The Role Of Protein Tyrosine Phosphatases In Breast Cancer
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The Role Of Protein Tyrosine Phosphatases In Breast Cancer
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Author : Christina Holzer
language : en
Publisher:
Release Date : 2009
The Role Of Protein Tyrosine Phosphatases In Breast Cancer written by Christina Holzer and has been published by this book supported file pdf, txt, epub, kindle and other format this book has been release on 2009 with categories.
Protein Tyrosine Phosphatases In Cancer
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Author : Benjamin G. Neel
language : en
Publisher: Springer
Release Date : 2016-08-05
Protein Tyrosine Phosphatases In Cancer written by Benjamin G. Neel and has been published by Springer this book supported file pdf, txt, epub, kindle and other format this book has been release on 2016-08-05 with Medical categories.
This book aims to bridge the gap in understanding how protein-tyrosine phosphatases (PTPs), which carry out the reverse reaction of tyrosine phosphorylation, feature in cancer cell biology. The expertly authored chapters will first review the general features of the PTP superfamily, including their overall structure and enzymological properties; use selected examples of individual PTP superfamily members, to illustrate emerging data on the role of PTPs in cancer; and will review the current status of PTP-based drug development efforts. Protein Tyrosine Phosphatases in Cancer,from renowned researchers Benjamin Neel and Nicholas Tonks, is invaluable reading for researchers in oncology, stem cell signaling,and biochemistry.
The Role Of Protein Tyrosine Phosphatase Gamma In Human Breast Carcinogenesis
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Author : Sherry T. Shu
language : en
Publisher:
Release Date : 2005
The Role Of Protein Tyrosine Phosphatase Gamma In Human Breast Carcinogenesis written by Sherry T. Shu and has been published by this book supported file pdf, txt, epub, kindle and other format this book has been release on 2005 with Carcinogenesis categories.
Abstract: Reduced expression of protein tyrosine phosphatase gamma (PTPG) has been shown in breast cancer cell lines and cancerous tissue. PTPG over-expression in breast cancer cell line MCF-7 leads to the inhibition of cell proliferation and anchorage- independent growth. To further investigate the anti-carcinogenic abilities of PTPG in vivo, athymic nude mice were implanted with MCF-7 cells, which were stably transfected with PTPG cDNA (M7-PTPG) or empty vectors (M7-PCR). Tumor formation was significantly lower at the M7-PTPG cells implanted sites (10%) compared to sites where M7-PCR cells were implanted (100%), indicating that tumor formation was inhibited by the effect of PTPG in vivo. To explore the signaling pathway that PTPG is involved, breast cancer-related signaling cDNA array assays were performed. Seventy genes showed at least a 1.5 fold of expression difference in M7-PTPG cells compared to M7- PCR cells. The increase of the levels of p21(cip) and p27(kip) in M7-PTPG cells was confirmed by Western blot analyses. M7-PTPG cells also showed delayed re-entry into the cell cycle after the cells were released from G0/G1 cell cycle arrest, accompanied by lower phosphorylation levels of ERK1/2, compared to the control cells. Moreover, there was an aberrant methylation pattern in the PTPG promoter region of the breast cancer cell lines and patient's cancerous tissue. PTPG expression in SkBr3 cells can be recovered by treating with deoxy-5-azacytidine (DAC) and trichostatin A (TSA). Our results indicate that PTPG inhibits breast tumor promotion in vivo, presumably through cell cycle arrest by the up-regulated p21(cip) and p27(kip) proteins; and DNA methylation is a possible mechanism that leads to PTPG silencing in breast cancer cells. The results obtained from this study suggest that PTPG plays important role in breast carcinogenesis and may serve as a breast cancer therapeutic target.
Opposing Roles For Protein Tyrosine Phosphatases Shp2 And Ptpn12 In Breast Cancer
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Author : Nicola Aceto
language : en
Publisher:
Release Date : 2011
Opposing Roles For Protein Tyrosine Phosphatases Shp2 And Ptpn12 In Breast Cancer written by Nicola Aceto and has been published by this book supported file pdf, txt, epub, kindle and other format this book has been release on 2011 with categories.
Characterization Of Protein Tyrosine Phosphatases In Human Breast Epithelial Cells Neoplastically Transformed By The Neu Oncogene
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Author : Yifan Zhai
language : en
Publisher:
Release Date : 1993
Characterization Of Protein Tyrosine Phosphatases In Human Breast Epithelial Cells Neoplastically Transformed By The Neu Oncogene written by Yifan Zhai and has been published by this book supported file pdf, txt, epub, kindle and other format this book has been release on 1993 with Breast categories.
Protein Tyrosine Phosphatases In Breast Cancer
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Author : Mairin Rafferty
language : en
Publisher:
Release Date : 2002
Protein Tyrosine Phosphatases In Breast Cancer written by Mairin Rafferty and has been published by this book supported file pdf, txt, epub, kindle and other format this book has been release on 2002 with categories.
Adhesion Linked Protein Tyrosine Phosphatases Morphogenesis And Breast Cancer Progression
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Author :
language : en
Publisher:
Release Date : 2004
Adhesion Linked Protein Tyrosine Phosphatases Morphogenesis And Breast Cancer Progression written by and has been published by this book supported file pdf, txt, epub, kindle and other format this book has been release on 2004 with categories.
