Role of the protein tyrosine phosphatase SHP-1 in Interleukin-6 regulation of prostate cancer cells

The Prostate ◽  
2010 ◽  
Vol 70 (14) ◽  
pp. 1491-1500 ◽  
Author(s):  
Helena Tassidis ◽  
Zoran Culig ◽  
Anette Gjörloff Wingren ◽  
Pirkko Härkönen
Keyword(s):  
Prostate Cancer ◽  
Cancer Cells ◽  
Protein Tyrosine Phosphatase ◽  
Interleukin 6 ◽  
Tyrosine Phosphatase ◽  
Prostate Cancer Cells ◽  
Protein Tyrosine

scholarly journals Knockdown of protein tyrosine phosphatase SHP-1 inhibits G1/S progression in prostate cancer cells through the regulation of components of the cell-cycle machinery

Oncogene ◽  
2009 ◽  
Vol 29 (3) ◽  
pp. 345-355 ◽  
Author(s):  
F J Rodríguez-Ubreva ◽  
A E Cariaga-Martinez ◽  
M A Cortés ◽  
M Romero-De Pablos ◽  
S Ropero ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Cell Cycle ◽  
Cancer Cells ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Prostate Cancer Cells ◽  
Protein Tyrosine ◽  
Cell Cycle Machinery

scholarly journals Androgen-regulation of the protein tyrosine phosphatase PTPRR activates ERK1/2 signalling in prostate cancer cells

BMC Cancer ◽  
2015 ◽  
Vol 15 (1) ◽  
Author(s):  
Jennifer Munkley ◽  
Nicholas P Lafferty ◽  
Gabriela Kalna ◽  
Craig N Robson ◽  
Hing Y Leung ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Cancer Cells ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Prostate Cancer Cells ◽  
Protein Tyrosine ◽  
Androgen Regulation

scholarly journals Downregulation of protein tyrosine phosphatase PTPL1 alters cell cycle and upregulates invasion-related genes in prostate cancer cells

2012 ◽  
Vol 29 (4) ◽  
pp. 349-358 ◽  
Author(s):  
Carolina Castilla ◽  
M. Luz Flores ◽  
José M. Conde ◽  
Rafael Medina ◽  
Francisco J. Torrubia ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Cell Cycle ◽  
Cancer Cells ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Prostate Cancer Cells ◽  
Protein Tyrosine

scholarly journals Interaction of Pyk2 and PTP-PEST with leupaxin in prostate cancer cells

2007 ◽  
Vol 292 (6) ◽  
pp. C2288-C2296 ◽  
Author(s):  
Surasri Nandan Sahu ◽  
Stephanie Nunez ◽  
Guang Bai ◽  
Anandarup Gupta
Keyword(s):  
Prostate Cancer ◽  
Cancer Cells ◽  
Rho Gtpase ◽  
Extended Family ◽  
Tyrosine Phosphatase ◽  
Adaptor Proteins ◽  
Prostate Cancer Cells ◽  
Protein Tyrosine ◽  
Signaling Complex

We have identified the presence of leupaxin (LPXN), which belongs to the paxillin extended family of focal adhesion-associated adaptor proteins, in prostate cancer cells. Previous studies have demonstrated that LPXN is a component of the podosomal signaling complex found in osteoclasts, where LPXN was found to associate with the protein tyrosine kinases Pyk2 and c-Src and the cytosolic protein tyrosine phosphatase-proline-, glutamate-, serine-, and threonine-rich sequence (PTP-PEST). In the current study, LPXN was detectable as a 50-kDa protein in PC-3 cells, a bone-derived metastatic prostate cancer cell line. In PC-3 cells, LPXN was also found to associate with Pyk2, c-Src, and PTP-PEST. A siRNA-mediated inhibition of LPXN resulted in decreased in vitro PC-3 cell migration. A recombinant adenoviral-mediated overexpression of LPXN resulted in an increased association of Pyk2 with LPXN, whereas a similar adenoviral-mediated overexpression of PTP-PEST resulted in decreased association of Pyk2 and c-Src with LPXN. The overexpression of LPXN in PC-3 cells resulted in increased migration, as assessed by in vitro Transwell migration assays. On the contrary, the overexpression of PTP-PEST in PC-3 cells resulted in decreased migration. The overexpression of LPXN resulted in increased activity of Rho GTPase, which was decreased in PTP-PEST-overexpressing cells. The increase in Rho GTPase activity following overexpression of LPXN was inhibited in the presence of Y27632, a selective inhibitor of Rho GTPase. In conclusion, our data demonstrate that LPXN forms a signaling complex with Pyk2, c-Src, and PTP-PEST to regulate migration of prostate cancer cells.

scholarly journals Cellular prostatic acid phosphatase: a protein tyrosine phosphatase involved in androgen-independent proliferation of prostate cancer

