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pancreatic neoplasms/phosphatase
Linkki tallennetaan leikepöydälle
Sivu 1 alkaen 311 tuloksia
Inhibition of protein phosphatase 2A sensitizes pancreatic cancer to chemotherapy by increasing drug perfusion via HIF-1α-VEGF mediated angiogenesis.
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Pancreatic cancer is a malignant disease without efficient treatment. Improved treatments are urgently needed to enhance or replace chemotherapy. Here we used a small molecular compound LB-100 to assess the effect of pharmacological inhibition of protein phosphatase 2A (PP2A) in combination with
Haloperidol induces demethylation and expression of the dual specificity phosphatase 6 gene in MIA PaCa-2 human pancreatic cancer cells.
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OBJECTIVE
The effects of antipsychotics on various gene expressions through change in DNA methylation have been reported. Dual-specificity phosphatase 6 (DUSP6) is an extracellular signal regulated kinase 1/2 (ERK1/2)-selective phosphatase, and its expression can be suppressed by intronic
Growth of the pancreatic cancer cell line PANC-1 is inhibited by protein phosphatase 2A inhibitors through overactivation of the c-Jun N-terminal kinase pathway.
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Protein phosphatase 2A (PP2A) is a multimeric serine/threonine phosphatase that can dephosphorylate multiple kinases. It is generally considered to be a cancer suppressor as its inhibition can induce phosphorylation and activation of substrate kinases that mainly accelerate growth. We previously
Somatostatin analogues inhibit growth of pancreatic cancer by stimulating tyrosine phosphatase.
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Several analogues of somatostatin were examined in the Mia PaCa-2 human pancreatic cancer cell line for their ability to promote tyrosine phosphatase activity affecting the receptors for the epidermal growth factor. The inhibition of growth of the Mia PaCa-2 cells in culture was also evaluated to
Phorbol ester reduces phosphorylation of epidermal growth factor receptor in pancreatic cancer cells by activation of a tyrosine phosphatase.
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In this study we report that phorbol 12-myristate 13-acetate (PMA) transiently reduced the level of EGF receptor tyrosine phosphorylation in three pancreatic cancer cell lines (HPAC, SW1990, and UCVA-1) in response to EGF. The effect was maximal at 40-90 min. Pretreatment with the protein kinase C
Pancreatic tumor cells with mutant K-ras suppress ERK activity by MEK-dependent induction of MAP kinase phosphatase-2.
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Activating mutations within the K-ras gene occur in a high percentage of human pancreatic carcinomas. We reported previously that the presence of oncogenic, activated K-ras in human pancreatic carcinoma cell lines did not result in constitutive activation of the extracellular signal-regulated
Jumonji AT-rich interactive domain 1B promotes the growth of pancreatic tumors via the phosphatase and tensin homolog/protein kinase B signaling pathway.
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Jumonji AT-rich interactive domain 1B (JARID1B) has been revealed to remove methyl residues from methylated lysine 4 on histone H3 (H3K4) and has also been reported to be associated with the progression of numerous types of tumor. However, its roles and mechanisms in pancreatic cancer (PC) remain
Inhibitory and stimulatory effects of somatostatin on two human pancreatic cancer cell lines: a primary role for tyrosine phosphatase SHP-1.
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Somatostatin (SS-14) and its structural analogue SMS 201-995 (SMS) are recognized as physiological inhibitors of multiple organs and tissue functions through specific membrane receptors (sst1-sst5). The effects of SS-14 and SMS in the growth control of the pancreatic cancer cell lines MIA PaCa-2 and
Down-regulation of the dual-specificity phosphatase MKP-1 suppresses tumorigenicity of pancreatic cancer cells.
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OBJECTIVE
In both pancreatic cancer and chronic pancreatitis, there is enhanced expression of mitogenic growth factors and their tyrosine kinase receptors, which have the capacity to activate mitogen-activated protein kinase (MAPK). In view of the important role of MAPK kinase phosphatase (MKP)-1 in
Genomic analysis of DUSP6, a dual specificity MAP kinase phosphatase, in pancreatic cancer.
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DUSP6 (alias PYST1), one of the dual-specificity tyrosine phosphatases, is localized on 12q21, one of the regions of frequent allelic loss in pancreatic cancer. This gene is composed of three exons, and two forms of alternatively spliced transcripts are ubiquitously expressed. Although no mutations
[Expression of mitogen activated protein kinase phosphatase-1 in pancreatic cancer].
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OBJECTIVE
To evaluate the expression of mitogen activated protein kinase phosphatase-1(MKP-1)in pancreatic cancer.
METHODS
Totally 60 cases of normal pancreas, chronic pancreatitis(CP), and pancreatic cancer tissues were collected by operation in our hospital. Pancreatic tissues were analyzed by
Activation of protein phosphatase 2A tumor suppressor as potential treatment of pancreatic cancer.
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We utilized three tiers of screening to identify novel therapeutic agents for pancreatic cancers. First, we analyzed 14 pancreatic cancer cell lines against a panel of 66 small-molecule kinase inhibitors and dasatinib was the most potent. Second, we performed RNA expression analysis on 3
The effects of all-trans-retinoic acid on cell cycle and alkaline phosphatase activity in pancreatic cancer cells.
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Pancreatic cancer is one of the tumors with the highest mortality, poorly responding to available chemotherapeutic agents. The objective of this study was to study the anticancer effects of all-trans retinoid acid, a functional form of vitamin A, on pancreatic cancer cells. Human pancreatic cancer
Blockade of dual-specificity phosphatase 28 decreases chemo-resistance and migration in human pancreatic cancer cells.
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Pancreatic cancer remains one of the most deadly cancers, with a grave prognosis. Despite numerous endeavors to improve treatment of the neoplasm, limited progress has been made. In the present study, we investigated the role of dual specificity phosphatase 28 (DUSP28) in relation to anti-cancer
Dynamic serum alkaline phosphatase is an indicator of overall survival in pancreatic cancer.
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