Stromal-epithelial interactions regulate mammary epithelial cell (MEC) fate via integrin-growth factor receptor (GFR) interactions. Integrin-GFR crosstalk influences MEC behavior through activation of tyrosine kinase signaling that is tempered by protein tyrosine phosphatase (PTP) activity of which we know little about. Using a degenerate RT-PCR to amplify PTPs expressed in differentiated versus non-differentiated MECs, we identified the Band 4.1 PTPs MEG1 and Dl as two candidate PTP metastasis suppressors. Our studies show that during MEC differentiation PTP MEGl and Dl expression rise dramatically, coincident with assembly of E-cadherin/Beta-catenin adherens junction formation. However, both mRNA and protein expression of MEGl and Dl become repressed following MEC tissue differentiation. Because we could not establish any correlation between MEC growth, or tissue polarization, this suggests that MEG1 and Dl expression may be functionally linked to adherens junction assembly. Consistently, malignant MECs that fail to assemble adherens junctions do not modulate MEGl or Dl expression. Moreover, MEGl expression is not induced in phenotypically reverting tumors, or down regulated in dormant structures. This suggests that these Band 4.1 PTPs may be functionally-linked to molecules mediating adherens junction formation.
The Role Of Rptp Alpha Like Protein Tyrosine Phosphatases In Mammary Tumorigenesis
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Author :
language : en
Publisher:
Release Date : 1999
The Role Of Rptp Alpha Like Protein Tyrosine Phosphatases In Mammary Tumorigenesis written by and has been published by this book supported file pdf, txt, epub, kindle and other format this book has been release on 1999 with categories.
Tyrosine phosphorylation is controlled by a balance of tyrosine kinases (PTKs) and protein tyrosine phosphatases (PTPs). Whereas the contribution of PTKs to breast tumorigenesis is the subject of intense scrutiny, the potential role of PTPs is poorly known. RPTP alpha is implicated in the activation of Src family kinases, and regulation of integrin signaling, cell adhesion, and growth factor responsiveness. To explore its potential contribution to human neoplasia, we surveyed RPTP alpha protein levels in primary human breast cancer. We found RPTPa levels to vary widely among tumors, with 29% of cases manifesting significant overexpression. High RPTP alpha protein levels correlated significantly with low tumor grade and positive estrogen receptor status. Expression of RPTPC alpha in breast carcinoma cells led to growth inhibition, associated with increased accumulation in G(0) and G(1), and delayed tumor growth and metastasis. To our knowledge, this is the first example of a study correlating expression level of a specific bona fide PTP with neoplastic disease status in humans.
Tumor Progression And Metastasis
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Author : Ahmed Lasfar
language : en
Publisher:
Release Date : 2020
Tumor Progression And Metastasis written by Ahmed Lasfar and has been published by this book supported file pdf, txt, epub, kindle and other format this book has been release on 2020 with categories.
Cell Adhesion Linked Protein Tyrosine Phosphatases And Breast Cancer Metastasis
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Author :
language : en
Publisher:
Release Date : 2004
Cell Adhesion Linked Protein Tyrosine Phosphatases And Breast Cancer Metastasis written by and has been published by this book supported file pdf, txt, epub, kindle and other format this book has been release on 2004 with categories.
21 "classical" protein tyrosine phosphatases (PTPs) were identified in human mammary epithelial cell (MEC) lines. Degenerate RT-PCR followed by restriction fragment differential display (RFDD) and specific RT-PCR were used to assess expression in the continuous HMT-3522 cell series that includes both non-malignant Si and tumorigenic T4-2 cells in monolayer and during normal and dysregulated morphogenesis in EHS-ECM (Matrigel). PTP expression was generally higher in tumorigenic T4-2 cells and unchanged by disorganized growth in Matigel. in contrast, coordination of expression was suggested by the transient upregulation (relative to monolayer cultures) of a number of PTPs during acinar morphogenesis of non-malignant Si. The kinetics of downregulation for some suggested that growth arrest may be the main regulatory input. Others however, downregulate with more rapid kinetics before significant growth arrest suggesting different regulatory inputs. Feedback from of cell-cell adherens junctions (AJ) may be one such input as ectopic expression of a dominant negative E-cadherin construct that blocks AJ formation delayed but did not prevent downregulation of selected PTPs. Modest upregulation of actin cytoskeleton regulating PTPs in response to decreases in substrate compliancy occur when normal MCF10A were plated on (1 order of magnitude) softer (tissue-like) Matrigel coupled polyacrylamide gels suggesting that these PTPs may be responding to, or mediating corresponding actin cytoskeletal reaorganization. PTPN12 is a cytoplasmic PTP highly expressed in MECs that localizes transiently to actin polymerizing zones including lamellopodial leading edges and the metaphase mitotic spindle and plasma membrane. Stable downregulation of PTPN12 by retroviral mediated shRNAi resulted in derangements of the actin cytoskeleton in MCF10A cells. These cells grew more rapidly and formed larger but normally polarized acini in Matrigel.