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  1. Article ; Online: Triptolide Inhibits Lung Cancer Cell Migration, Invasion, and Metastasis.

    Reno, Theresa A / Kim, Jae Y / Raz, Dan J

    The Annals of thoracic surgery

    2015  Volume 100, Issue 5, Page(s) 1817–24; discussion 1824–5

    Abstract: Background: Triptolide is an extract from Tripterygium wilfordii used in traditional Chinese medicine to treat autoimmune disorders. Triptolide has anticancer effects in vitro and is reported to impair cancer cell migration. We studied whether ... ...

    Abstract Background: Triptolide is an extract from Tripterygium wilfordii used in traditional Chinese medicine to treat autoimmune disorders. Triptolide has anticancer effects in vitro and is reported to impair cancer cell migration. We studied whether triptolide inhibits lung cancer cell migration and metastasis.
    Methods: We determined the microRNA expression profile of triptolide-treated cells. We tested the effects of triptolide treatment on migration and invasion of lung cancer cells by using Transwell filters coated with fibronectin and Matrigel, respectively. Western blot analyses were used to compare expression of proteins involved in cell migration before and after 10 nmol/L triptolide treatment. Tail vein injections with H358 cells were performed. The mice were treated with 1 mg/kg triptolide or vehicle by intraperitoneal injection three times per week. Lung and liver metastases were compared at 9 weeks. Means of groups were compared by using a t test.
    Results: Triptolide altered the expression of microRNAs involved in cellular movement and significantly decreased migration and invasion of lung cancer cells from approximately 18 to 3 cells per field (p < 0.001). Triptolide decreases focal adhesion kinase expression, which leads to impairment of downstream signaling. Finally, triptolide-treated mice injected with lung cancer cells significantly decreased metastatic colony formation in the lungs (p < 0.01).
    Conclusions: Triptolide decreases lung cancer cell migration and invasion in vitro and inhibits metastatic tumor formation in mice. Triptolide suppresses focal adhesion kinase, which causes deregulation of the migration machinery. These results suggest that triptolide inhibits lung cancer metastasis and should be investigated as a new lung cancer therapy.
    MeSH term(s) Antineoplastic Agents, Alkylating/pharmacology ; Antineoplastic Agents, Alkylating/therapeutic use ; Cell Movement/drug effects ; Diterpenes/pharmacology ; Diterpenes/therapeutic use ; Epoxy Compounds/pharmacology ; Epoxy Compounds/therapeutic use ; Humans ; Lung Neoplasms/drug therapy ; Lung Neoplasms/pathology ; Neoplasm Invasiveness ; Neoplasm Metastasis/drug therapy ; Phenanthrenes/pharmacology ; Phenanthrenes/therapeutic use ; Tumor Cells, Cultured
    Chemical Substances Antineoplastic Agents, Alkylating ; Diterpenes ; Epoxy Compounds ; Phenanthrenes ; triptolide (19ALD1S53J)
    Language English
    Publishing date 2015-11
    Publishing country Netherlands
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 211007-6
    ISSN 1552-6259 ; 0003-4975
    ISSN (online) 1552-6259
    ISSN 0003-4975
    DOI 10.1016/j.athoracsur.2015.05.074
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 252: Show issues Location:
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  2. Article ; Online: The triptolide derivative MRx102 inhibits Wnt pathway activation and has potent anti-tumor effects in lung cancer.

    Reno, Theresa A / Tong, Sun-Wing / Wu, Jun / Fidler, John M / Nelson, Rebecca / Kim, Jae Y / Raz, Dan J

    BMC cancer

    2016  Volume 16, Page(s) 439

    Abstract: Background: The natural compound triptolide has been shown to decrease cell proliferation and induce apoptosis and cellular senescence. We previously demonstrated that triptolide decreases tumor formation and metastasis of human non-small cell lung ... ...

