scholarly journals CANCER BIOLOGY: Drug-resistant breast cancer cells frequently retain expression of a functional wild-type p53 protein

1996 ◽  
Vol 17 (7) ◽  
pp. 1417-1427 ◽  
Author(s):  
Jean M. Gudas ◽  
Hoang Nguyen ◽  
Tao Li ◽  
Lisa Sadzewicz ◽  
Robert Robey ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Cancer Cells ◽  
Cancer Biology ◽  
Breast Cancer Cells ◽  
P53 Protein ◽  
Drug Resistant ◽  
Wild Type ◽  
Wild Type P53

scholarly journals Induction of p53 expression and apoptosis by a recombinant dual-target MDM2/MDMX inhibitory protein in wild-type p53 breast cancer cells

2013 ◽  
Vol 43 (6) ◽  
pp. 1935-1942 ◽  
Author(s):  
QIAN-QIAN GENG ◽  
DAN-FENG DONG ◽  
NAN-ZHENG CHEN ◽  
YIN-YING WU ◽  
EN-XIAO LI ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Cancer Cells ◽  
Breast Cancer Cells ◽  
Wild Type ◽  
Inhibitory Protein ◽  
P53 Expression ◽  
Wild Type P53 ◽  
Dual Target

scholarly journals Biochemical Background in Mitochondria Affects 2HG Production by IDH2 and ADHFE1 in Breast Carcinoma

Cancers ◽  
2021 ◽  
Vol 13 (7) ◽  
pp. 1709
Author(s):  
Jitka Špačková ◽  
Klára Gotvaldová ◽  
Aleš Dvořák ◽  
Alexandra Urbančoková ◽  
Kateřina Pospíšilová ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Breast Carcinoma ◽  
Cancer Cells ◽  
Cancer Biology ◽  
Breast Cancer Cells ◽  
Breast Cancer Patients ◽  
Wild Type ◽  
Isocitrate Dehydrogenase 2 ◽  
Enzyme Molecules ◽  
Analytical Approaches

Mitochondrial production of 2-hydroxyglutarate (2HG) can be catalyzed by wild-type isocitrate dehydrogenase 2 (IDH2) and alcohol dehydrogenase, iron-containing 1 (ADHFE1). We investigated whether biochemical background and substrate concentration in breast cancer cells promote 2HG production. To estimate its role in 2HG production, we quantified 2HG levels and its enantiomers in breast cancer cells using analytical approaches for metabolomics. By manipulation of mitochondrial substrate fluxes using genetic and pharmacological approaches, we demonstrated the existence of active competition between 2HG producing enzymes, i.e., IDH2 and ADHFE1. Moreover, we showed that distinct fractions of IDH2 enzyme molecules operate in distinct oxido-reductive modes, providing NADPH and producing 2HG simultaneously. We have also detected 2HG release in the urine of breast cancer patients undergoing adjuvant therapy and detected a correlation with stages of breast carcinoma development. In summary, we provide a background for vital mitochondrial production of 2HG in breast cancer cells with outcomes towards cancer biology and possible future diagnosis of breast carcinoma.

scholarly journals 2-[(4-Hydroxybenzyl) Amino] Phenol (HBAP) Restores the Mutated p53 to the Level Similar to That of Wild-Type p53 Protein and Inhibits Breast Cancer Growth in vivo to by Inducing Tumor Cells Apoptosis

2020 ◽  
Vol 8 ◽  
Author(s):  
Chenxi Xu ◽  
Jianjian Zhuang ◽  
Xiaobo Zhang
Keyword(s):  
Breast Cancer ◽  
Tumor Cells ◽  
Deep Sea ◽  
Breast Cancer Cells ◽  
P53 Protein ◽  
Mutant P53 ◽  
Wild Type ◽  
Amino Phenol ◽  
Wild Type P53

