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  1. Article: Pias1 is essential for erythroid and vascular development in the mouse embryo

    Constanzo, Jerfiz D / Mi Deng / Smita Rindhe / Ke-jing Tang / Cheng-cheng Zhang / Pier Paolo Scaglioni

    Developmental biology. 2016 July 01, v. 415

    2016  

    Abstract: The protein inhibitor of activated STAT-1 (PIAS1) is one of the few known SUMO E3 ligases. PIAS1 has been implicated in several biological processes including repression of innate immunity and DNA repair. However, PIAS1 function during development and ... ...

    Abstract The protein inhibitor of activated STAT-1 (PIAS1) is one of the few known SUMO E3 ligases. PIAS1 has been implicated in several biological processes including repression of innate immunity and DNA repair. However, PIAS1 function during development and tissue differentiation has not been studied. Here, we report that Pias1 is required for proper embryonic development. Approximately 90% of Pias1 null embryos die in utero between E10.5 and E12.5. We found significant apoptosis within the yolk sac (YS) blood vessels and concomitant loss of red blood cells (RBCs) resulting in profound anemia. In addition, Pias1 loss impairs YS angiogenesis and results in defective capillary plexus formation and blood vessel occlusions. Moreover, heart development is impaired as a result of loss of myocardium muscle mass. Accordingly, we found that Pias1 expression in primary myoblasts enhances the induction of cardiac muscle genes MyoD, Myogenin and Myomaker. PIAS1 protein regulation of cardiac gene transcription is dependent on transcription factors Myocardin and Gata-4. Finally, endothelial cell specific inactivation of Pias1 in vivo impairs YS erythrogenesis, angiogenesis and recapitulates loss of myocardium muscle mass. However, these defects are not sufficient to recapitulate the lethal phenotype of Pias1 null embryos. These findings highlight Pias1 as an essential gene for YS erythropoiesis and vasculogenesis in vivo.
    Keywords DNA repair ; GATA transcription factors ; anemia ; angiogenesis ; apoptosis ; blood vessels ; embryogenesis ; endothelial cells ; erythrocytes ; erythropoiesis ; genes ; innate immunity ; ligases ; mice ; muscles ; myoblasts ; myocardium ; phenotype ; transcription (genetics) ; yolk sac
    Language English
    Dates of publication 2016-0701
    Size p. 98-110.
    Publishing place Elsevier Inc.
    Document type Article
    ZDB-ID 1114-9
    ISSN 1095-564X ; 0012-1606
    ISSN (online) 1095-564X
    ISSN 0012-1606
    DOI 10.1016/j.ydbio.2016.04.013
    Database NAL-Catalogue (AGRICOLA)

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    In stock of ZB MED Bonn / Germany

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  2. Article ; Online: PIAS1-FAK Interaction Promotes the Survival and Progression of Non-Small Cell Lung Cancer

    Jerfiz D. Constanzo / Ke-jing Tang / Smita Rindhe / Margherita Melegari / Hui Liu / Ximing Tang / Jaime Rodriguez-Canales / Ignacio Wistuba / Pier Paolo Scaglioni

    Neoplasia : An International Journal for Oncology Research, Vol 18, Iss 5, Pp 282-

    2016  Volume 293

    Abstract: The sequence of genomic alterations acquired by cancer cells during tumor progression and metastasis is poorly understood. Focal adhesion kinase (FAK) is a non-receptor tyrosine kinase that integrates cytoskeleton remodeling, mitogenic signaling and cell ...

