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  • 1
    Keywords: CANCER ; CELLS ; EXPRESSION ; INVASION ; tumor ; TUMOR-CELLS ; CELL ; Germany ; human ; IN-VIVO ; VIVO ; SITE ; SITES ; PROTEIN ; cell line ; MOLECULES ; TUMORS ; PATIENT ; CONTRAST ; PHOSPHORYLATION ; treatment ; MOLECULE ; MOUSE ; NO ; STAGE ; TUMOR PROGRESSION ; METASTASIS ; REQUIRES ; NUDE-MICE ; CELL-LINE ; LINE ; MELANOMA ; EXTRACELLULAR-MATRIX ; ADHESION ; MAMMALIAN-CELLS ; MIGRATION ; INTEGRIN ALPHA(V)BETA(3) ; MALIGNANT-MELANOMA ; malignant melanoma ; DIFFERENTIAL EXPRESSION ; TUMOR CELLS ; MATRIX ; ONCOLOGY ; CAPACITY ; INCREASE ; extracellular matrix ; MELANOMA-CELLS ; analysis ; TUMOR-CELL ; USA ; function ; MEDIATED ADHESION ; correlation ; in vivo ; correlates ; 3-DIMENSIONAL COLLAGEN LATTICES ; L-plastin ; MATRIX METALLOPROTEINASE-2 MMP-2
    Abstract: The leukocyte specific actin-binding protein L-plastin is aberrantly expressed in several nonhematopoetic malignant tumors. However, little is known about the functional consequences of L-plastin expression. Here, we investigated the function of L-plastin in human malignant melanoma cells. Knock-down of endogenous L-plastin by siRNA treatment reduced migration of the melanoma cell line IF6. However, in melanoma patients, no correlation existed between L-plastin expression and tumor stages. This implied that additional factors such as phosphorylation of L-plastin may influence its function in tumor cells. To investigate this further, EGFP-tagged wild-type L-plastin (wt-LPL-EGFP) and a mutated, nonphosphorylatable L-plastin protein (5A7A-LPL-EGFP), were expressed in the L-plastin negative melanoma cell line MV3. Biochemical analysis revealed that wt-LPL-EGFP is phosphorylated in MV3 cells while 5A7A-LPL-EGFP is not. Although both wt-LPL-EGFP and 5A7A-LPL-EGFP were targeted to, and promote the formation of, vinculin-containing adhesion sites, static adhesion to either Matrigel or isolated extracellular matrix molecules was neither influenced by expression of wt-LPL-EGFP nor by expression of 5A7A-LPL-EGFP when compared with EGFP expressing control cells. In contrast, haptotactic, but not chemotactic, migration of melanoma cells towards either Matrigel or isolated extracellular matrix molecules was similarly enhanced, if either 5A7A-LPL-EGFP or wt-LPL-EGFP were expressed in MV3 cells. Interestingly, only cells expressing the phosphorylatable wt-LPL-EGFP protein showed enhanced invasion into Matrigel. In line with these findings the in vivo metastatic capacity of mouse B16 melanoma cells correlates with expression and phosphorylation of L-plastin. These data show that an increase in melanoma cell invasiveness requires not only expression but also phosphorylation of L-plastin. (c) 2007 Wiley-Liss, Inc
    Type of Publication: Journal article published
    PubMed ID: 17290393
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  • 2
    Keywords: CELLS ; PROTEIN ; MOLECULES ; ACTIVATION ; COMPLEX ; T cells ; BINDING ; PHOSPHORYLATION ; ADHESION ; ACTIN CYTOSKELETON ; IMMUNOLOGICAL SYNAPSE ; HUMAN NEUTROPHILS ; T-CELL-ACTIVATION ; INCREASES ; FIMBRIN
    Abstract: Formation of immune synapses (IS) between T cells and APC requires multiple rearrangements in the actin cytoskeleton and selective receptor accumulation in supramolecular activation clusters (SMAC). The inner cluster (central SMAC) contains the TCR/CD3 complex. The outer cluster (peripheral SMAC) contains the integrin LFA-1 and Talin. Molecular mechanisms selectively stabilizing receptors in the IS remained largely unknown. Here, we demonstrate that sustained LFA-1 clustering in the IS is a consequence of the combined activities of the actin-bundling protein L-plastin (LPL) and calmodulin. Thus, upon antigen-recognition of T cells, LPL accumulated predominantly in the peripheral SMAC. siRNA-mediated knock-down of LPL led to a failure of LFA-1 and Talin redistribution - however, not TCR/CD3 relocalization - into the IS. As a result of this LPL knock-down, the T-cell/APC interface became smaller over time and T-cell proliferation was inhibited. Importantly, binding of calmodulin to LPL was required for the maintenance of LPL in the IS and consequently inhibition of calmodulin also prevented stable accumulation of LFA-1 and Talin, but not CD3, in the IS
    Type of Publication: Journal article published
    PubMed ID: 20683899
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