P53 is a transcriptional factor that plays important roles in apoptosis and is mutated in more than 50% of tumor cells. However, the restoration of mutated p53 to the level similar to wild-type p53 by a natural compound has not been explored intensively. In this study, the 2-[(4-hydroxybenzyl) amino] phenol (HBAP) compound, obtained from deep-sea virus-challenged thermophile Geobacillus sp. E263, interacted specifically with the mutated p53 protein. HBAP was able to induce apoptosis of p53-mutated breast cancer cells, but not normal breast cells and p53-unmutated breast cancer cells. HBAP activated the mutant p53 transcriptional activity by restoring the function of mutant p53 to that of wild-type p53. Further analysis indicated that HBAP bound only to the DNA binding domain of mutant p53 and that the interaction was dependent on the HBAP hydroxyl groups. In vivo data demonstrated that HBAP was toxicity-free and could suppress tumor growth by inducing tumor cell apoptosis. Therefore our findings revealed that recovering mutated p53 function to that of wild-type p53 caused by HBAP triggered cancer cell apoptosis and that metabolites from deep-sea virus-challenged thermophiles could be a promising source of anti-tumor drugs.

scholarly journals Modulation of the poly (ADP-ribose) polymerase inhibitor response and DNA recombination in breast cancer cells by drugs affecting endogenous wild-type p53

2014 ◽  
Vol 35 (10) ◽  
pp. 2273-2282 ◽  
Author(s):  
Ivanildce Cristiane Ireno ◽  
Rahel Stephanie Wiehe ◽  
Andreea Iulia Stahl ◽  
Stephanie Hampp ◽  
Sevtap Aydin ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Cancer Cells ◽  
Breast Cancer Cells ◽  
Dna Recombination ◽  
Wild Type ◽  
Polymerase Inhibitor ◽  
Wild Type P53

scholarly journals Wild-type p53 controls the level of fibronectin expression in breast cancer cells

2017 ◽  
Vol 38 (4) ◽  
pp. 2551-2557 ◽  
Author(s):  
Daeun You ◽  
Seung Pil Jung ◽  
Yisun Jeong ◽  
Soo Youn Bae ◽  
Sangmin Kim
Keyword(s):  
Breast Cancer ◽  
Cancer Cells ◽  
Breast Cancer Cells ◽  
Wild Type ◽  
Fibronectin Expression ◽  
Wild Type P53

scholarly journals Biochemical Background in Mitochondria Affects 2HG Production by IDH2 and ADHFE1 in Breast Carcinoma

2021 ◽  
Author(s):  
Jitka Špačková ◽  
Klára Gotvaldová ◽  
Aleš Dvořák ◽  
Alexandra Urbančoková ◽  
Kateřina Pospíšilová ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Breast Carcinoma ◽  
Adjuvant Therapy ◽  
Cancer Cells ◽  
Cancer Biology ◽  
Breast Cancer Cells ◽  
Wild Type ◽  
Isocitrate Dehydrogenase 2 ◽  
Enzyme Molecules ◽  
Analytical Approaches

Mitochondrial production of 2-hydroxyglutarate (R-2HG) can be catalyzed by wild-type isocitrate dehydrogenase 2 (IDH2) and alcohol dehydrogenase, iron-containing 1 (ADHFE1). We investigated whether biochemical background and substrate concentration in breast cancer cells promote 2HG production. To estimate its role in 2HG production, we analyzed 2HG levels and its enantiomers in breast cancer cells using analytical approaches for metabolomics. By manipulation of mitochondrial substrate fluxes, including glutaminolysis, using genetic and pharmacological approaches we demonstrated the existence of an active competition between 2HG producing enzymes, i.e. IDH2 and ADHFE1. Moreover, we show that distinct fractions of IDH2 enzyme molecules operate in distinct oxido-reductive modes, providing NADPH and producing 2HG simultaneously. We have also detected 2HG release into breast cancer patient´s urine undergoing adjuvant therapy and detected a correlation with stages of breast carcinoma development. In summary, we provide a background for vital mitochondrial production of 2HG in breast cancer cells with outcomes towards cancer biology and possible future diagnosis of breast carcinoma.

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