    Abstract The sequence of genomic alterations acquired by cancer cells during tumor progression and metastasis is poorly understood. Focal adhesion kinase (FAK) is a non-receptor tyrosine kinase that integrates cytoskeleton remodeling, mitogenic signaling and cell survival. FAK has previously been reported to undergo nuclear localization during cell migration, cell differentiation and apoptosis. However, the mechanism behind FAK nuclear accumulation and its contribution to tumor progression has remained elusive. We report that amplification of FAK and the SUMO E3 ligase PIAS1 gene loci frequently co-occur in non-small cell lung cancer (NSCLC) cells, and that both gene products are enriched in a subset of primary NSCLCs. We demonstrate that endogenous FAK and PIAS1 proteins interact in the cytoplasm and the cell nucleus of NSCLC cells. Ectopic expression of PIAS1 promotes proteolytic cleavage of the FAK C-terminus, focal adhesion maturation and FAK nuclear localization. Silencing of PIAS1 deregulates focal adhesion turnover, increases susceptibility to apoptosis in vitro and impairs tumor xenograft formation in vivo. Nuclear FAK in turn stimulates gene transcription favoring DNA repair, cell metabolism and cytoskeleton regulation. Consistently, ablation of FAK by CRISPR/Cas9 editing, results in basal DNA damage, susceptibility to ionizing radiation and impaired oxidative phosphorylation. Our findings provide insight into a mechanism regulating FAK cytoplasm-nuclear distribution and demonstrate that FAK activity in the nucleus promotes NSCLC survival and progression by increasing cell-ECM interaction and DNA repair regulation.
    Keywords Medicine ; R ; Internal medicine ; RC31-1245 ; Neoplasms. Tumors. Oncology. Including cancer and carcinogens ; RC254-282
    Subject code 570
    Publishing date 2016-05-01T00:00:00Z
    Publisher Elsevier
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  3. Article ; Online: Corrigendum to “PIAS1-FAK Interaction Promotes the Survival and Progression of Non–Small Cell Lung Cancer” [Neoplasia 18 (2016) 282-293].

    Jerfiz D. Constanzo / Ke-jing Tang / Smita Rindhe / Margherita Melegari / Hui Liu / Ximing Tang / Jaime Rodriguez-Canales / Ignacio Wistuba / Pier Paolo Scaglioni

    Neoplasia: An International Journal for Oncology Research, Vol 18, Iss 7, p

    2016  Volume 457

    Keywords Medicine ; R ; Internal medicine ; RC31-1245 ; Neoplasms. Tumors. Oncology. Including cancer and carcinogens ; RC254-282
    Language English
    Publishing date 2016-07-01T00:00:00Z
    Publisher Elsevier
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  4. Article ; Online: Fatty Acid Oxidation Mediated by Acyl-CoA Synthetase Long Chain 3 Is Required for Mutant KRAS Lung Tumorigenesis

    Mahesh S. Padanad / Georgia Konstantinidou / Niranjan Venkateswaran / Margherita Melegari / Smita Rindhe / Matthew Mitsche / Chendong Yang / Kimberly Batten / Kenneth E. Huffman / Jingwen Liu / Ximing Tang / Jaime Rodriguez-Canales / Neda Kalhor / Jerry W. Shay / John D. Minna / Jeffrey McDonald / Ignacio I. Wistuba / Ralph J. DeBerardinis / Pier Paolo Scaglioni

    Cell Reports, Vol 16, Iss 6, Pp 1614-

    2016  Volume 1628

    Abstract: KRAS is one of the most commonly mutated oncogenes in human cancer. Mutant KRAS aberrantly regulates metabolic networks. However, the contribution of cellular metabolism to mutant KRAS tumorigenesis is not completely understood. We report that mutant ... ...

    Abstract KRAS is one of the most commonly mutated oncogenes in human cancer. Mutant KRAS aberrantly regulates metabolic networks. However, the contribution of cellular metabolism to mutant KRAS tumorigenesis is not completely understood. We report that mutant KRAS regulates intracellular fatty acid metabolism through Acyl-coenzyme A (CoA) synthetase long-chain family member 3 (ACSL3), which converts fatty acids into fatty Acyl-CoA esters, the substrates for lipid synthesis and β-oxidation. ACSL3 suppression is associated with depletion of cellular ATP and causes the death of lung cancer cells. Furthermore, mutant KRAS promotes the cellular uptake, retention, accumulation, and β-oxidation of fatty acids in lung cancer cells in an ACSL3-dependent manner. Finally, ACSL3 is essential for mutant KRAS lung cancer tumorigenesis in vivo and is highly expressed in human lung cancer. Our data demonstrate that mutant KRAS reprograms lipid homeostasis, establishing a metabolic requirement that could be exploited for therapeutic gain.
    Keywords ACSL3 ; mutant KRAS ; lung cancer ; cancer metabolism ; fatty acid oxidation ; lipid metabolism ; mouse cancer models ; Biology (General) ; QH301-705.5
    Language English
    Publishing date 2016-08-01T00:00:00Z
    Publisher Elsevier
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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