Expression of S100 proteins in normal human tissues and common cancers using tissue microarrays: S100A6, S100A8, S100A9 and S100A11 are all overexpressed in common cancers

Cross, Simon S.; Hamdy, Freddie C.; Deloulme, Jean-Christophe; Rehman, Ishtiaq

doi:10.1111/j.1365-2559.2005.02097.x

Cited by 231 publications

(185 citation statements)

References 37 publications

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“…In an immunohistochemical survey of S100 protein expression in 28 tissue types and 21 tumor types, Cross et al found expression of S100A6 and S100A8 in 12% and 29% of breast cancers. 37 Our findings are consistent with those of Carlsson et al who found downregulation of S100A6 regardless of pathological stage and up-regulation of S100A8 in breast cancer using serial analysis of gene expression (SAGE). 38 Kennedy et al have shown that BRCA1 is capable of repressing several of the members of the S100A family including S100A8 and that functional BRCA1 is required for this repression.…”

Section: Protein Identificationsupporting

confidence: 93%

Differentiating Proteomic Biomarkers in Breast Cancer by Laser Capture Microdissection and MALDI MS

Sanders

Dias

et al. 2008

J. Proteome Res.

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We assessed proteomic patterns in breast cancer using MALDI MS and laser capture microdissected cells. Protein and peptide expression in invasive mammary carcinoma versus normal mammary epithelium and estrogen-receptor positive versus estrogen-receptor negative tumors were compared. Biomarker candidates were identified by statistical analysis and classifiers were developed and validated in blinded test sets. Several of the m/z features used in the classifiers were identified by LC-MS/MS and two were confirmed by immunohistochemistry. (2) reproducibility analyses, (3) interinstitutional sample variability, (4) variability of samples with age, (5) complete list of features defined for the IMC vs NME comparison, (6) subset of features used for the IMC vs NME classifier, (7) IMC vs NME classification LOOCV error depending on selection of k-value for the KNN algorithm, (8) complete list of features defined for the ER+ vs ER− comparison, (9) subset of features used for the ER+ vs ER− classifier, (10) ER+ vs ER− classification LOOCV error depending on selection of k-value for the KNN algorithm, (11) detailed protein identification data. This material is available free of charge via the Internet at Keywords

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Section: Protein Identificationsupporting

confidence: 93%

Differentiating Proteomic Biomarkers in Breast Cancer by Laser Capture Microdissection and MALDI MS

Sanders

Dias

et al. 2008

J. Proteome Res.

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“…Although S100A6 overexpression in pancreatic and other cancers, including gastric (Yang et al, 2007), thyroid (Brown et al, 2006), breast (Cross et al, 2005) and colorectal (Komatsu et al, 2000) has been documented, its precise role in cancer is not known. In pancreatic cancer, the expression of S100A6 appears to correlate with aggressive disease in that high levels of tumour S100A6 are associated with poorer outcome (Vimalachandran et al, 2005), whereas pancreatic cancer cells depleted of S100A6 are less invasive (Ohuchida et al, 2005).…”

Section: Discussionmentioning

confidence: 99%

S100A6 binds to annexin 2 in pancreatic cancer cells and promotes pancreatic cancer cell motility

et al. 2009

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BACKGROUND: High levels of S100A6 have been associated with poor outcome in pancreatic cancer patients. The functional role of S100A6 is, however, poorly understood. METHODS: Immunoprecipitation followed by two-dimensional gel electrophoresis and mass spectrometry were undertaken to identify S100A6 interacting proteins in pancreatic cancer cells. Immunohistochemistry and coimmunofluorescence were performed to examine expression or colocalisation of proteins. siRNA was used to deplete specific proteins and effects on motility were measured using Boyden Chamber and wound healing assays. RESULTS: Our proteomic screen to identify S100A6 interacting proteins revealed annexin 11, annexin 2, tropomyosin b and a candidate novel interactor lamin B1. Of these, annexin 2 was considered particularly interesting, as, like S100A6, it is expressed early in the development of pancreatic cancer and overexpression occurs with high frequency in invasive cancer. Reciprocal immunoprecipitation confirmed the interaction between annexin 2 and S100A6 and the proteins colocalised, particularly in the plasma membrane of cultured pancreatic cancer cells and primary pancreatic tumour tissue. Analysis of primary pancreatic cancer specimens (n ¼ 55) revealed a strong association between high levels of cytoplasmic S100A6 and the presence of annexin 2 in the plasma membrane of cancer cells (P ¼ 0.009). Depletion of S100A6 was accompanied by diminished levels of membrane annexin 2 and caused a pronounced reduction in the motility of pancreatic cancer cells. CONCLUSION: These findings point towards a functional role for S100A6 that may help explain the link between S100A6 expression in pancreatic cancer and aggressive disease.

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“…[5][6][7][8][9][10] Subsequent studies showed that S100A6 may also be involved in the regulation of cancer progression. 11 The deregulation of S100A6 expression during malignant transformation has thus far been described in human pancreatic cancer, malignant thyroid neoplasms, malignant melanoma, breast cancer, hepatocellular carcinoma, lung cancer, prostate cancer, and colorectal carcinoma.…”

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confidence: 99%

S100A6 Overexpression Is Associated with Poor Prognosis and Is Epigenetically Up-Regulated in Gastric Cancer

Wang

Zhang

Zhong

et al. 2010

The American Journal of Pathology

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S100A6 has been implicated in a variety of biological functions as well as tumorigenesis. In this study, we investigated the expression status of S100A6 in relation to the clinicopathological features and prognosis of patients with gastric cancer and further explored a possible association of its expression with epigenetic regulation. S100A6 expression was remarkably increased in 67.5% of gastric cancer tissues as compared with matched noncancerous tissues. Statistical analysis demonstrated a clear correlation between high S100A6 expression and various clinicopathological features, such as depth of wall invasion, positive lymph node involvement, liver metastasis, vascular invasion, and tumor-node metastasis stage (P < 0.05 in all cases), as well as revealed that S100A6 is an independent prognostic predictor (P ‫؍‬ 0.026) significantly related to poor prognosis (P ‫؍‬ 0.0004). Further exploration found an inverse relationship between S100A6 expression and the methylation status of the seventh and eighth CpG sites in the promoter/first exon and the second to fifth sites in the second exon/second intron. In addition, the level of histone H3 acetylation was found to be significantly higher in S100A6-expressing cancer cells. After 5-azacytidine or trichostatin A treatment, S100A6 expression was clearly increased in S100A6 low-expressing cells. In conclusion, our results suggested that S100A6 plays an important role in the progression of gastric cancer, affecting patient prognosis, and is up-regulated by epigenetic regulation. (Am J

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Expression of S100 proteins in normal human tissues and common cancers using tissue microarrays: S100A6, S100A8, S100A9 and S100A11 are all overexpressed in common cancers

Abstract: S100A6, S100A8, S100A9 and S100A11 are all expressed in common cancers, especially breast cancer. In addition, S100A11 undergoes a nucleocytoplasmic translocation which may have a direct influence on the proliferation of the cancer cells.

Cited by 231 publications

References 37 publications

Differentiating Proteomic Biomarkers in Breast Cancer by Laser Capture Microdissection and MALDI MS

Differentiating Proteomic Biomarkers in Breast Cancer by Laser Capture Microdissection and MALDI MS

S100A6 binds to annexin 2 in pancreatic cancer cells and promotes pancreatic cancer cell motility

S100A6 Overexpression Is Associated with Poor Prognosis and Is Epigenetically Up-Regulated in Gastric Cancer

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