res 3:90–99
Fuyuhiro Y, Yashiro M, Noda S, Kashiwagi S, Matsuoka J, Doi Y, Kato Y et al (2010) Clinical significance of vimentin-positive gastric cancer cells. Anticancer Res 30:5239–5243
Takemura K, Hirayama R, Hirokawa K, Inagaki M, Tsujimura K, Esaki Y, Mishima Y (1994) Expression of vimentin in gastric cancer: a possible indicator for prognosis. Pathobiology 62:149–154
Jin H, Morohashi S, Sato F, Kudo Y, Akasaka H, Tsutsumi S, Ogasawara H et al (2010) Vimentin expression of esophageal squamous cell carcinoma and its aggressive potential for lymph node metastasis. Biomed Res 31:105–112
Hu L, Lau SH, Tzang CH, Wen JM, Wang W, Xie D, Huang M et al (2004) Association of Vimentin overexpression and hepatocellular carcinoma metastasis. Oncogene 23:298–302
Li ZM, Wen YJ, Yang HB, Qin G, Tian L, Deng HX, Wen B (2008) Enhanced expression of human vimentin intermediate filaments in hepatocellular carcinoma cells decreases their proliferative and invasive abilities in vitro. Zhonghua Zhong Liu Za Zhi 30:408–412
Zou H, Harrington J, Rego RL, Ahlquist DA (2007) A novel method to capture methylated human DNA from stool: implications for colorectal cancer screening. Clin Chem 53:1646–1651
Chen WD, Han ZJ, Skoletsky J, Olson J, Sah J, Myeroff L, Platzer P et al (2005) Detection in fecal DNA of colon cancer-specific methylation of the nonexpressed vimentin gene. J Natl Cancer Inst 97:1124–1132
von Bassewitz DB, Roessner A, Grundmann E (1982) Intermediate-sized filaments in cells of normal human colon mucosa, adenomas and carcinomas. Pathol Res Pract 175:238–255
Ngan CY, Yamamoto H, Seshimo I, Tsujino T, Man-i M, Ikeda JI, Konishi K et al (2007) Quantitative evaluation of vimentin expression in tumour stroma of colorectal cancer. Br J Cancer 96:986–992
McInroy L, Maatta A (2007) Down-regulation of vimentin expression inhibits carcinoma cell migration and adhesion. Biochem Biophys Res Commun 360:109–114
Alfonso P, Nunez A, Madoz-Gurpide J, Lombardia L, Sanchez L, Casal JI (2005) Proteomic expression analysis of colorectal cancer by two-dimensional differential gel electrophoresis. Proteomics 5:2602–2611
Di Bella A, Regoli M, Nicoletti C, Ermini L, Fonzi L, Bertelli E (2009) An appraisal of intermediate filament expression in adult and developing pancreas: vimentin is expressed in alpha cells of rat and mouse embryos. J Histochem Cytochem 57:577–586
Hong SH, Misek DE, Wang H, Puravs E, Hinderer R, Giordano TJ, Greenson JK et al (2006) Identification of a specific vimentin isoform that induces an antibody response in pancreatic cancer. Biomark Insights 1:175–183
Liu C, Chen Y, Yu X, Jin C, Xu J, Long J, Ni Q et al (2008) Proteomic analysis of differential proteins in pancreatic carcinomas: effects of MBD1 knock-down by stable RNA interference. BMC Cancer 8:121
Yin T, Wang C, Liu T, Zhao G, Zhou F (2006) Implication of EMT induced by TGF-beta1 in pancreatic cancer. J Huazhong Univ Sci Technolog Med Sci 26:700–702
Walsh N, O’Donovan N, Kennedy S, Henry M, Meleady P, Clynes M, Dowling P (2009) Identification of pancreatic cancer invasion-related proteins by proteomic analysis. Proteome Sci 7:3
Korsching E, Packeisen J, Liedtke C, Hungermann D, Wulfing P, van Diest PJ, Brandt B et al (2005) The origin of vimentin expression in invasive breast cancer: epithelial–mesenchymal transition, myoepithelial histogenesis or histogenesis from progenitor cells with bilinear differentiation potential? J Pathol 206:451–457
