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  1. Article ; Online: Protein interacting with C kinase 1 suppresses invasion and anchorage-independent growth of astrocytic tumor cells.

    Cockbill, Louisa M R / Murk, Kai / Love, Seth / Hanley, Jonathan G

    Molecular biology of the cell

    2015  Volume 26, Issue 25, Page(s) 4552–4561

    Abstract: Astrocytic tumors are the most common form of primary brain tumor. Astrocytic tumor cells infiltrate the surrounding CNS tissue, allowing them to evade removal upon surgical resection of the primary tumor. Dynamic changes to the actin cytoskeleton are ... ...

    Abstract Astrocytic tumors are the most common form of primary brain tumor. Astrocytic tumor cells infiltrate the surrounding CNS tissue, allowing them to evade removal upon surgical resection of the primary tumor. Dynamic changes to the actin cytoskeleton are crucial to cancer cell invasion, but the specific mechanisms that underlie the particularly invasive phenotype of astrocytic tumor cells are unclear. Protein interacting with C kinase 1 (PICK1) is a PDZ and BAR domain-containing protein that inhibits actin-related protein 2/3 (Arp2/3)-dependent actin polymerization and is involved in regulating the trafficking of a number of cell-surface receptors. Here we report that, in contrast to other cancers, PICK1 expression is down-regulated in grade IV astrocytic tumor cell lines and also in clinical cases of the disease in which grade IV tumors have progressed from lower-grade tumors. Exogenous expression of PICK1 in the grade IV astrocytic cell line U251 reduces their capacity for anchorage-independent growth, two-dimensional migration, and invasion through a three-dimensional matrix, strongly suggesting that low PICK1 expression plays an important role in astrocytic tumorigenesis. We propose that PICK1 negatively regulates neoplastic infiltration of astrocytic tumors and that manipulation of PICK1 is an attractive possibility for therapeutic intervention.
    MeSH term(s) Actin Cytoskeleton/genetics ; Actin-Related Protein 2-3 Complex/genetics ; Astrocytes/metabolism ; Astrocytes/pathology ; Astrocytoma/genetics ; Astrocytoma/pathology ; Brain Neoplasms/genetics ; Brain Neoplasms/pathology ; Carrier Proteins/biosynthesis ; Carrier Proteins/genetics ; Cell Line, Tumor ; Cell Movement ; Cell Proliferation ; Female ; Gene Expression Regulation, Neoplastic ; Humans ; Male ; Neoplasm Invasiveness ; Nuclear Proteins/biosynthesis ; Nuclear Proteins/genetics
    Chemical Substances Actin-Related Protein 2-3 Complex ; Carrier Proteins ; Nuclear Proteins ; PICk1 protein, human
    Language English
    Publishing date 2015-10-14
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1098979-1
    ISSN 1939-4586 ; 1059-1524
    ISSN (online) 1939-4586
    ISSN 1059-1524
    DOI 10.1091/mbc.E15-05-0270
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 2853: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)
    Zs.MO 410: Show issues

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  2. Article ; Online: The antagonistic modulation of Arp2/3 activity by N-WASP, WAVE2 and PICK1 defines dynamic changes in astrocyte morphology.

    Murk, Kai / Blanco Suarez, Elena M / Cockbill, Louisa M R / Banks, Paul / Hanley, Jonathan G

    Journal of cell science

    2013  Volume 126, Issue Pt 17, Page(s) 3873–3883

    Abstract: Astrocytes exhibit a complex, branched morphology, allowing them to functionally interact with numerous blood vessels, neighboring glial processes and neuronal elements, including synapses. They also respond to central nervous system (CNS) injury by a ... ...

    Abstract Astrocytes exhibit a complex, branched morphology, allowing them to functionally interact with numerous blood vessels, neighboring glial processes and neuronal elements, including synapses. They also respond to central nervous system (CNS) injury by a process known as astrogliosis, which involves morphological changes, including cell body hypertrophy and thickening of major processes. Following severe injury, astrocytes exhibit drastically reduced morphological complexity and collectively form a glial scar. The mechanistic details behind these morphological changes are unknown. Here, we investigate the regulation of the actin-nucleating Arp2/3 complex in controlling dynamic changes in astrocyte morphology. In contrast to other cell types, Arp2/3 inhibition drives the rapid expansion of astrocyte cell bodies and major processes. This intervention results in a reduced morphological complexity of astrocytes in both dissociated culture and in brain slices. We show that this expansion requires functional myosin II downstream of ROCK and RhoA. Knockdown of the Arp2/3 subunit Arp3 or the Arp2/3 activator N-WASP by siRNA also results in cell body expansion and reduced morphological complexity, whereas depleting WAVE2 specifically reduces the branching complexity of astrocyte processes. By contrast, knockdown of the Arp2/3 inhibitor PICK1 increases astrocyte branching complexity. Furthermore, astrocyte expansion induced by ischemic conditions is delayed by PICK1 knockdown or N-WASP overexpression. Our findings identify a new morphological outcome for Arp2/3 activation in restricting rather than promoting outwards movement of the plasma membrane in astrocytes. The Arp2/3 regulators PICK1, and N-WASP and WAVE2 function antagonistically to control the complexity of astrocyte branched morphology, and this mechanism underlies the morphological changes seen in astrocytes during their response to pathological insult.
    MeSH term(s) Actin-Related Protein 2-3 Complex/genetics ; Actin-Related Protein 2-3 Complex/metabolism ; Amides/pharmacology ; Animals ; Astrocytes/cytology ; Astrocytes/drug effects ; Astrocytes/metabolism ; Carrier Proteins/genetics ; Carrier Proteins/metabolism ; Cells, Cultured ; Central Nervous System/metabolism ; Colforsin/pharmacology ; Enzyme Inhibitors/pharmacology ; Fibroblasts ; HEK293 Cells ; Heterocyclic Compounds, 4 or More Rings/pharmacology ; Humans ; Mice ; Myosin Type II/antagonists & inhibitors ; Myosin Type II/metabolism ; Nuclear Proteins/genetics ; Nuclear Proteins/metabolism ; Pyridines/pharmacology ; RNA Interference ; RNA, Small Interfering ; Rats ; Thiazoles/pharmacology ; Thiones/pharmacology ; Uracil/analogs & derivatives ; Uracil/pharmacology ; Vasodilator Agents/pharmacology ; Wiskott-Aldrich Syndrome Protein, Neuronal/genetics ; Wiskott-Aldrich Syndrome Protein, Neuronal/metabolism ; rhoA GTP-Binding Protein/antagonists & inhibitors ; rhoA GTP-Binding Protein/metabolism
    Chemical Substances Actin-Related Protein 2-3 Complex ; Amides ; CK-0993548 ; Carrier Proteins ; Enzyme Inhibitors ; Heterocyclic Compounds, 4 or More Rings ; Nuclear Proteins ; PICk1 protein, human ; Pyridines ; RNA, Small Interfering ; SMIFH2 compound ; Thiazoles ; Thiones ; Vasodilator Agents ; Wiskott-Aldrich Syndrome Protein, Neuronal ; Y 27632 (138381-45-0) ; Colforsin (1F7A44V6OU) ; blebbistatin (20WC4J7CQ6) ; Uracil (56HH86ZVCT) ; Myosin Type II (EC 3.6.1.-) ; rhoA GTP-Binding Protein (EC 3.6.5.2)
    Language English
    Publishing date 2013-07-10
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2993-2
    ISSN 1477-9137 ; 0021-9533
    ISSN (online) 1477-9137
    ISSN 0021-9533
    DOI 10.1242/jcs.125146
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1200: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)
    Zs.MG 14: Show issues

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