Proteome analysis of human androgen‐independent prostate cancer cell lines: Variable metastatic potentials correlated with vimentin expression

Wu, Mingfu; Bai, Xiaojing; Xu, Gang; Wei, Juncheng; Zhu, Tao; Zhang, Yongtao; Li, Qiong; Liu, Ping; Song, Anping; Zhao, Liangpin; Chen, Gang; Han, Zhiqiang; Wang, Shixuan; Zhou, Jianfeng; Lu, Ye; Ma, Dong

doi:10.1002/pmic.200600643

Cited by 55 publications

(38 citation statements)

References 39 publications

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“…They found that calreticulin precursor was upregulated in highly metastatic cells. 15 In this study, calreticulin precursor was found upregulated in PDGA. These phenomena suggest that calreticulin precursor is closely related to malignant phenotype of cancer.…”

Section: Discussionmentioning

confidence: 85%

Identification of Differentiation-Related Proteins in Gastric Adenocarcinoma Tissues by Proteomics

Zhou

Yao

Zhang

et al. 2016

Technol Cancer Res Treat

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There is a significant correlation between the degree of tumor differentiation and the survival of patients with gastric cancers. In this report, we compared proteomic differences between poorly differentiated gastric adenocarcinoma tissues and welldifferentiated gastric adenocarcinoma tissues in order to identify differentiation-related proteins that may be closely correlated with differentiation of gastric cancer pathogenesis. We identified 7 proteins, of which calreticulin precursor, tapasinERP57 heterodimer, pyruvate kinase isozymes M1/M2 isoform M2, class Pi glutathione S-transferase, and chain A crystal structure of human enolase 1 were upregulated in poorly differentiated gastric adenocarcinoma compared with well-differentiated gastric adenocarcinoma, while myosin-11 isoform SM2A and actin alpha cardiac were downregulated. Two of them, pyruvate kinase isozymes M1/M2 isoform M2 and enolase 1 are enzymes involved in glycolytic pathway. The upregulation of pyruvate kinase isozymes M1/M2 isoform M2 and enolase 1 in poorly differentiated gastric adenocarcinoma was confirmed by Western blotting and immunohistochemistry. Furthermore, we observed 107 cases with gastric adenocarcinoma and found that the high expression of pyruvate kinase isozymes M1/M2 isoform M2 and enolase 1 correlates with tumor size (P ¼ .0001 and P ¼ .0017, respectively), depth of invasion (P ¼ .0024 and P ¼ .0261, respectively), and poor prognosis of patients. In conclusion, with this proteomic analysis, pyruvate kinase isozymes M1/M2 isoform M2 and enolase 1 were identified upregulated in poorly differentiated gastric adenocarcinoma comparing with well-differentiated gastric adenocarcinoma. The expression level of pyruvate kinase isozymes M1/M2 isoform M2 and enolase 1 was significantly correlated with overall survival. Some of them would be differentiation-related cancer biomarkers and are associated with tumor metastasis, invasion, and prognosis.

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Section: Discussionmentioning

confidence: 85%

Identification of Differentiation-Related Proteins in Gastric Adenocarcinoma Tissues by Proteomics

Zhou

Yao

Zhang

et al. 2016

Technol Cancer Res Treat

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“…Ablation of vimentin expression inhibits migration and invasion of colon and breast cancer cell lines (McInroy and Maatta, 2007) and promotes conversion of tumourigenic prostate epithelial cells into slow growing, less aggressive cells (Liu et al, 2003b). Upregulation of vimentin has been reported in prostate cancer, lung cancer and carcinosarcoma and vimentin have been used as a marker for lung cancer detection (Liu et al, 2004;Wu et al, 2007;Pardo et al, 2008;Wei et al, 2008). In colorectal tumours, increased vimentin expression correlates with the presence of oncogenic KRAS and with nuclear beta-catenin.…”

Section: Cytoskeletal Proteinsmentioning

confidence: 99%

Differential tissue-specific protein markers of vaginal carcinoma

et al. 2009

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The objective was to identify proteins differentially expressed in vaginal cancer to elucidate relevant cancer-related proteins. A total of 16 fresh-frozen tissue biopsies, consisting of 5 biopsies from normal vaginal epithelium, 6 from primary vaginal carcinomas and 5 from primary cervical carcinomas, were analysed using two-dimensional gel electrophoresis (2-DE) and MALDI-TOF mass spectrometry. Of the 43 proteins identified with significant alterations in protein expression between non-tumourous and tumourous tissue, 26 were upregulated and 17 were downregulated. Some were similarly altered in vaginal and cervical carcinoma, including cytoskeletal proteins, tumour suppressor proteins, oncoproteins implicated in apoptosis and proteins in the ubiquitin -proteasome pathway. Three proteins were uniquely altered in vaginal carcinoma (DDX48, erbB3-binding protein and biliverdin reductase) and five in cervical carcinoma (peroxiredoxin 2, annexin A2, sarcomeric tropomyosin kappa, human ribonuclease inhibitor and prolyl-4-hydrolase beta). The identified proteins imply involvement of multiple different cellular pathways in the carcinogenesis of vaginal carcinoma. Similar protein alterations were found between vaginal and cervical carcinoma suggesting common tumourigenesis. However, the expression level of some of these proteins markedly differs among the three tissue specimens indicating that they might be useful molecular markers.