Gilles C, Polette M, Zahm JM, Tournier JM, Volders L, Foidart JM, Birembaut P (1999) Vimentin contributes to human mammary epithelial cell migration. J Cell Sci 112(Pt 24):4615–4625
Domagala W, Lasota J, Bartkowiak J, Weber K, Osborn M (1990) Vimentin is preferentially expressed in human breast carcinomas with low estrogen receptor and high Ki-67 growth fraction. Am J Pathol 136:219–227
Kokkinos MI, Wafai R, Wong MK, Newgreen DF, Thompson EW, Waltham M (2007) Vimentin and epithelial-mesenchymal transition in human breast cancer—observations in vitro and in vivo. Cells Tissues Organs 185:191–203
Li M, Zhang B, Sun B, Wang X, Ban X, Sun T, Liu Z et al (2010) A novel function for vimentin: the potential biomarker for predicting melanoma hematogenous metastasis. J Exp Clin Cancer Res 29:109
Chu YW, Seftor EA, Romer LH, Hendrix MJ (1996) Experimental coexpression of vimentin and keratin intermediate filaments in human melanoma cells augments motility. Am J Pathol 148:63–69
Hendrix MJ, Seftor EA, Chu YW, Seftor RE, Nagle RB, McDaniel KM, Leong SP et al (1992) Coexpression of vimentin and keratins by human melanoma tumor cells: correlation with invasive and metastatic potential. J Natl Cancer Inst 84:165–174
Ben-Ze’ev A, Raz A (1985) Relationship between the organization and synthesis of vimentin and the metastatic capability of B16 melanoma cells. Cancer Res 45:2632–2641
Caselitz J, Janner M, Breitbart E, Weber K, Osborn M (1983) Malignant melanomas contain only the vimentin type of intermediate filaments. Virchows Arch A Pathol Anat Histopathol 400:43–51
Yamada T, Kawamata T, Walker DG, McGeer PL (1992) Vimentin immunoreactivity in normal and pathological human brain tissue. Acta Neuropathol 84:157–162
Trog D, Yeghiazaryan K, Schild HH, Golubnitschaja O (2008) Up-regulation of vimentin expression in low-density malignant glioma cells as immediate and late effects under irradiation and temozolomide treatment. Amino Acids 34:539–545
Fortin S, Le Mercier M, Camby I, Spiegl-Kreinecker S, Berger W, Lefranc F, Kiss R (2010) Galectin-1 is implicated in the protein kinase C epsilon/vimentin-controlled trafficking of integrin-beta1 in glioblastoma cells. Brain Pathol 20:39–49
Bouamrani A, Ramus C, Gay E, Pelletier L, Cubizolles M, Brugiere S, Wion D et al (2010) Increased phosphorylation of vimentin in noninfiltrative meningiomas. PLoS One 5:e9238
Kawahara E, Oda Y, Ooi A, Katsuda S, Nakanishi I, Umeda S (1988) Expression of glial fibrillary acidic protein (GFAP) in peripheral nerve sheath tumors. A comparative study of immunoreactivity of GFAP, vimentin, S-100 protein, and neurofilament in 38 schwannomas and 18 neurofibromas. Am J Surg Pathol 12:115–120
Broers JL, de Leij L, Rot MK, ter Haar A, Lane EB, Leigh IM, Wagenaar SS et al (1989) Expression of intermediate filament proteins in fetal and adult human lung tissues. Differentiation 40:119–128
Upton MP, Hirohashi S, Tome Y, Miyazawa N, Suemasu K, Shimosato Y (1986) Expression of vimentin in surgically resected adenocarcinomas and large cell carcinomas of lung. Am J Surg Pathol 10:560–567
Al-Saad S, Al-Shibli K, Donnem T, Persson M, Bremnes RM, Busund LT (2008) The prognostic impact of NF-kappaB p105, vimentin, E-cadherin and Par6 expression in epithelial and stromal compartment in non-small-cell lung cancer. Br J Cancer 99:1476–1483
Rho JH, Roehrl MH, Wang JY (2009) Glycoproteomic analysis of human lung adenocarcinomas using glycoarrays and tandem mass spectrometry: differential expression and glycosylation patterns of vimentin and fetuin A isoforms. Protein J 28:148–160
