The role of protein tyrosine phosphatases in prostate cancer biology

Nunes‐Xavier, Caroline E.; Mingo, Janire; López, José I.; Pulido, Rafael

doi:10.1016/j.bbamcr.2018.06.016

Cited by 20 publications

(15 citation statements)

References 156 publications

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“…The cytoplasmic protein tyrosine phosphatase (PTP), characterized by containing two Src homology 2 (SH2) N-terminus, a single catalytic domain, and a C-terminal PTP domain, is referred to as SHP-1. The expression of SHP-1 in prostate cancer is inversely correlated with tumor stage and malignancy, as well as with biochemical recurrence after prostatectomy [51][52][53][54]. In addition, SHP-1 is known to have a tumor-suppressor role in various cancers due to the SHP-1-negative regulation of JAKs-STAT activation via growth factors and cytokines [54][55][56][57].…”

Section: Discussionmentioning

confidence: 99%

Crosstalk between Prostate Cancer Cells and Tumor-Associated Fibroblasts Enhances the Malignancy by Inhibiting the Tumor Suppressor PLZF

Noh

Jeong

Lee

et al. 2020

Cancers

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Although prostate cancer is clinically manageable during the early stages of progression, metastatic progression severely compromises the prognosis and leads to mortality. Constitutive activation of STAT3 has been connected to prostate cancer malignancy, and abolishing the STAT3 activity may diminish tumor growth and metastasis. However, its suppressor genes and pathways have not been well established. In this study, we show that promyelocytic leukemia zinc finger (PLZF) has a putative tumor-suppressor function in prostate cancer by inhibiting phosphorylation of STAT3. Compared with a benign prostate, high-grade prostate cancer patient tissue was negatively correlated with PLZF expression. PLZF depletion accelerated proliferation and survival, migration, and invasion in human prostate cancer cells. Mechanistically, we demonstrated a novel role of PLZF as the transcriptional regulator of the tyrosine phosphatase SHP-1 that inhibits the oncogenic JAKs–STAT3 pathway. These results suggest that the collapse of PLZF expression by the CCL3 derived from fibroblasts accelerates the cell migration and invasion properties of prostate cancer cells. Our results suggest that increasing PLZF could be an attractive strategy for suppressing prostate cancer metastasis as well as for tumor growth.

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Section: Discussionmentioning

confidence: 99%

Crosstalk between Prostate Cancer Cells and Tumor-Associated Fibroblasts Enhances the Malignancy by Inhibiting the Tumor Suppressor PLZF

Noh

Jeong

Lee

et al. 2020

Cancers

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“…Recently, it was shown that growth factor receptor-bound protein 10 (GRB10), has pro-proliferative function in prostate carcinoma [86], and that it sustains AR activity by interacting with PP2A [87]. [88] and are omitted from this presentation with the exception of PTEN. Protein-protein interactions were downloaded from the STRING [89] website (experiments and databases interaction sources were used) and visualized in Cytoscape [90].…”

Section: Phosphorylationmentioning

confidence: 99%

“…Kinases, adapter proteins, and transcription factors are shown to visualize the network that drives prostate cancer progression. The roles of phosphatases in prostate cancer have been recently reviewed [88] and are omitted from this presentation with the exception of PTEN. Protein-protein interactions were downloaded from the STRING [89] website (experiments and databases interaction sources were used) and visualized in Cytoscape [90].…”

Section: Phosphorylationmentioning

confidence: 99%

Post-Translational Modifications That Drive Prostate Cancer Progression

Samaržija

2021

Biomolecules

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While a protein primary structure is determined by genetic code, its specific functional form is mostly achieved in a dynamic interplay that includes actions of many enzymes involved in post-translational modifications. This versatile repertoire is widely used by cells to direct their response to external stimuli, regulate transcription and protein localization and to keep proteostasis. Herein, post-translational modifications with evident potency to drive prostate cancer are explored. A comprehensive list of proteome-wide and single protein post-translational modifications and their involvement in phenotypic outcomes is presented. Specifically, the data on phosphorylation, glycosylation, ubiquitination, SUMOylation, acetylation, and lipidation in prostate cancer and the enzymes involved are collected. This type of knowledge is especially valuable in cases when cancer cells do not differ in the expression or mutational status of a protein, but its differential activity is regulated on the level of post-translational modifications. Since their driving roles in prostate cancer, post-translational modifications are widely studied in attempts to advance prostate cancer treatment. Current strategies that exploit the potential of post-translational modifications in prostate cancer therapy are presented.

