scholarly journals Data set of the protein expression profiles of Luminal A, Claudin-low and overexpressing HER2 + breast cancer cell lines by iTRAQ labelling and tandem mass spectrometry

Data in Brief ◽  
2015 ◽  
Vol 4 ◽  
pp. 292-301 ◽  
Author(s):  
Karla Grisel Calderón-González ◽  
Ma Luz Valero Rustarazo ◽  
Maria Luisa Labra-Barrios ◽  
César Isaac Bazán-Méndez ◽  
Alejandra Tavera-Tapia ◽  
...  
2015 ◽  
Vol 124 ◽  
pp. 50-78 ◽  
Author(s):  
Karla Grisel Calderón-González ◽  
Ma Luz Valero Rustarazo ◽  
Maria Luisa Labra-Barrios ◽  
César Isaac Bazán-Méndez ◽  
Alejandra Tavera-Tapia ◽  
...  

Biomolecules ◽  
2020 ◽  
Vol 10 (2) ◽  
pp. 183 ◽  
Author(s):  
Biri-Kovács ◽  
Adorján ◽  
Szabó ◽  
Szeder ◽  
Bősze ◽  
...  

Human epidermal growth factor (HER2) is a transmembrane tyrosine kinase receptor that is frequently overexpressed in breast cancer. Its increased level prognoses a poor patient outcome and a high mortality rate. Despite the widening spectrum of therapies that are becoming available to treat HER2+ breast cancer, its side effects and resistance still make this protein a valuable object of research in targeted tumor therapy. The role of tumor-targeting peptides has become more and more prominent in the last few decades due to their simple synthesis and pharmakokinetic properties. Here, we examine two fluorescently-labeled HER2-specific peptides and their combined analogues that are developed to target the extracellular region of HER2. The peptides are investigated on breast cancer cell lines with different HER2 expression profiles. Moreover, their extracellular localization and specificity are confirmed by flow cytometry and confocal microscopy. Therefore, a new, combined HER2 binding conjugate is obtained that interacts with HER2-overexpressing cells with high affinity and specificity. Furthermore, secondary structure prediction reveals that the α-helical content of the peptides is associated with their receptor recognition. This highly specific conjugate can be used as a starting point for diagnostical or drug-targeting purposes in upcoming studies.


2020 ◽  
Vol 17 (1) ◽  
Author(s):  
Lori A. Sturtz ◽  
Guisong Wang ◽  
Punit Shah ◽  
Richard Searfoss ◽  
Praveen-Kumar Raj-Kumar ◽  
...  

Abstract Background Proteomic studies are typically conducted using flash-frozen (FF) samples utilizing tandem mass spectrometry (MS). However, FF specimens are comprised of multiple cell types, making it difficult to ascertain the proteomic profiles of specific cells. Conversely, OCT-embedded (Optimal Cutting Temperature compound) specimens can undergo laser microdissection (LMD) to capture and study specific cell types separately from the cell mixture. In the current study, we compared proteomic data obtained from FF and OCT samples to determine if samples that are stored and processed differently produce comparable results. Methods Proteins were extracted from FF and OCT-embedded invasive breast tumors from 5 female patients. FF specimens were lysed via homogenization (FF/HOM) while OCT-embedded specimens underwent LMD to collect only tumor cells (OCT/LMD-T) or both tumor and stromal cells (OCT/LMD-TS) followed by incubation at 37 °C. Proteins were extracted using the illustra triplePrep kit and then trypsin-digested, TMT-labeled, and processed by two-dimensional liquid chromatography-tandem mass spectrometry (2D LC–MS/MS). Proteins were identified and quantified with Proteome Discoverer v1.4 and comparative analyses performed to identify proteins that were significantly differentially expressed amongst the different processing methods. Results Among the 4,950 proteins consistently quantified across all samples, 216 and 171 proteins were significantly differentially expressed (adjusted p-value < 0.05; |log2 FC|> 1) between FF/HOM vs. OCT/LMD-T and FF/HOM vs. OCT/LMD-TS, respectively, with most proteins being more highly abundant in the FF/HOM samples. PCA and unsupervised hierarchical clustering analysis with these 216 and 171 proteins were able to distinguish FF/HOM from OCT/LMD-T and OCT/LMD-TS samples, respectively. Similar analyses using significantly differentially enriched GO terms also discriminated FF/HOM from OCT/LMD samples. No significantly differentially expressed proteins were detected between the OCT/LMD-T and OCT/LMD-TS samples but trended differences were detected. Conclusions The proteomic profiles of the OCT/LMD-TS samples were more similar to those from OCT/LMD-T samples than FF/HOM samples, suggesting a strong influence from the sample processing methods. These results indicate that in LC–MS/MS proteomic studies, FF/HOM samples exhibit different protein expression profiles from OCT/LMD samples and thus, results from these two different methods cannot be directly compared.


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