2005 ◽  
Vol 12 (4) ◽  
pp. 805-822 ◽  
Author(s):  
Suresh Veeramani ◽  
Ta-Chun Yuan ◽  
Siu-Ju Chen ◽  
Fen-Fen Lin ◽  
Juliette E Petersen ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Cancer Cells ◽  
Cancer Progression ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Prostatic Acid Phosphatase ◽  
Prostate Cancer Progression ◽  
Prostate Cancer Cells ◽  
Her 2 ◽  
Androgen Independent

Human prostatic acid phosphatase (PAcP) was used as a valuable surrogate marker for monitoring prostate cancer prior to the availability of prostate-specific antigen (PSA). Even though the level of PAcP is increased in the circulation of prostate cancer patients, its intracellular level and activity are greatly diminished in prostate cancer cells. Recent advances in understanding the function of the cellular form of PAcP (cPAcP) have shed some light on its role in prostate carcinogenesis, which may have potential applications for prostate cancer therapy. It is now evident that cPAcP functions as a neutral protein tyrosine phosphatase (PTP) in prostate cancer cells and dephosphorylates HER-2/ErbB-2/Neu (HER-2: human epidermal growth factor receptor-2) at the phosphotyrosine (p-Tyr) residues. Dephosphorylation of HER-2 at its p-Tyr residues results in the down-regulation of its specific activity, which leads to decreases in growth and tumorigenicity of those cancer cells. Conversely, decreased cPAcP expression correlates with hyperphosphorylation of HER-2 at tyrosine residues and activation of downstream extracellular signal-regulated kinase (ERK)/mitogen activated protein kinase (MAPK) signaling, which results in prostate cancer progression as well as androgen-independent growth of prostate cancer cells. These in vitro results on the effect of cPAcP on androgen-independent growth of prostate cancer cells corroborate the clinical findings that cPAcP level is greatly decreased in advanced prostate cancer and provide insights into one of the molecular mechanisms involved in prostate cancer progression. Results from experiments using xenograft animal models further indicate a novel role of cPAcP as a tumor suppressor. Future studies are warranted to clarify the use of cPAcP as a therapeutic agent in human prostate cancer patients.

Integrative genome wide analysis of protein tyrosine phosphatases identifies CDC25C as prognostic and predictive marker for chemoresistance in breast cancer

2021 ◽  
pp. 1-14
Author(s):  
Rachel Topno ◽  
Nazia Nazam ◽  
Pallawi Kumari ◽  
Manoj Kumar ◽  
Pallavi Agarwal
Keyword(s):  
Breast Cancer ◽  
Cancer Cells ◽  
Protein Tyrosine Phosphatase ◽  
Breast Cancer Cells ◽  
Tyrosine Phosphatase ◽  
Expression Patterns ◽  
Prognostic Index ◽  
Predictive Marker ◽  
Protein Tyrosine

BACKGROUND: The breast cancer subtype deficient in estrogen receptor and human epidermal growth factor receptor-2 (ER-/HER2-) displays enhanced aggressiveness, metastasis and disease relapse due to chemoresistance. ER-/HER2- patients lack molecularly targeted treatment hence, new therapeutic and prognostic biomarkers are required for better patient management. OBJECTIVES: To investigate the prognostic role of protein tyrosine phosphatase genes in Breast Cancer and their relevance as predictive markers for chemoresistance. METHODS: We examined the expression of 114 protein tyrosine phosphatase (PTP) genes in 1700 breast cancer patient’s tumor samples with respect to ER-/HER2- subtype. Correlation of relevant candidates with chemoresistance was analyzed in breast cancer cells resistant to taxane/anthracycline based drugs. The prognostic value of key candidates was assessed using Kaplan Meier plots and Nottingham prognostic index and expression pattern was confirmed using qRT-PCR. The epigenetic regulation was analyzed using ChIP-Seq datasets. By plotting ROC plots, clinical outcome after treatment with taxane and anthracycline was established. RESULTS: Overexpression of CDC25A and CDC25C and under-expression of DUSP16 was observed in tumor samples of ER-/HER2- patients and breast cancer cells. Similar expression patterns of these candidate genes were observed in MCF7 cells resistant to paclitaxel and adriamycin and also correlated with poor prognosis of breast cancer patients. Increased CDC25A and CDC25C in ER-/HER2- cells was found to be regulated epigenetically by histone H3K4 methylation. Overall, the present study establishes increased expression of protein tyrosine phosphatase CDC25C as a poor prognostic marker for breast cancer. CONCLUSION: Our study highlights the role of CDC25C in chemoresistance to taxane and anthracycline based therapy and proposes CDC25C as a potential predictive marker for these cancer therapies.

Sign in / Sign up

Export Citation Format

Share Document