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“…Aberrant protein phosphorylation is one of most typical characteristics of tumor cells. Protein tyrosine phosphatases (PTPs) are critical enzymes that modulate the phosphorylation status of intracellular signaling molecules ( 6 – 8 ). It is well-established that PTPs negatively or positively regulate cancer-associated signaling pathways in breast cancer ( 8 – 10 ).…”

Section: Introductionmentioning

confidence: 99%

“…Protein tyrosine phosphatases (PTPs) are critical enzymes that modulate the phosphorylation status of intracellular signaling molecules ( 6 – 8 ). It is well-established that PTPs negatively or positively regulate cancer-associated signaling pathways in breast cancer ( 8 – 10 ). PTP1B overexpression promotes proliferation and migration by regulating the phosphorylation of steroid receptor coactivator ( 11 ).…”

Section: Introductionmentioning

confidence: 99%

PTPRA facilitates cancer growth and migration via the TNF‑α‑mediated PTPRA‑NF‑κB pathway in MCF‑7 breast cancer cells

et al. 2020

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Protein tyrosine phosphatase receptor type A (PTPRA), one of the classic protein tyrosine phosphatases, is crucial for modulating tumorigenesis and metastasis in breast cancer; however, its functional mechanism has not fully elucidated. The present study assessed PTPRA expression and estimated its clinical impact on survival using the Gene Expression Profiling Interactive Analysis database (GEPIA). Growth curves, colony formations and Transwell assays were utilized to examine cell proliferation and migration. Additionally, luciferase reporter assays were used to examine the potential tumor signaling pathways targeted by PTPRA in HEK293T cells. Furthermore, quantitative PCR (qPCR) was utilized to confirm the transcriptional regulation of PTPRA expression. Bioinformatic analyses of data from GEPIA identified PTPRA overexpression in patients with breast cancer. The growth curve, colony formation and transwell experiments demonstrated that PTPRA upregulation significantly promoted the cell proliferation and migration of MCF-7 breast cancer cells. In contrast, PTPRA knockdown significantly attenuated cell proliferation and migration. Mechanistic experiments revealed that the transcriptional activity of NF-κB was higher compared with other classic tumor pathways when they were activated by PTPRA in HEK293T cells. Furthermore, the transcriptional activity of NF-κB was altered in a PTPRA-dose-dependent manner. Additionally, following exposure to TNF-α, PTPRA-deficient MCF-7 cells exhibited lower NF-κB transcriptional activity compared with normal control cells. The results of the present study demonstrate that PTPRA overexpression accelerates inflammatory tumor phenotypes in breast cancer and that the TNF-α-mediated PTPRA-NF-κB pathway may offer novel insight into early diagnosis and optimum treatment for breast cancer.

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The role of protein tyrosine phosphatases in prostate cancer biology

Cited by 20 publications

References 156 publications

Crosstalk between Prostate Cancer Cells and Tumor-Associated Fibroblasts Enhances the Malignancy by Inhibiting the Tumor Suppressor PLZF

Crosstalk between Prostate Cancer Cells and Tumor-Associated Fibroblasts Enhances the Malignancy by Inhibiting the Tumor Suppressor PLZF

Post-Translational Modifications That Drive Prostate Cancer Progression

PTPRA facilitates cancer growth and migration via the TNF‑α‑mediated PTPRA‑NF‑κB pathway in MCF‑7 breast cancer cells

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The role of protein tyrosine phosphatases in prostate cancer biology

Cited by 20 publications

References 156 publications

Crosstalk between Prostate Cancer Cells and Tumor-Associated Fibroblasts Enhances the Malignancy by Inhibiting the Tumor Suppressor PLZF

Crosstalk between Prostate Cancer Cells and Tumor-Associated Fibroblasts Enhances the Malignancy by Inhibiting the Tumor Suppressor PLZF

Post-Translational Modifications That Drive Prostate Cancer Progression

PTPRA facilitates cancer growth and migration via the TNF‑&alpha;‑mediated PTPRA‑NF‑&kappa;B pathway in MCF‑7 breast cancer cells

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PTPRA facilitates cancer growth and migration via the TNF‑α‑mediated PTPRA‑NF‑κB pathway in MCF‑7 breast cancer cells