scholarly journals In situ characterizing membrane lipid phenotype of breast cancer cells using mass spectrometry profiling

2015 ◽  
Vol 5 (1) ◽  
Author(s):  
Manwen He ◽  
Shuai Guo ◽  
Zhili Li
Keyword(s):  
Breast Cancer ◽  
Mass Spectrometry ◽  
Cancer Cells ◽  
Breast Cancer Cells ◽  
Membrane Lipid ◽  
Lipid Phenotype

scholarly journals Biocompatible Electrochemical Sensor Based on Platinum-Nickel Alloy Nanoparticles for In Situ Monitoring of Hydrogen Sulfide in Breast Cancer Cells

Nanomaterials ◽  
2022 ◽  
Vol 12 (2) ◽  
pp. 258
Author(s):  
Asit Kumar Panda ◽  
Murugan Keerthi ◽  
Rajalakshmi Sakthivel ◽  
Udesh Dhawan ◽  
Xinke Liu ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Hydrogen Sulfide ◽  
Electrochemical Sensor ◽  
Cancer Cells ◽  
Breast Cancer Cells ◽  
In Situ Monitoring ◽  
Quantitative Detection ◽  
Alloy Nanoparticles ◽  
Ptni Alloy

Hydrogen sulfide (H2S), an endogenous gasotransmitter, is produced in mammalian systems and is closely associated with pathological and physiological functions. Nevertheless, the complete conversion of H2S is still unpredictable owing to the limited number of sensors for accurate and quantitative detection of H2S in biological samples. In this study, we constructed a disposable electrochemical sensor based on PtNi alloy nanoparticles (PtNi NPs) for sensitive and specific in situ monitoring of H2S released by human breast cancer cells. PtNi alloy NPs with an average size of 5.6 nm were prepared by a simple hydrothermal approach. The conversion of different forms of sulfides (e.g., H2S, HS−, and S2−) under various physiological conditions hindered the direct detection of H2S in live cells. PtNi NPs catalyze the electrochemical oxidation of H2S in a neutral phosphate buffer (PB, pH 7.0). The PtNi-based sensing platform demonstrated a linear detection range of 0.013–1031 µM and the limit of detection was 0.004 µM (S/N = 3). Moreover, the PtNi sensor exhibited a sensitivity of 0.323 μA μM−1 cm−2. In addition, the stability, repeatability, reproducibility, and anti-interference ability of the PtNi sensor exhibited satisfactory results. The PtNi sensor was able to successfully quantify H2S in pond water, urine, and saliva samples. Finally, the biocompatible PtNi electrode was effectively employed for the real-time quantification of H2S released from breast cancer cells and mouse fibroblasts.

scholarly journals Single-band upconversion nanoprobes for multiplexed simultaneous in situ molecular mapping of cancer biomarkers

2015 ◽  
Vol 6 (1) ◽  
Author(s):  
Lei Zhou ◽  
Rui Wang ◽  
Chi Yao ◽  
Xiaomin Li ◽  
Chengli Wang ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Cancer Cells ◽  
Western Blotting ◽  
Breast Cancer Cells ◽  
Molecular Mapping ◽  
Single Band ◽  
Upconversion Nanoparticles ◽  
Single Colour ◽  
Tissue Specimens

Abstract The identification of potential diagnostic markers and target molecules among the plethora of tumour oncoproteins for cancer diagnosis requires facile technology that is capable of quantitatively analysing multiple biomarkers in tumour cells and tissues. Diagnostic and prognostic classifications of human tumours are currently based on the western blotting and single-colour immunohistochemical methods that are not suitable for multiplexed detection. Herein, we report a general and novel method to prepare single-band upconversion nanoparticles with different colours. The expression levels of three biomarkers in breast cancer cells were determined using single-band upconversion nanoparticles, western blotting and immunohistochemical technologies with excellent correlation. Significantly, the application of antibody-conjugated single-band upconversion nanoparticle molecular profiling technology can achieve the multiplexed simultaneous in situ biodetection of biomarkers in breast cancer cells and tissue specimens and produce more accurate results for the simultaneous quantification of proteins present at low levels compared with classical immunohistochemical technology.

scholarly journals Modulation of in Situ Estrogen Synthesis by Proline-, Glutamic Acid-, and Leucine-Rich Protein-1: Potential Estrogen Receptor Autocrine Signaling Loop in Breast Cancer Cells

