scholarly journals Mass Spectrometry Analysis of the Native Protein Complex Containing Actinin-4 in Prostate Cancer Cells

2006 ◽  
Vol 6 (3) ◽  
pp. 479-491 ◽  
Author(s):  
Tomohiko Hara ◽  
Kazufumi Honda ◽  
Miki Shitashige ◽  
Masaya Ono ◽  
Hideyasu Matsuyama ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Mass Spectrometry ◽  
Cancer Cells ◽  
Protein Complex ◽  
Mass Spectrometry Analysis ◽  
Native Protein ◽  
Prostate Cancer Cells ◽  
Spectrometry Analysis

scholarly journals A re-evaluation of LINE-1 ORF2 expression in LNCaP prostate cancer cells

Mobile DNA ◽  
2019 ◽  
Vol 10 (1) ◽  
Author(s):  
Erica M. Briggs ◽  
Corrado Spadafora ◽  
Susan K. Logan
Keyword(s):  
Prostate Cancer ◽  
Cancer Cells ◽  
Cellular Localization ◽  
Mass Spectrometry Analysis ◽  
Hek293 Cells ◽  
Lncap Cells ◽  
Prostate Cancer Cells ◽  
Spectrometry Analysis ◽  
Sirna Knockdown ◽  
Long Interspersed Element

Abstract Background We previously examined expression of Long Interspersed Element-1 (LINE-1) in a variety of prostate cancer cells including hormone-dependent LNCaP cells. These studies demonstrated expression and sub-cellular localization of LINE-1 proteins, ORF1p, with antibody 4H1, and ORF2p, with antibody chA1-L1. Results Here we conduct immunoprecipitation/mass spectrometry analysis using chA1-L1 antibody against ORF2p in LNCaP cells. Our results indicate that antigens detected by the antibody include the transcriptional regulator BCLAF1. We show that chA1-L1 recognizes BCLAF1 using siRNA knockdown and overexpression of a tagged BCLAF1. We also show that chA1-L1 antibody recognizes ORF2p in HEK293 cells overexpressing LINE-1. Further, analysis of ORF2p (chA1-L1) and BCLAF1 foci using immunofluorescence in LNCaP cells showed significant colocalization. Conclusions Overall, our findings indicate that chA1-L1 antibody recognizes both BCLAF1 and ORF2p but the majority of antigen recognized in LNCaP cells is BCLAF1.

scholarly journals Molecular signatures associated with prostate cancer cell line (PC-3) exposure to inactivated Zika virus

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Jeany Delafiori ◽  
Estela de Oliveira Lima ◽  
Mohamed Ziad Dabaja ◽  
Flávia Luísa Dias-Audibert ◽  
Diogo Noin de Oliveira ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Cell Growth ◽  
Cancer Cells ◽  
Cancer Cell ◽  
Zika Virus ◽  
Prostate Cancer Cell ◽  
Antiproliferative Effect ◽  
Mass Spectrometry Analysis ◽  
Molecular Signatures ◽  
Prostate Cancer Cells

Abstract The recent outbreak of Zika virus (ZIKV) infection associated with microcephaly cases has elicited much research on the mechanisms involved in ZIKV-host cell interactions. It has been described that Zika virus impairs cell growth, raising a hypothesis about its oncolytic potential against cancer cells. ZIKV tumor cell growth inhibition was later confirmed for glioblastoma. It was also demonstrated that an inactivated ZIKV prototype (ZVp) based on bacterial outer membrane vesicles has antiproliferative activity upon other cancer cell lines, such as PC-3 prostate cancer cell. This study aims at understanding the pathways that might be involved with the antiproliferative effect of Zika virus against prostate cancer cells. A metabolomic approach based on high-resolution mass spectrometry analysis led to the identification of 21 statistically relevant markers of PC-3 cells treated with ZVp. The markers were associated with metabolic alterations that trigger lipid remodeling, endoplasmic reticulum stress, inflammatory mediators, as well as disrupted porphyrin and folate metabolism. These findings highlight molecular signatures of ZVp-induced response that may be involved on cellular pathways triggered by its antiproliferative effect. To our knowledge, this is the first reported metabolomic assessment of ZIKV effect on prostate cancer cells, a promising topic for further research.

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.

scholarly journals HRD1 Elicitation of An Anti-Warburg Effect by Targeting PFKP to Inhibit Breast Cancer Growth and Progression

2020 ◽  
Author(s):  
Ya Fan ◽  
Wang Jia ◽  
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 in vivo were observed by subcutaneous tumorigenesis in nude mice. 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. Conclusions: 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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