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  • 1
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    German Medical Science; Düsseldorf, Köln
    In:  56. Jahrestagung der Deutschen Gesellschaft für Neurochirurgie e.V. (DGNC), 3èmes journées françaises de Neurochirurgie (SFNC); 20050507-20050511; Strasbourg; DOCP177 /20050504/
    Publication Date: 2005-05-05
    Keywords: ddc: 610
    Language: English
    Type: conferenceObject
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  • 2
    Keywords: brain ; CANCER ; CELLS ; ENDOTHELIAL-CELLS ; EXPRESSION ; tumor ; AGENTS ; Germany ; human ; MICROSCOPY ; neoplasms ; GENE ; GENES ; PROTEIN ; PROTEINS ; DRUG ; TUMORS ; FAMILY ; CELL-LINES ; MEMBERS ; TRANSPORT ; resistance ; MEMBRANE ; PCR ; DELIVERY ; LOCALIZATION ; PHENOTYPE ; MULTIDRUG-RESISTANCE ; GLIOMAS ; chemoresistance ; multidrug resistance ; SUBCELLULAR-LOCALIZATION ; AGENT ; ONCOLOGY ; RE ; BRAIN-TUMORS ; GLIOMA ; endothelial cells ; P-GLYCOPROTEIN ; TRANSPORTER ; SUBTYPE ; BASOLATERAL HEPATOCYTE MEMBRANE ; MRP4 CONFERS RESISTANCE ; LEVEL ; SUBTYPES ; EFFLUX PUMPS ; immunofluorescence ; membrane transport proteins ; MICROVESSEL ENDOTHELIUM ; multidrug resistance protein ; MULTIDRUG-RESISTANCE PROTEINS ; oligoastrocytoma ; oligodendroglioma ; RAT ASTROCYTES ; SUBFAMILY
    Abstract: Delivery of therapeutic agents to the brain and its neoplasms depends on the presence of membrane transport proteins in the blood-brain barrier and in the target cells. The cellular and subcellular localization of these membrane transporters determines the drug accessibility to the brain and its tumors. We therefore analyzed the expression and localization of six members of the multidrug resistance protein family of ATP-dependent efflux pumps (ABCCI-ABCC6, formerly MRPI-MRP6) and of six organic anion uptake transporters (OATPIA2, OATP1B1, OATP1B3, OATP1C1, OAT2B1, and OATP4A1) in 61 human glioma specimens of different histologic subtypes. Real-thine PCRs indicated expressions of ABCO, ABCC3, ABCC4, and ABCC5. In addition, we detected expressions of the OATP uptake transporter genes SLCOIA2, SWO1C1, SLCO2B1, and SLC04A1. At. the protein level, however, only OATPIA2 and OATP2B1 were detectable by immunofluorescence microscopy in the luminal membrane of endothelial cells forming the blood-brain barrier and the blood-tumor barrier, but not in the glioma cells. ABCC4 and ABCC5 proteins were the major ABCC subfamily members in gliomas, localized both at the luminal side of the endothetial cells and in the glioma cells of astrocytic tumors and in the astrocytic portions of oligoastrocytomas. These results indicate that expression of ABCC4 and ABCC5 is associated with an astrocytic phenotype, in accordance with their expression in astrocytes and with the higher chemoresistance of astrocytic tumors as compared with oligodendrogliomas. Our data provide a basis for the assessment of the role of uptake transporters and efflux pumps in the accessibility of human gliomas for chemotherapeutic agents
    Type of Publication: Journal article published
    PubMed ID: 16357150
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  • 3
    Keywords: ENDOTHELIAL-CELLS ; EXPRESSION ; KINASE ; C-JUN ; MICROARRAY ANALYSIS ; E-cadherin ; PLASMINOGEN-ACTIVATOR INHIBITOR-1 ; p38 MAPK ; PHASE PROTEIN ARRAYS ; UROKINASE-TYPE
    Abstract: The supporting role of urokinase-type plasminogen activator (uPA) and its inhibitor plasminogen activator inhibitor 1 (PAI-1) in migration and invasion is well known. In addition, both factors are key components in cancer cell-related signaling. However, little information is available for uPA and PAI-1-associated signaling pathways in primary cancers and corresponding lymph node metastases. The aim of this study was to compare the expression of uPA and PAI-1-associated signaling proteins in 52 primary breast cancers and corresponding metastases. Proteins were extracted from formalin-fixed paraffin-embedded tissue samples of the primary tumors and metastases. Protein lysates were subsequently analyzed by reverse phase protein array for the expression of members of the PI3K/AKT (FAK, GSK3-beta, ILK, pGSK3-beta, PI3K, and ROCK) and the MAPK pathways (pp38, pSTAT3, and p38). A solid correlation of uPA expression existed between primary tumors and metastases, whereas PAI-1 expression did not significantly correlate between them. The correlations of uPA and PAI-1 with signaling pathways found in primary tumors did not persist in metastases. Analysis of single molecules revealed that some correlated well between tumors and metastases (FAK, pGSK3-beta, ILK, Met, PI3K, ROCK, uPA, p38, and pp38), whereas others did not (PAI-1 and GSK3-beta). Whether the expression of a protein correlated between tumor and metastasis or not was independent of the pathway the protein is related to. These findings hint at a complete deregulation of uPA and PAI-1-related signaling in metastases, which might be the reason why uPA and PAI-1 reached clinical relevance only for lymph node-negative breast cancer tissues.
    Type of Publication: Journal article published
    PubMed ID: 22496926
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