New mechanisms found for PTEN protein

2007 ◽  
Keyword(s):  
Pten Protein

scholarly journals MicroRNA-1297 suppressed the Akt/GSK3β signaling pathway and stimulated neural apoptosis in an in vivo sevoflurane exposure model

2021 ◽  
Vol 49 (4) ◽  
pp. 030006052098210
Author(s):  
Quan Wang ◽  
Jingcong Luo ◽  
Ruiqiang Sun ◽  
Jia Liu
Keyword(s):  
Protein Expression ◽  
Signaling Pathway ◽  
Neuronal Apoptosis ◽  
In Vitro Model ◽  
Nervous System Development ◽  
Exposure Model ◽  
Control Group ◽  
Pten Protein ◽  
Vitro Model

Objective Common inhalation anesthetics used for clinical anesthesia (such as sevoflurane) may induce nerve cell apoptosis during central nervous system development. Furthermore, anesthetics can produce cognitive impairments, such as learning and memory impairments, that continue into adulthood. However, the precise mechanism remains largely undefined. We aimed to determine the function of microRNA-1297 (miR-1297) in sevoflurane-induced neurotoxicity. Methods Reverse transcription-polymerase chain reaction assays were used to analyze miR-1297 expression in sevoflurane-exposed mice. MTT and lactate dehydrogenase (LDH) assays were used to measure cell growth, and neuronal apoptosis was analyzed using flow cytometry. Western blot analyses were used to measure PTEN, PI3K, Akt, and GSK3β protein expression. Results In sevoflurane-exposed mice, miR-1297 expression was up-regulated compared with the control group. MiR-1297 up-regulation led to neuronal apoptosis, inhibition of cell proliferation, and increased LDH activity in the in vitro model of sevoflurane exposure. MiR-1297 up-regulation also suppressed the Akt/GSK3β signaling pathway and induced PTEN protein expression in the in vitro model. PTEN inhibition (VO-Ohpic trihydrate) reduced PTEN protein expression and decreased the effects of miR-1297 down-regulation on neuronal apoptosis in the in vitro model. Conclusion Collectively, the results indicated that miR-1297 stimulates sevoflurane-induced neurotoxicity via the Akt/GSK3β signaling pathway by regulating PTEN expression.

scholarly journals 10P The clinical actionability of PTEN protein and gene expression analysis in HR- and HER2+ breast cancers

2021 ◽  
Vol 32 ◽  
pp. S25
Author(s):  
N. Fusco ◽  
E. Sajjadi ◽  
K. Venetis ◽  
M. Invernizzi ◽  
D. Gambini ◽  
...  
Keyword(s):  
Gene Expression ◽  
Expression Analysis ◽  
Gene Expression Analysis ◽  
Breast Cancers ◽  
Pten Protein

scholarly journals PTEN Protein Loss by Immunostaining: Analytic Validation and Prognostic Indicator for a High Risk Surgical Cohort of Prostate Cancer Patients

2011 ◽  
Vol 17 (20) ◽  
pp. 6563-6573 ◽  
Author(s):  
Tamara L. Lotan ◽  
Bora Gurel ◽  
Siobhan Sutcliffe ◽  
David Esopi ◽  
Wennuan Liu ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
High Risk ◽  
Cancer Patients ◽  
Prognostic Indicator ◽  
Protein Loss ◽  
Pten Protein

Reduced Expression of PTEN Protein and Its Prognostic Implications in Invasive Ductal Carcinoma of the Breast

Oncology ◽  
2005 ◽  
Vol 68 (4-6) ◽  
pp. 398-404 ◽  
Author(s):  
Shinichi Tsutsui ◽  
Hiroshi Inoue ◽  
Kazuhiro Yasuda ◽  
Kosuke Suzuki ◽  
Hidefumi Higashi ◽  
...  
Keyword(s):  
Invasive Ductal Carcinoma ◽  
Ductal Carcinoma ◽  
Carcinoma Of The Breast ◽  
Pten Protein ◽  
Prognostic Implications

scholarly journals Binding of PTEN to Specific PDZ Domains Contributes to PTEN Protein Stability and Phosphorylation by Microtubule-associated Serine/Threonine Kinases

2005 ◽  
Vol 280 (32) ◽  
pp. 28936-28943 ◽  
Author(s):  
Miguel Valiente ◽  
Amparo Andrés-Pons ◽  
Beatriz Gomar ◽  
Josema Torres ◽  
Anabel Gil ◽  
...  
Keyword(s):  
Protein Stability ◽  
Pdz Domains ◽  
Pten Protein ◽  
Threonine Kinases

scholarly journals Registered report: A coding-independent function of gene and pseudogene mRNAs regulates tumour biology

eLife ◽  
2015 ◽  
Vol 4 ◽  
Author(s):  
Israr Khan ◽  
John Kerwin ◽  
Kate Owen ◽  
Erin Griner ◽  
Keyword(s):  
Cell Proliferation ◽  
Tumor Cell ◽  
Cancer Biology ◽  
Open Science ◽  
Tumor Cell Proliferation ◽  
Independent Function ◽  
Pten Protein ◽  
Protein Levels ◽  
High Profile ◽  
Tumour Biology