    Abstract Background: The natural compound triptolide has been shown to decrease cell proliferation and induce apoptosis and cellular senescence. We previously demonstrated that triptolide decreases tumor formation and metastasis of human non-small cell lung cancer cells (NSCLC). Due to the toxicity of triptolide, derivatives of the natural compound have been developed that show more favorable toxicity profiles and pharmacokinetics in animal models. The purpose of this study was to evaluate MRx102 as a novel therapeutic for lung cancer.
    Methods: Mice injected subcutaneously with H460 lung cancer cells were treated with MRx102 or carboplatin to determine the effect of MRx102 on tumor formation in comparison to standard treatment. Patient-derived xenografts (PDX) with different WIF1 expression levels were treated with MRx102 or cisplatin. We tested the effects of MRx102 treatment on migration and invasion of lung cancer cells using Transwell filters coated with fibronectin and Matrigel, respectively. Tail vein injections using H460 and A549 cells were performed.
    Results: Here we report that the triptolide derivative MRx102 significantly decreases NSCLC proliferation and stimulates apoptosis. Further, MRx102 potently inhibits NSCLC haptotactic migration and invasion through Matrigel. In vivo, NSCLC tumor formation and metastasis were greatly decreased by MRx102 treatment. The decrease in tumor formation by MRx102 in the patient-derived xenograft model was WIF1-dependent, demonstrating that MRx102 is a potent inhibitor of the Wnt pathway in low WIF1 expressing NSCLC patient tumors.
    Conclusions: These results indicate that MRx102 has potent antitumor effects both in vitro and in vivo, and is a potential novel therapy for the treatment of NSCLC.
    MeSH term(s) A549 Cells ; Adaptor Proteins, Signal Transducing/metabolism ; Animals ; Antineoplastic Agents/administration & dosage ; Antineoplastic Agents/adverse effects ; Antineoplastic Agents/therapeutic use ; Apoptosis/drug effects ; Carboplatin/administration & dosage ; Carboplatin/therapeutic use ; Carcinoma, Non-Small-Cell Lung/drug therapy ; Carcinoma, Non-Small-Cell Lung/metabolism ; Carcinoma, Non-Small-Cell Lung/pathology ; Cell Movement/drug effects ; Cell Proliferation/drug effects ; Diterpenes/adverse effects ; Diterpenes/therapeutic use ; Drug Evaluation, Preclinical ; Drug Therapy, Combination ; Epoxy Compounds/adverse effects ; Epoxy Compounds/therapeutic use ; Humans ; Lung Neoplasms/drug therapy ; Lung Neoplasms/metabolism ; Lung Neoplasms/pathology ; Mice ; Neoplasm Invasiveness ; Phenanthrenes/administration & dosage ; Phenanthrenes/adverse effects ; Phenanthrenes/therapeutic use ; Repressor Proteins/metabolism ; Wnt Signaling Pathway/drug effects ; Xenograft Model Antitumor Assays
    Chemical Substances Adaptor Proteins, Signal Transducing ; Antineoplastic Agents ; Diterpenes ; Epoxy Compounds ; MRx102 ; Phenanthrenes ; Repressor Proteins ; WIF1 protein, human ; triptolide (19ALD1S53J) ; Carboplatin (BG3F62OND5)
    Language English
    Publishing date 2016--11
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
    ISSN 1471-2407
    ISSN (online) 1471-2407
    DOI 10.1186/s12885-016-2487-7
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Dynamic phosphorylation of tyrosine 665 in pseudopodium-enriched atypical kinase 1 (PEAK1) is essential for the regulation of cell migration and focal adhesion turnover.

    Bristow, Jeanne M / Reno, Theresa A / Jo, Minji / Gonias, Steven L / Klemke, Richard L

    The Journal of biological chemistry

    2012  Volume 288, Issue 1, Page(s) 123–131

    Abstract: Pseudopodium-enriched atypical kinase 1 (PEAK1) is a recently described tyrosine kinase that associates with the actin cytoskeleton and focal adhesion (FA) in migrating cells. PEAK1 is known to promote cell migration, but the responsible mechanisms ... ...

