Quantitative tissue proteomic investigation of invasive ductal carcinoma of breast with luminal B HER2 positive and HER2 enriched subtypes towards potential diagnostic and therapeutic biomarkers

Pendharkar, Namita; Gajbhiye, Akshada; Taunk, Khushman; RoyChoudhury, Sourav; Dhali, Snigdha; Seal, Shubhendu; Mane, Anupama; Abhang, Subodhini A.; Santra, Manas Kumar; Chaudhury, Koel; Rapole, Srikanth

doi:10.1016/j.jprot.2015.11.024

Cited by 28 publications

(31 citation statements)

References 92 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Studies have demonstrated that ANXA3 is a potential biomarker for carcinogenesis, metastasis and resistance to chemotherapy in many cancers such as ovarian cancer [11], gastric cancer [12], breast cancer [13, 14] and liver carcinoma [15, 16]. But there is hardly any investigation of its role in CRC.…”

Section: Discussionmentioning

confidence: 99%

High-throughput proteomics integrated with gene microarray for discovery of colorectal cancer potential biomarkers

Zhong

et al. 2016

Oncotarget

View full text Add to dashboard Cite

Proteins, as executives of genes' instructions, are responsible for cellular phenotypes. Integrating proteomics with gene microarray, we conducted this study to identify potential protein biomarkers of colorectal cancer (CRC). Isobaric tags with related and absolute quantitation (iTRAQ) labeling mass spectrometry (MS) was applied to screen and identify differentially expressed proteins between paired CRC and adjacent normal mucosa. Meanwhile, Affymetrix U133plus2.0 microarrays were used to perform gene microarray analysis. Verification experiments included immunohistochemistry (IHC), western blot and enzyme-linked immunosorbent assay (ELISA) of selected proteins. Overall, 5469 differentially expressed proteins were detected with iTRAQ-MS from 24 matched CRC and adjacent normal tissues. And gene microarray identified 39859 differential genes from 52 patients. Of these, 3083 differential proteins had corresponding differentially expressed genes, with 245 proteins and their genes showed >1.5-fold change in expression level. Gene ontology enrichment analysis revealed that up-regulated proteins were more involved in cell adhesion and motion than down-regulated proteins. In addition, up-regulated proteins were more likely to be located in nucleus and vesicles. Further verification experiments with IHC confirmed differential expression levels of 5 proteins (S100 calcium-binding protein A9, annexin A3, nicotinamide phosphoribosyltransferase, carboxylesterase 2 and calcium activated chloride channel A1) between CRC and normal tissues. Besides, western blot showed a stepwise increase of annexin A3 abundance in normal colorectal mucosa, adenoma and CRC tissues. ELISA results revealed significantly higher serum levels of S100 calcium-binding protein A9 and annexin A3 in CRC patients than healthy controls, validating diagnostic value of these proteins. Cell experiments showed that inhibition of annexin A3 could suppress CRC cell proliferation and aggressiveness. S100 calcium-binding protein A9, annexin A3, nicotinamide phosphoribosyltransferase, carboxylesterase 2 and calcium activated chloride channel A1 were probably potential biomarkers of colorectal cancer. Annexin A3 was a potentially valuable therapeutic target of CRC.

show abstract

Section: Discussionmentioning

confidence: 99%

High-throughput proteomics integrated with gene microarray for discovery of colorectal cancer potential biomarkers

Zhong

et al. 2016

Oncotarget

View full text Add to dashboard Cite

show abstract

“…In addition, Cao J et al have identified that PRDX1 protects the tumour suppressive function of PTEN phosphatase from ROS-induced inactivation, and inhibits Ras-driven mammary tumours [58]. Notably, biomarker studies have confirmed that PRDX1 is one of the diagnostic biomarkers for invasive ductal carcinoma of breast with human epidermal growth factor receptor-2 (HER2)-enriched subtypes [59], and PRDX1 protects ERa from oxidative stress-induced suppression and is a protein biomarker of favourable prognosis in mammary tumours [60]. miRNAs post-transcriptionally repress gene expression mostly by binding to the 3 0 UTR of mRNA transcripts to either cause degradation or prevent translation, depending upon complementarity.…”

Section: Prdx1 and Breast Cancermentioning

confidence: 99%

Peroxiredoxin 1 – an antioxidant enzyme in cancer

Ding

Fan

2016

J Cellular Molecular Medi

171

131

View full text Add to dashboard Cite

Peroxiredoxins (PRDXs), a ubiquitous family of redox‐regulating proteins, are reported of potential to eliminate various reactive oxygen species (ROS). As a major member of the antioxidant enzymes, PRDX1 can become easily over‐oxidized on its catalytically active cysteine induced by a variety of stimuli in vitro and in vivo. In nucleus, oligomeric PRDX1 directly associates with p53 or transcription factors such as c‐Myc, NF‐κB and AR, and thus affects their bioactivities upon gene regulation, which in turn induces or suppresses cell death. Additionally, PRDX1 in cytoplasm has anti‐apoptotic potential through direct or indirect interactions with several ROS‐dependent (redox regulation) effectors, including ASK1, p66Shc, GSTpi/JNK and c‐Abl kinase. PRDX1 is proven to be a versatile molecule regulating cell growth, differentiation and apoptosis. Recent studies have found that PRDX1 and/or PRDX1‐regulated ROS‐dependent signalling pathways play an important role in the progression and metastasis of human tumours, particularly in breast, oesophageal and lung cancers. In this paper, we review the structure, effector functions of PRDX1, its role in cancer and the pivotal role of ROS in anticancer treatment.

show abstract

“…The latest 12-Plex ‘DiLeu’ isobaric tags are cheaper as reagents can be readily synthesized in-house 47 unlike other members in these strategies. Both iTRAQ and TMT strategies have been broadly employed in cancer studies for drug discovery 49 , investigating cancer signaling 50 , as well as for investigating diagnostic and prognosis markers 51 . iTRAQ has also been employed to predict cancer recurrence and patient survival in triple negative breast tissue samples 52 .…”

Section: Quantitative Mass Spectrometry-based Proteomic Strategies Inmentioning

confidence: 99%

Advancement of mass spectrometry-based proteomics technologies to explore triple negative breast cancer

et al. 2017

View full text Add to dashboard Cite

Understanding the complexity of cancer biology requires extensive information about the cancer proteome over the course of the disease. The recent advances in mass spectrometry-based proteomics technologies have led to the accumulation of an incredible amount of such proteomic information. This information allows us to identify protein signatures or protein biomarkers, which can be used to improve cancer diagnosis, prognosis and treatment. For example, mass spectrometry-based proteomics has been used in breast cancer research for over two decades to elucidate protein function. Breast cancer is a heterogeneous group of diseases with distinct molecular features that are reflected in tumour characteristics and clinical outcomes. Compared with all other subtypes of breast cancer, triple-negative breast cancer is perhaps the most distinct in nature and heterogeneity. In this review, we provide an introductory overview of the application of advanced proteomic technologies to triple-negative breast cancer research.

show abstract

Quantitative tissue proteomic investigation of invasive ductal carcinoma of breast with luminal B HER2 positive and HER2 enriched subtypes towards potential diagnostic and therapeutic biomarkers

Cited by 28 publications

References 92 publications

High-throughput proteomics integrated with gene microarray for discovery of colorectal cancer potential biomarkers

High-throughput proteomics integrated with gene microarray for discovery of colorectal cancer potential biomarkers

Peroxiredoxin 1 – an antioxidant enzyme in cancer

Advancement of mass spectrometry-based proteomics technologies to explore triple negative breast cancer

Contact Info

Product

Resources

About