Characterization of PTPN2 and its use as a biomarker

Bussières-Marmen, Stéphanie; Hutchins, Andrew P.; Schirbel, Anja; Rebert, Nancy A.; Tiganis, Tony; Fiocchi, Claudio; Miranda‐Saavedra, Diego; Tremblay, Michel L.

doi:10.1016/j.ymeth.2013.08.020

Cited by 19 publications

(22 citation statements)

References 39 publications

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“…Three splicing variants of the gene have been reported, resulting in three different isoforms of the protein, differing in their C-termini [26]. The difference is assumed to determine substrate specificity as well as cellular locations of the proteins.…”

Section: Discussionmentioning

confidence: 99%

Loss of protein tyrosine phosphatase, non-receptor type 2 is associated with activation of AKT and tamoxifen resistance in breast cancer

Karlsson

Veenstra

Emin

et al. 2015

Breast Cancer Res Treat

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Gene copy loss of PTPN2 was detected in 16% (34/215) of the tumours and this was significantly correlated with lower levels of PTPN2 mRNA. PTPN2 gene loss and lower mRNA levels were associated with activation of AKT and a poor prognosis. Furthermore, PTPN2 gene loss was a significant predictive marker of poor benefit from tamoxifen treatment.In conclusion, genomic loss of PTPN2 may be a previously unknown mechanism of PI3K/AKT upregulation in breast cancer. PTPN2 status is a potential new clinical marker of endocrine treatment benefit which could guide further individualised therapies in breast cancer.

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Section: Discussionmentioning

confidence: 99%

Loss of protein tyrosine phosphatase, non-receptor type 2 is associated with activation of AKT and tamoxifen resistance in breast cancer

Karlsson

Veenstra

Emin

et al. 2015

Breast Cancer Res Treat

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“…Ptp61F is the fly ortholog of mammalian PTPN1 (PTP1B) [113] and PTPN2 (TC‐PTP) [114], and plays fundamental roles in growth, life span and fecundity [115]. Structurally, Ptp61F contains a PTP catalytic domain, 2 proline‐rich motifs (PXPXXP) and, depending on the splice isoform, a C‐terminus with either a nuclear‐targeting motif (isoform Ptp61Fn ), or with a hydrophobic stretch that localizes Ptp61F to the cytoplasm (isoform Ptp61Fm ) [116].…”

Section: The Drosophila Tyrosine Phosphatome Is a Streamlined Versionmentioning

confidence: 99%

A Drosophila‐centric view of protein tyrosine phosphatases

et al. 2015

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a b s t r a c tMost of our knowledge on protein tyrosine phosphatases (PTPs) is derived from human pathologies and mouse knockout models. These models largely correlate well with human disease phenotypes, but can be ambiguous due to compensatory mechanisms introduced by paralogous genes. Here we present the analysis of the PTP complement of the fruit fly and the complementary view that PTP studies in Drosophila will accelerate our understanding of PTPs in physiological and pathological conditions. With only 44 PTP genes, Drosophila represents a streamlined version of the human complement. Our integrated analysis places the Drosophila PTPs into evolutionary and functional contexts, thereby providing a platform for the exploitation of the fly for PTP research and the transfer of knowledge onto other model systems.

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“…Recent reports have found PTPN2 is a regulator of inflammatory response [9]. Its crosstalk with inflammatory pathways such as JAK/STAT has been found in immune cells like astrocytes and macrophages [32].…”

Section: Discussionmentioning

confidence: 99%

“…Previous studies have confirmed immune and inflammatory responses in the gingival epithelium play an initial role on the onset and development of diabetic periodontitis [7, 8]. Protein tyrosine phosphatase nonreceptor type 2 (PTPN2) is an intracellular tyrosine-specific phosphatase, which is expressed in epithelial cells, fibroblasts, or endothelial cells [9]. The biological function of PTPN2 is believed to vary in response to proinflammatory stimuli such as interferon-gamma (IFN- γ ), tumor necrosis factor (TNF- α ), hyperosmotic stress, or hyperglycemia [10, 11].…”

Section: Introductionmentioning

confidence: 99%

Comparison of Experimental Diabetic Periodontitis Induced byPorphyromonas gingivalisin Mice

Wang

Zhang

Aprecio

et al. 2016

Journal of Diabetes Research

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Periodontitis is one of the severe complications in diabetic patients and gingival epithelium plays an initial role on the onset and progression of this disease. However the potential mechanism is yet sufficiently understood. Meanwhile, the research on the correlational experimental animal models was also insufficient. Here, we established periodontitis with type 2 diabetes in db/db and Tallyho/JngJ (TH) mice and periodontitis with type 1 diabetes in streptozotocin induced diabetes C57BL/6J (STZ-C57) mice by oral infection of periodontal pathogen Porphyromonas gingivalis W50. We demonstrated that periodontal infected mice with high blood glucose levels showed dramatically more alveolar bone loss than their counterparts, in which infected db/db mice exhibited the most bone defects. No contrary impact could be observed between this periodontal infection and onset and severity of diabetes. The expressions of PTPN2 were inhibited whereas the expression of JAK1, STAT1, and STAT3 increased dramatically in gingival epithelia and the serum TNF-α also significantly increased in the mice with diabetic periodontitis. Our results indicated that the variations of inflammation-related protein expressions in gingival epithelia might lead to the phenotype differences in the mice with diabetic periodontitis.

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Characterization of PTPN2 and its use as a biomarker

Cited by 19 publications

References 39 publications

Loss of protein tyrosine phosphatase, non-receptor type 2 is associated with activation of AKT and tamoxifen resistance in breast cancer

Loss of protein tyrosine phosphatase, non-receptor type 2 is associated with activation of AKT and tamoxifen resistance in breast cancer

A Drosophila‐centric view of protein tyrosine phosphatases

Comparison of Experimental Diabetic Periodontitis Induced byPorphyromonas gingivalisin Mice

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