    Abstract Pseudopodium-enriched atypical kinase 1 (PEAK1) is a recently described tyrosine kinase that associates with the actin cytoskeleton and focal adhesion (FA) in migrating cells. PEAK1 is known to promote cell migration, but the responsible mechanisms remain unclear. Here, we show that PEAK1 controls FA assembly and disassembly in a dynamic pathway controlled by PEAK1 phosphorylation at Tyr-665. Knockdown of endogenous PEAK1 inhibits random cell migration. In PEAK1-deficient cells, FA lifetimes are decreased, FA assembly times are shortened, and FA disassembly times are extended. Phosphorylation of Tyr-665 in PEAK1 is essential for normal PEAK1 localization and its function in the regulation of FAs; however, constitutive phosphorylation of PEAK1 Tyr-665 is also disruptive of its function, indicating a requirement for precise spatiotemporal regulation of PEAK1. Src family kinases are required for normal PEAK1 localization and function. Finally, we provide evidence that PEAK1 promotes cancer cell invasion through Matrigel by a mechanism that requires dynamic regulation of Tyr-665 phosphorylation.
    MeSH term(s) Antineoplastic Agents/pharmacology ; Cell Line, Tumor ; Cell Movement ; Cell Proliferation ; Collagen/chemistry ; Drug Combinations ; Focal Adhesions/chemistry ; Gene Expression Regulation ; Humans ; Laminin/chemistry ; Paxillin/metabolism ; Phosphorylation ; Protein-Tyrosine Kinases/chemistry ; Proteoglycans/chemistry ; Time Factors ; Tyrosine/chemistry ; src-Family Kinases/metabolism
    Chemical Substances Antineoplastic Agents ; Drug Combinations ; Laminin ; Paxillin ; Proteoglycans ; matrigel (119978-18-6) ; Tyrosine (42HK56048U) ; Collagen (9007-34-5) ; PEAK1 protein, human (EC 2.7.10.1) ; Protein-Tyrosine Kinases (EC 2.7.10.1) ; src-Family Kinases (EC 2.7.10.2)
    Language English
    Publishing date 2012-10-26
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.M112.410910
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Uc I Zs.108: Show issues Location:
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  4. Article ; Online: KRas induces a Src/PEAK1/ErbB2 kinase amplification loop that drives metastatic growth and therapy resistance in pancreatic cancer.

    Kelber, Jonathan A / Reno, Theresa / Kaushal, Sharmeela / Metildi, Cristina / Wright, Tracy / Stoletov, Konstantin / Weems, Jessica M / Park, Frederick D / Mose, Evangeline / Wang, Yingchun / Hoffman, Robert M / Lowy, Andrew M / Bouvet, Michael / Klemke, Richard L

    Cancer research

    2012  Volume 72, Issue 10, Page(s) 2554–2564

    Abstract: Early biomarkers and effective therapeutic strategies are desperately needed to treat pancreatic ductal adenocarcinoma (PDAC), which has a dismal 5-year patient survival rate. Here, we report that the novel tyrosine kinase PEAK1 is upregulated in human ... ...

    Abstract Early biomarkers and effective therapeutic strategies are desperately needed to treat pancreatic ductal adenocarcinoma (PDAC), which has a dismal 5-year patient survival rate. Here, we report that the novel tyrosine kinase PEAK1 is upregulated in human malignancies, including human PDACs and pancreatic intraepithelial neoplasia (PanIN). Oncogenic KRas induced a PEAK1-dependent kinase amplification loop between Src, PEAK1, and ErbB2 to drive PDAC tumor growth and metastasis in vivo. Surprisingly, blockade of ErbB2 expression increased Src-dependent PEAK1 expression, PEAK1-dependent Src activation, and tumor growth in vivo, suggesting a mechanism for the observed resistance of patients with PDACs to therapeutic intervention. Importantly, PEAK1 inactivation sensitized PDAC cells to trastuzumab and gemcitabine therapy. Our findings, therefore, suggest that PEAK1 is a novel biomarker, critical signaling hub, and new therapeutic target in PDACs.
    MeSH term(s) Animals ; Biomarkers, Tumor/analysis ; Carcinoma, Pancreatic Ductal/genetics ; Cell Line, Tumor ; Drug Resistance, Neoplasm ; Genes, erbB-2 ; Genes, ras ; Humans ; Mice ; Mice, Transgenic ; Models, Molecular ; Neoplasm Metastasis/genetics ; Neoplasm Transplantation ; Oncogene Protein pp60(v-src)/genetics ; Pancreatic Neoplasms/genetics ; Protein-Tyrosine Kinases/genetics ; Signal Transduction/genetics ; Transcriptional Activation ; Up-Regulation
    Chemical Substances Biomarkers, Tumor ; SRC protein, Rous sarcoma virus (147416-06-6) ; PEAK1 protein, human (EC 2.7.10.1) ; Protein-Tyrosine Kinases (EC 2.7.10.1) ; Oncogene Protein pp60(v-src) (EC 2.7.10.2)
    Language English
    Publishing date 2012-05-15
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 1432-1
    ISSN 1538-7445 ; 0008-5472
    ISSN (online) 1538-7445
    ISSN 0008-5472
    DOI 10.1158/0008-5472.CAN-11-3552
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Uh III Zs.135/5: Show issues Location:
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  5. Article ; Online: Reversed-phase chromatography with multiple fraction concatenation strategy for proteome profiling of human MCF10A cells.

