Differential molecular profiling between skin carcinomas reveals four newly reported genes potentially implicated in squamous cell carcinoma development

Marionnet, Claire; Lalou, Claude; Mollier, Karine; Chazal, Marjorie; Delestaing, G.; Compan, Delphine; Vérola, O; Vilmer, C; Cuminet, J; Dubertret, Louis; Basset-Séguin, Nicole

doi:10.1038/sj.onc.1206571

Cited by 41 publications

(45 citation statements)

References 19 publications

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“…Increasing evidence from several laboratories suggests that RhoC expression is associated with particularly aggressive, metastatic cancers; however, this has never been reported for CaP (Moscow et al, 1994;del Peso et al, 1997;Fritz et al, 1999;Imamura et al, 1999;Clark et al, 2000;Sahai and Marshall, 2002;Carr et al, 2003;Horiuchi et al, 2003;Kamai et al, 2003;Marionnet et al, 2003;Shinto et al, 2003;Wang et al, 2003;Kondo et al, 2004). We hypothesized that RhoC may be involved in CaP metastasis.…”

Section: Rho Gtpase Expression In Cap Cellsmentioning

confidence: 92%

“…Although these studies demonstrate a role for these GTPases in CaP cell cytoskeletal reorganization, they have not fully made the connection with motility, invasion or metastasis. Further, it is becoming increasingly evident that the vast majority of human tumors overexpress RhoA, but overexpression of RhoC is limited to particularly aggressive and metastatic forms of cancer (Moscow et al, 1994;del Peso et al, 1997;Fritz et al, 1999;Imamura et al, 1999;Clark et al, 2000;Sahai and Marshall, 2002;Carr et al, 2003;Horiuchi et al, 2003;Kamai et al, 2003;Marionnet et al, 2003;Shinto et al, 2003;Wang et al, 2003;Kondo et al, 2004) The PC-3 cells, derived from a bone metastasis, were the only CaP cell line to express active RhoC protein.…”

Section: )mentioning

confidence: 99%

“…RhoC GTPase is a Rho protein implicated in the progression and metastasis of several cancers, including breast, ovarian, pancreas, gastric cancer, hepatocellular carcinoma, bladder, colorectal and cutaneous melanoma (Moscow et al, 1994;del Peso et al, 1997;Suwa et al, 1998;Fritz et al, 1999;van Golen et al, 1999van Golen et al, , 2000Imamura et al, 1999;Clark et al, 2000;Sahai and Marshall 2002;Carr et al, 2003;Horiuchi et al, 2003;Kamai et al, 2003;Marionnet et al, 2003;Shinto et al, 2003;Wang et al, 2003;Kondo et al, 2004). Our laboratory has demonstrated that ectopic expression of wild-type RhoC in immortalized human mammary epithelial cells leads to a metastatic phenotype (van Golen et al, 2000a, b).…”

Section: Introductionmentioning

confidence: 99%

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RhoC GTPase is required for PC-3 prostate cancer cell invasion but not motility

et al. 2005

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Section: Rho Gtpase Expression In Cap Cellsmentioning

confidence: 92%

Section: )mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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RhoC GTPase is required for PC-3 prostate cancer cell invasion but not motility

et al. 2005

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“…It is noteworthy that EMMPRIN belonged to 4 genes specifically up-regulated in SCCs as compared to BCCs of the skin. 30 The authors demonstrated that the increase in EMMPRIN expression was due to an enhanced transcription rather than to a gene dosage effect. 30 In line with these observations, we found that SCCs of the oral cavity also expressed high levels of EMMPRIN in more than 90% of cases.…”

Section: Discussionmentioning

confidence: 99%

High incidence of EMMPRIN expression in human tumors

Riethdorf

Reimers

Assmann

et al. 2006

Intl Journal of Cancer

206

172

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Extracellular matrix metalloproteinase inducer expressed by tumor cells stimulates peritumoral fibroblasts to produce matrix metalloproteinases, thus contributing to tumor invasion and metastasis. To assess its suitability as potential therapeutic target, the overall incidence of EMMPRIN expression in normal and neoplastic tissues was analyzed. EMMPRIN expression was detected immunohistochemically using monoclonal antibodies MEM-M6/1 and HIM6 and tissue microarrays with 2,348 and 608 tissue samples from 129 distinct tumor types and 76 different normal tissues, respectively. Expression and glycosylation state of EMMPRIN in human breast cancer cells were analyzed by Western blot analysis with monoclonal antibodies recognizing distinct carbohydrate structures and biochemical methods. EMMPRIN expression was found in 112 of 129 tumor entities analyzed with malignant tumors being EMMPRIN positive more frequently than benign tumors. A remarkable heterogeneity in EMMPRIN expression between tumor entities was observed. Among others, squamous-cell carcinomas (60-100%), pancreatic (87%), chromophobic kidney (83%), hepatocellular (83%) or medullary breast (83%) adenocarcinomas as well as glioblastoma multiforme (79%) presented with a particular high incidence of EMMPRIN expression. There were a limited number of EMMPRIN-positive normal cell types including proliferatively active and differentiating epithelial cells, germ cells, myocardial cells in the left heart ventricle or vascular endothelial cells of the brain. We could further demonstrate that breast cancer cells expressed EMMPRIN isoforms differing in the presence or absence of Lewis X glycan structures. Our results may assist in defining the suitability of EMMPRIN as therapeutic target and predicting negative side effects. ' 2006 Wiley-Liss, Inc.Key words: extracellular matrix metalloproteinase inducer expression; human normal tissues; human tumors; glycosylation Tumor cell invasion and metastasis requires degradation of extracellular matrix components, which is mainly achieved by various proteolytic enzymes including zinc-dependent matrix metalloproteinases (MMPs). Analysis of MMP expression patterns in tumor specimens revealed that the majority of these enzymes are produced by stromal cells surrounding the tumor rather than by tumor cells themselves. An increasing body of evidence, however, suggests that MMP synthesis is stimulated by tumor cells in a paracrine fashion. This stimulation is at least partially attributed to extracellular matrix metalloproteinase inducer (EMMPRIN, also designated CD147 or basigin), a 58 kDa surface glycoprotein of the immunoglobulin superfamily, originally purified from the plasma membrane of cancer cells. 1 EMMPRIN has been demonstrated to stimulate production of MMP-1, -2, -3, -9, -14, -15 in fibroblasts surrounding tumor cells. 2 As shown by Sun and Hemler, 3 EMMPRIN also appears to participate in the induction of MMP production in tumor cells in an autocrine fashion. Accordingly, MDA-MB-436 human breast cancer cells recombinantly...

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“…Cdc42 is overexpressed in some breast cancers and there is accumulating evidence that activated Cdc42 contributes to the accumulation of ErbB1 in cells through the regulation of c-Cbl function (Abraham, Kuriakose et al 2001;Marionnet, Lalou et al 2003). The view that Cdc42 is involved in human breast carcinogenesis is supported by a rodents model of breast carcinoma where the expression of a dominant negative mutant of Cdc42 reduced the number of focal contacts, inhibited colony formation in soft agar and affected cell growth in vivo (Fritz, Just et al 1999).…”

Section: Cdc42 Family In Breast Tumorsmentioning

confidence: 80%