Putative circulating markers of the early and advanced stages of breast cancer identified by high-resolution label-free proteomics

Panis, Carolina; Pizzatti, Luciana; Herrera, Ana Cristina; Cecchini, Rúbens; Abdelhay, Eliana

doi:10.1016/j.canlet.2012.11.020

Cited by 45 publications

(32 citation statements)

References 44 publications

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“…Furthermore, it was showed that gelsolin expression was reduced in human mammary lesions as the disease progressed; atypical ductal hyperplasia!ductal carcinoma in situ!invasive carcinoma (32)(33)(34). However, a previous report indicated that gelsolin levels were increased in the plasma of breast cancer patients (35), suggesting the role of gelsolin in carcinogenesis needs to be further investigated. In this study we showed that gelsolin was upregulated in plasma of the rats given high n-3:n-6 ratios.…”

Section: Discussionmentioning

confidence: 99%

Proteomic Changes Induced by Effective Chemopreventive Ratios of n-3:n-6 Fatty Acids and Tamoxifen against MNU-Induced Mammary Cancer in the Rat

Skibinski

Thompson

Das

et al. 2013

Cancer Prevention Research

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We used a proteomic approach to gain insights into the mechanisms of protection at the protein level by a high n-3:n-6 ratio in the absence and presence of Tamoxifen. Four groups were treated with 1-methyl-1-nitrosourea (MNU) and fed the following diets with varied n-3:n-6 ratios; group 1 ¼ 1:1; groups 2 and 3 ¼ 10:1 and 25:1, respectively; group 4: (25:1) plus Tamoxifen (1 mg/kg diet). The plasma from six rats/group was pooled and analyzed with the isobaric tags for relative and absolute quantitation method; 148 proteins were identified with 95% confidence by ProteinPilot 4.0. In plasma of rats fed 10:1, 25:1 n-3:n-6, and 25:1 plus Tamoxifen, the number of proteins that met our criteria (P 0.05, error factor 2) were 10, 14, and 19 proteins, respectively. Selected proteins were further validated by Western blotting. Compared to 1:1, both 10:1 and 25:1 diets upregulated vitamin D binding protein, gelsolin, and 14-3-3 sigma, reported to have tumor suppressive effects, whereas alpha-1B-glycoprotein, which has been reported to be elevated in the serum of breast cancer patients was decreased. Compared to 25:1, the 25:1 plus Tamoxifen diet downregulated apolipoprotein E, haptoglobin, and inter-a-inhibitor H4 heavy chain. Ingenuity pathway analysis determined that the trends of specific proteins were related to lipid metabolism in the 25:1 n-3:n-6 group, whereas the 25:1 n-3:n-6 plus Tamoxifen group included proteins involved in cancer and inflammation. Our results show that several proteins were altered in a manner consistent with chemoprevention. Such proteins may serve as biomarkers to monitor efficacy of n-3 and Tamoxifen in future clinical chemoprevention trials. Cancer Prev Res; 6(9); 979-88. Ó2013 AACR.

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Section: Discussionmentioning

confidence: 99%

Proteomic Changes Induced by Effective Chemopreventive Ratios of n-3:n-6 Fatty Acids and Tamoxifen against MNU-Induced Mammary Cancer in the Rat

Skibinski

Thompson

Das

et al. 2013

Cancer Prevention Research

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“…Such techniques provide further advantages for serum proteomics studies as high-sensitivity, real-time measurements, faster quantification and enhanced reproducibility [59]. In this context, studies employing the MS-label-free strategy have provided a new scenario of circulating proteins, not before described in cancer [29,30].…”

Section: Serum Proteomicsmentioning

confidence: 99%

“…The OxiCAT approach provides a reliable picture regarding the redox state of the cell and can be employed for analyzing both plasmatic and tissular changes in the thiol content. Enhanced oxidative stress occurs in several cancers [29,30] and is the major source of cysteine oxidation; therefore, the study of the redox proteomics constitutes a promising tool for cancer research in the future.…”

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confidence: 99%

Proteomic Tools for Cancer Research: Updating the Oncoproteomics

Panis

2013

J Proteomics Bioinform

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“…GRHL3 is highly expressed in the early stages of breast cancer, which was observed both in tumor and plasma samples, but its expression is greatly reduced in advanced stages of this disease. 35 In another study, GRHL3-positive breast cancer cases correlated with a favorable prognosis, while GRHL3-negative cases had a poor prognosis. In cases with lymph node invasion, GRHL3 also contributed to longer survival times.…”

Section: Grainyhead-like 3 (Grhl3)mentioning

confidence: 99%

“…Mammary gland ducts 17,19,20 Breast cancer [17][18][19][20][21] Colon and rectum 7 Colorectal cancer 23,24 Lining of the stomach 26 Gastric cancer 25,26 Oral epithelium 7 Oral squamous cell carcinoma 27 Liver ducts 45 Hepatocellular carcinoma 28 Renal epithelium 46 Clear cell renal cell carcinoma Skin cancer 32,33 Mammary gland ducts 37 Breast cancer [34][35][36] Lung airways 7 Lung cancer 37,38 Urinary bladder 44 ?…”

Section: Future Perspectivesmentioning

confidence: 99%

Recent discoveries concerning the involvement of transcription factors from the Grainyhead-like family in cancer

Mlacki

Kikulska

Krzywińska

et al. 2015

Exp Biol Med (Maywood)

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The Grainyhead-like (GRHL) family of transcription factors has three mammalian members, which are currently termed Grainyhead-like 1 (GRHL1), Grainyhead-like 2 (GRHL2), and Grainyhead-like 3 (GRHL3). These factors adopt a DNA-binding immunoglobulin fold homologous to the DNA-binding domain of key tumor suppressor p53. Their patterns of expression are tissue and developmentally specific. Earlier studies of the GRHL proteins focused on their functions in mammalian development. In recent years, these factors have been linked to many different types of cancer: squamous cell carcinoma of the skin, breast cancer, gastric cancer, hepatocellular carcinoma, colorectal cancer, clear cell renal cell carcinoma, neuroblastoma, prostate cancer, and cervical cancer. The roles of GRHL proteins in these various types of cancer are complex, and in some cases appear to be contradictory: they can serve to promote cancer development, or they may act as tumor suppressors, depending on the particular GRHL protein involved and on the cancer type. The reasons for obvious discrepancies in results from different studies remain unclear. At the molecular level, the GRHL transcription factors regulate the expression of genes whose products are involved in cellular proliferation, differentiation, adhesion, and polarity. We herein review the roles of GRHL proteins in cancer development, and we critically examine relevant molecular mechanisms, which were proposed by different authors. We also discuss the significance of recent discoveries implicating the involvement of GRHL transcription factors in cancer and highlight potential future applications of this knowledge in cancer treatment.

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Putative circulating markers of the early and advanced stages of breast cancer identified by high-resolution label-free proteomics

Cited by 45 publications

References 44 publications

Proteomic Changes Induced by Effective Chemopreventive Ratios of n-3:n-6 Fatty Acids and Tamoxifen against MNU-Induced Mammary Cancer in the Rat

Proteomic Changes Induced by Effective Chemopreventive Ratios of n-3:n-6 Fatty Acids and Tamoxifen against MNU-Induced Mammary Cancer in the Rat

Proteomic Tools for Cancer Research: Updating the Oncoproteomics

Recent discoveries concerning the involvement of transcription factors from the Grainyhead-like family in cancer

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