The Reproducibility Project: Cancer Biology seeks to address growing concerns about reproducibility in scientific research by conducting replications of selected experiments from a number of high-profile papers in the field of cancer biology. The papers, which were published between 2010 and 2012, were selected on the basis of citations and Altmetric scores (<xref ref-type="bibr" rid="bib9">Errington et al., 2014</xref>). This Registered report describes the proposed replication plan of key experiments from ‘A coding-independent function of gene and pseudogene mRNAs regulates tumour biology’ by <xref ref-type="bibr" rid="bib26">Poliseno et al. (2010)</xref>, published in Nature in 2010. The key experiments to be replicated are reported in Figures 1D, 2F-H, and 4A. In these experiments, Poliseno and colleagues report microRNAs miR-19b and miR-20a transcriptionally suppress both PTEN and PTENP1 in prostate cancer cells (Figure 1D; <xref ref-type="bibr" rid="bib26">Poliseno et al., 2010</xref>). Decreased expression of PTEN and/or PTENP1 resulted in downregulated PTEN protein levels (Figure 2H), downregulation of both mRNAs (Figure 2G), and increased tumor cell proliferation (Figure 2F; <xref ref-type="bibr" rid="bib26">Poliseno et al., 2010</xref>). Furthermore, overexpression of the PTEN 3′ UTR enhanced PTENP1 mRNA abundance limiting tumor cell proliferation, providing additional evidence for the co-regulation of PTEN and PTENP1 (Figure 4A; <xref ref-type="bibr" rid="bib26">Poliseno et al., 2010</xref>). The Reproducibility Project: Cancer Biology is collaboration between the Center for Open Science and Science Exchange, and the results of the replications will be published in eLife.

In silico approach of naringin as potent phosphatase and tensin homolog (PTEN) protein agonist against prostate cancer

2020 ◽  
pp. 1-10 ◽  
Author(s):  
Sankar Muthumanickam ◽  
Thangamariyappan Indhumathi ◽  
Pandi Boomi ◽  
Ramachandran Balajee ◽  
Jeyaraman Jeyakanthan ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
In Silico ◽  
Pten Protein ◽  
Phosphatase And Tensin Homolog ◽  
Tensin Homolog

scholarly journals The relevance of precision epitope mapping for accurate oncologic diagnostic based on PTEN protein expression in tumours

2017 ◽  
Vol 28 ◽  
pp. vii8-vii9
Author(s):  
J. Mingo ◽  
S. Luna ◽  
A. Gaafar ◽  
R. Ruiz ◽  
A. Carracedo ◽  
...  
Keyword(s):  
Protein Expression ◽  
Epitope Mapping ◽  
Pten Protein

scholarly journals Decreased phosphatase PTEN amplifies PI3K signaling and enhances proinflammatory cytokine release in COPD

2017 ◽  
Vol 313 (2) ◽  
pp. L230-L239 ◽  
Author(s):  
Satoru Yanagisawa ◽  
Jonathan R. Baker ◽  
Chaitanya Vuppusetty ◽  
Peter Fenwick ◽  
Louise E. Donnelly ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Pi3k Pathway ◽  
Negative Regulator ◽  
Pi3k Signaling ◽  
Pten Protein ◽  
Protein Levels ◽  
Enhanced Production ◽  
Phosphorylated Akt ◽  
Peripheral Lung ◽  
The Impact

The phosphatidylinositol 3-kinase (PI3K) pathway is activated in chronic obstructive pulmonary disease (COPD), but the regulatory mechanisms for this pathway are yet to be elucidated. The aim of this study was to determine the expression and role of phosphatase and tensin homolog deleted from chromosome 10 (PTEN), a negative regulator of the PI3K pathway, in COPD. PTEN protein expression was measured in the peripheral lung of COPD patients compared with smoking and nonsmoking controls. The direct influence of cigarette smoke extract (CSE) on PTEN expression was assessed using primary lung epithelial cells and a cell line (BEAS-2B) in the presence or absence of l-buthionine-sulfoximine (BSO) to deplete intracellular glutathione. The impact of PTEN knockdown by RNA interference on cytokine production was also examined. In peripheral lung, PTEN protein was significantly decreased in patients with COPD compared with the subjects without COPD ( P < 0.001) and positively correlated with the severity of airflow obstruction (forced expiratory volume in 1-s percent predicted; r = 0.50; P = 0.0012). Conversely, phosphorylated Akt, as a marker of PI3K activation, showed a negative correlation with PTEN protein levels ( r = −0.41; P = 0.0042). In both primary bronchial epithelial cells and BEAS-2B cells, CSE decreased PTEN protein, which was reversed by N-acetyl cysteine treatment. PTEN knockdown potentiated Akt phosphorylation and enhanced production of proinflammatory cytokines, such as IL-6, CXCL8, CCL2, and CCL5. In conclusion, oxidative stress reduces PTEN protein levels, which may result in increased PI3K signaling and amplification of inflammation in COPD.

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