Chu S, Xu H, Ferro TJ, Rivera PX (2007) Poly(ADP-ribose) polymerase-1 regulates vimentin expression in lung cancer cells. Am J Physiol Lung Cell Mol Physiol 293:L1127–L1134
Gilles C, Polette M, Piette J, Delvigne AC, Thompson EW, Foidart JM, Birembaut P (1996) Vimentin expression in cervical carcinomas: association with invasive and migratory potential. J Pathol 180:175–180
Williams AA, Higgins JP, Zhao H, Ljunberg B, Brooks JD (2009) CD 9 and vimentin distinguish clear cell from chromophobe renal cell carcinoma. BMC Clin Pathol 9:9
Gustmann C, Altmannsberger M, Osborn M, Griesser H, Feller AC (1991) Cytokeratin expression and vimentin content in large cell anaplastic lymphomas and other non-Hodgkin’s lymphomas. Am J Pathol 138:1413–1422
Yamamoto Y, Izumi K, Otsuka H (1992) An immunohistochemical study of epithelial membrane antigen, cytokeratin, and vimentin in papillary thyroid carcinoma. Recognition of lethal and favorable prognostic types. Cancer 70:2326–2333
Coppola D, Fu L, Nicosia SV, Kounelis S, Jones M (1998) Prognostic significance of p53, bcl-2, vimentin, and S100 protein-positive Langerhans cells in endometrial carcinoma. Hum Pathol 29:455–462
Bargagna-Mohan P, Hamza A, Kim YE, Khuan Abby Ho Y, Mor-Vaknin N, Wendschlag N, Liu J et al (2007) The tumor inhibitor and antiangiogenic agent withaferin A targets the intermediate filament protein vimentin. Chem Biol 14:623–634
Lahat G, Zhu QS, Huang KL, Wang S, Bolshakov S, Liu J, Torres K et al (2010) Vimentin is a novel anti-cancer therapeutic target; insights from in vitro and in vivo mice xenograft studies. PLoS One 5:e10105
Wu KJ, Zeng J, Zhu GD, Zhang LL, Zhang D, Li L, Fan JH et al (2009) Silibinin inhibits prostate cancer invasion, motility and migration by suppressing vimentin and MMP-2 expression. Acta Pharmacol Sin 30:1162–1168
Singh RP, Raina K, Sharma G, Agarwal R (2008) Silibinin inhibits established prostate tumor growth, progression, invasion, and metastasis and suppresses tumor angiogenesis and epithelial-mesenchymal transition in transgenic adenocarcinoma of the mouse prostate model mice. Clin Cancer Res 14:7773–7780
Dong TT, Zhou HM, Wang LL, Feng B, Lv B, Zheng MH (2011) Salinomycin selectively targets ‘CD133+’ cell subpopulations and decreases malignant traits in colorectal cancer lines. Ann Surg Oncol 18(6):1797–1804
Zhang X, Ladd A, Dragoescu E, Budd WT, Ware JL, Zehner ZE (2009) MicroRNA-17-3p is a prostate tumor suppressor in vitro and in vivo, and is decreased in high grade prostate tumors analyzed by laser capture microdissection. Clin Exp Metastasis 26:965–979
Braun J, Hoang-Vu C, Dralle H, Huttelmaier S (2010) Downregulation of microRNAs directs the EMT and invasive potential of anaplastic thyroid carcinomas. Oncogene 29:4237–4244
Bouchard PR, Hutabarat RM, Thompson KM (2010) Discovery and development of therapeutic aptamers. Annu Rev Pharmacol Toxicol 50:237–257
Acknowledgments
We apologize to the authors of many other relevant studies that are not cited because of space limitations. Work in the authors’ laboratory was supported by Grants from the National Institutes of Health to Dr. Shulin Li (NIH RO1CA120895).
Conflict of interest
We declare that none of the authors has a financial interest related to this work.
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Satelli, A., Li, S. Vimentin in cancer and its potential as a molecular target for cancer therapy. Cell. Mol. Life Sci. 68, 3033–3046 (2011). https://doi.org/10.1007/s00018-011-0735-1
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DOI: https://doi.org/10.1007/s00018-011-0735-1