    Wang, Yuexi / Yang, Feng / Gritsenko, Marina A / Wang, Yingchun / Clauss, Therese / Liu, Tao / Shen, Yufeng / Monroe, Matthew E / Lopez-Ferrer, Daniel / Reno, Theresa / Moore, Ronald J / Klemke, Richard L / Camp, David G / Smith, Richard D

    Proteomics

    2011  Volume 11, Issue 10, Page(s) 2019–2026

    Abstract: In this study, we evaluated a concatenated low pH (pH 3) and high pH (pH 10) reversed-phase liquid chromatography strategy as a first dimension for two-dimensional liquid chromatography tandem mass spectrometry ("shotgun") proteomic analysis of trypsin- ... ...

    Abstract In this study, we evaluated a concatenated low pH (pH 3) and high pH (pH 10) reversed-phase liquid chromatography strategy as a first dimension for two-dimensional liquid chromatography tandem mass spectrometry ("shotgun") proteomic analysis of trypsin-digested human MCF10A cell sample. Compared with the more traditional strong cation exchange method, the use of concatenated high pH reversed-phase liquid chromatography as a first-dimension fractionation strategy resulted in 1.8- and 1.6-fold increases in the number of peptide and protein identifications (with two or more unique peptides), respectively. In addition to broader identifications, advantages of the concatenated high pH fractionation approach include improved protein sequence coverage, simplified sample processing, and reduced sample losses. The results demonstrate that the concatenated high pH reversed-phased strategy is an attractive alternative to strong cation exchange for two-dimensional shotgun proteomic analysis.
    MeSH term(s) Acetonitriles/chemistry ; Breast/chemistry ; Breast/cytology ; Breast/metabolism ; Cell Line ; Chromatography, Reverse-Phase/methods ; Cluster Analysis ; Epithelial Cells/chemistry ; Epithelial Cells/cytology ; Epithelial Cells/metabolism ; Formates/chemistry ; Humans ; Hydrogen-Ion Concentration ; Peptide Fragments/chemistry ; Peptide Fragments/isolation & purification ; Peptide Fragments/metabolism ; Peptide Mapping/methods ; Proteome/chemistry ; Proteome/metabolism ; Proteomics/methods ; Tandem Mass Spectrometry/methods ; Trypsin/metabolism ; Urea/chemistry
    Chemical Substances Acetonitriles ; Formates ; Peptide Fragments ; Proteome ; formic acid (0YIW783RG1) ; Urea (8W8T17847W) ; Trypsin (EC 3.4.21.4) ; acetonitrile (Z072SB282N)
    Language English
    Publishing date 2011-04-18
    Publishing country Germany
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 2032093-0
    ISSN 1615-9861 ; 1615-9853
    ISSN (online) 1615-9861
    ISSN 1615-9853
    DOI 10.1002/pmic.201000722
    Database MEDical Literature Analysis and Retrieval System OnLINE

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