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“…3,4 A classical EMT protein is vimentin; numerous reports show that vimentin is overexpressed in invasive human tumors but is nearly undetectable in non-invasive, stationary tumors. 3,[5][6][7] Vimentin is a Type III intermediate filament 8 and its overexpression correlates with metastatic disease, EMT induction, poor prognosis and reduced patient survival. 7,[9][10][11] Similar correlations between vimentin overexpression and invasion are observed in cancer cell lines and mouse models across most tumor types.…”

mentioning

confidence: 99%

“…3,[5][6][7] Vimentin is a Type III intermediate filament 8 and its overexpression correlates with metastatic disease, EMT induction, poor prognosis and reduced patient survival. 7,[9][10][11] Similar correlations between vimentin overexpression and invasion are observed in cancer cell lines and mouse models across most tumor types. 6,12 In breast cancer, in particular, vimentin positive tumors were observed in younger women, usually lacked estrogen and progesterone receptors, and correlated with high-grade cancer 13 and tumor size.…”

mentioning

confidence: 99%

Withaferin A inhibits breast cancer invasion and metastasis at sub‐cytotoxic doses by inducing vimentin disassembly and serine 56 phosphorylation

Thaiparambil

Bender

Ganesh

et al. 2011

Intl Journal of Cancer

238

208

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Withaferin A (WFA) is purified from the plant Withania somnifera and inhibits the vimentin cytoskeleton. Vimentin overexpression in cancer correlates with metastatic disease, induction of epithelial to mesenchymal transition and reduced patient survival. As vimentin functions in cell motility, we wanted to test the hypothesis that WFA inhibits cancer metastasis by disrupting vimentin function. These data showed that WFA had weak cytotoxic and apoptotic activity at concentrations less than or equal to 500 nM, but retained potent anti-invasive activity at these low doses. Imaging of breast cancer cell lines revealed that WFA induces perinuclear vimentin accumulation followed by rapid vimentin depolymerization. A concomitant induction of vimentin ser56 phosphorylation was observed, which is consistent with vimentin disassembly. Structure activity relationships were established using a set of chemically modified WFA analogs and showed that the predicted vimentin-binding region of WFA is necessary to induce vimentin ser56 phosphorylation and for its anti-invasive activity. Pharmacokinetic studies in mice revealed that WFA reaches peak concentrations up to 2 lM in plasma with a half-life of 1.36 hr following a single 4 mg/kg dose. In a breast cancer metastasis mouse model, WFA showed dose-dependent inhibition of metastatic lung nodules and induced vimentin ser56 phosphorylation, with minimal toxicity to lung tissue. Based upon these studies, we conclude that WFA is a potent breast cancer anti-metastatic agent and the anti-metastatic activity of WFA is, at least in part, mediated through its effects on vimentin and vimentin ser56 phosphorylation.Metastatic disease is the major cause of death in almost all cancer types; however, most treatments are developed to target the primary tumor and not the metastases. This is due to metastatic cells being difficult to detect, highly aggressive, chemoresistant and experimentally challenging to model. 1 At present, there is no agent in clinical use that effectively prevents metastasis and most patients ultimately succumb to metastatic disease.The metastatic process can be broadly categorized into three stages-tumor cell invasion into surrounding tissue, intravasation into blood or lymphatic vessels and extravasation into a new host environment. These events are triggered by genetic and epigenetic alterations that transform stationary epithelial cells into migratory cells, a process termed epithelialmesenchymal transition (EMT). 2,3 Recent data suggests that cancer cells can re-trigger EMT to migrate into surrounding tissue. 3,4 A classical EMT protein is vimentin; numerous reports show that vimentin is overexpressed in invasive human tumors but is nearly undetectable in non-invasive, stationary tumors. 3,[5][6][7] Vimentin is a Type III intermediate filament 8 and its overexpression correlates with metastatic disease, EMT induction, poor prognosis and reduced patient survival. 7,[9][10][11] Similar correlations between vimentin overexpression and invasion are observed in cancer ce...

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Proteome analysis of human androgen‐independent prostate cancer cell lines: Variable metastatic potentials correlated with vimentin expression

Cited by 55 publications

References 39 publications

Identification of Differentiation-Related Proteins in Gastric Adenocarcinoma Tissues by Proteomics

Identification of Differentiation-Related Proteins in Gastric Adenocarcinoma Tissues by Proteomics

Differential tissue-specific protein markers of vaginal carcinoma

Withaferin A inhibits breast cancer invasion and metastasis at sub‐cytotoxic doses by inducing vimentin disassembly and serine 56 phosphorylation

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