2008 ◽  
Vol 22 (3) ◽  
pp. 649-664 ◽  
Author(s):  
Rajib Rajhans ◽  
Hareesh B. Nair ◽  
Sujit S. Nair ◽  
Valerie Cortez ◽  
Kijima Ikuko ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Estrogen Receptor ◽  
Glutamic Acid ◽  
Cancer Cells ◽  
Breast Cancer Cells ◽  
Breast Tumors ◽  
Aromatase Activity ◽  
Aromatase Expression ◽  
Estrogen Synthesis

Abstract In situ estrogen synthesis is implicated in tumor cell proliferation through autocrine or paracrine mechanisms especially in postmenopausal women. Several recent studies demonstrated activity of aromatase, an enzyme that plays a critical role in estrogen synthesis in breast tumors. Proline-, glutamic acid-, and leucine-rich protein-1 (PELP1/MNAR) is an estrogen receptor (ER) coregulator, and its expression is deregulated in breast tumors. In this study, we examined whether PELP1 promotes tumor growth by promoting local estrogen synthesis using breast cancer cells (MCF7) that stably overexpress PELP1. Immunohistochemistry revealed increased aromatase expression in MCF7-PELP1-induced xenograft tumors. Real-time PCR analysis showed enhanced activation of the aromatase promoter in MCF7-PELP1 clones compared with MCF7 cells. Using a tritiated-water release assay, we demonstrated that MCF7-PELP1 clones exhibit increased aromatase activity compared with control MCF-7 cells. PELP1 deregulation uniquely up-regulated aromatase expression via activation of aromatase promoter I.3/II, and growth factor signaling enhanced PELP1 activation of aromatase. PELP1-mediated induction of aromatase requires functional Src and phosphatidylinositol-3-kinase pathways. Mechanistic studies revealed that PELP1 interactions with ER-related receptor-α and proline-rich nuclear receptor coregulatory protein 2 lead to activation of aromatase. Immunohistochemistry analysis of breast tumor array showed increased expression of aromatase in ductal carcinoma in situ and node-positive tumors compared with no or weak expression in normal breast tissue. Fifty-four percent (n = 79) of PELP1-overexpressing tumors also overexpressed aromatase compared with 36% (n = 47) in PELP1 low-expressing tumors. Our results suggest that PELP1 regulation of aromatase represents a novel mechanism for in situ estrogen synthesis leading to tumor proliferation by autocrine loop and open a new avenue for ablating local aromatase activity in breast tumors.

scholarly journals Anti-Warburg effect by targeting HRD1-PFKP pathway may inhibit breast cancer progression

2020 ◽  
Author(s):  
Ya Fan ◽  
Jia Wang ◽  
Yuemei Xu ◽  
Yipin Wang ◽  
Tao Song ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Mass Spectrometry ◽  
Cancer Cells ◽  
Warburg Effect ◽  
Breast Cancer Cells ◽  
Aerobic Glycolysis ◽  
Mass Spectrometry Analysis ◽  
Cancer Proliferation ◽  
Spectrometry Analysis ◽  
Proliferation And Invasion

Abstract Background: Our previous studies have shown that the E3 ubiquitin ligase of HMG-CoA reductase degradation 1 (HRD1) functions as a tumor suppressor, as overexpression of HRD1 suppressed breast cancer proliferation and invasion. However, its role in breast cancer cell glucose metabolism was unclear. Here, our aim was to uncover the role and molecular mechanisms of HRD1 in regulating aerobic glycolysis in breast cancer. Methods: The effect of HRD1 on robic glycolysis in breast cancer cells were assessed. Then the proliferation, colony formation ability, invasion and migration of breast cancer cells were evaluated. The relationship between HRD1 and PFKP was validated by Mass spectrometry analysis, immunofluorescence and co-immunoprecipitation. The level of PFKP ubiquitination was measured using ubiquitylation assay. Furthermore, the tumor growth and metastasis in mice xenografts were observed. Results: We found that upregulation of HRD1 clearly decreased aerobic glycolysis, and subsequently inhibited breast cancer proliferation and invasion. Mass spectrometry analysis results revealed a large HRD1 interactome, which included PFKP (platelet isoform of phosphofructokinase), a critical enzyme involved in the Warburg Effect in breast cancer. Mechanistically, HRD1 interacted and colocalized with PFKP in the cytoplasm, targeted PFKP for ubiquitination and degradation, and ultimately reduced PFKP expression and activity in breast cancer cells. HRD1 inhibited breast cancer growth and metastasis in vivo through a PFKP-dependent wayConclusions: Our findings reveal a new regulatory role of HRD1 in Warburg effect and provide a key contributor in breast cancer metabolism.

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