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TranscriptomicsTranscriptional response of ovarian cancer cell lines to HGF and CDDP
HGF sensitizes ovarian cancer cells to chemotherapeutics, e.g. cisplatin (CDDP), through a signaling cascade activated by its MET oncogene encoded receptor and transduced by the p38MAPK. This cascade results in the regulation of a common set of transcripts in three ovarian cancer cell lines, with di...
ORGANISM(S): Homo sapiens 
2013-12-31 | E-GEOD-24589 | biostudies-arrayexpress
ProteomicsIncreased Basal MET phosphorylation is a Hallmark of Hepatocyte Dysregulation in Liver Disease: Mouse
Non-alcoholic fatty liver disease (NAFLD) is gaining evermore importance due to rapidly rising incidence rates especially in western countries. As the disease progresses, it can develop into hepatocellular carcinoma. Related metabolic changes have been extensively studied in the past. However, the m...
ORGANISM(S): Mus musculus (Mouse) 
2024-01-15 | PXD041563 | Pride
Western diet  dynamic pathway modeling  hepatocyte dysregulation  fatty liver disease  hgf signal transduction 
ProteomicsIdentification of phosphorylation sites regulated by lysophosphatidic acid (LPA) in OCMI91s ovarian cancer cells
Elevated levels of lysophosphatidic acid (LPA) species accumulate in the ascites of ovarian high grade serous cancer (HGSC) and are associated with a short relapse-free survival. LPA is known to support the metastatic spread of cancer cells by activating a multitude of signaling pathways through G-p...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2023-01-25 | MSV000091146 | MassIVE
ProteomicsIdentification of phosphorylation sites regulated by lysophosphatidic acid (LPA) in OVCAR8 ovarian cancer cells
Elevated levels of lysophosphatidic acid (LPA) species accumulate in the ascites of ovarian high grade serous cancer (HGSC) and are associated with a short relapse-free survival. LPA is known to support the metastatic spread of cancer cells by activating a multitude of signaling pathways through G-p...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2023-01-26 | MSV000091158 | MassIVE
TranscriptomicsExpression data from MDCK cells exposed to HGF +/- MAPK inhibitors
Gene expression in Madin Darby canine kidney cells grown for 7 days to confluence on Transwell filters and exposed to HGF +/- inhibitors of the MAPK pathway (MAPK is one of the pathways activated when HGF binds to the CMET receptor tyrosine kinase). We used microarrays to detail the program of gene ...
ORGANISM(S): Canis lupus familiaris 
2010-05-25 | E-GEOD-9435 | biostudies-arrayexpress
UnknownMet-HGF/SF signal transduction induces mimp, a novel mitochondrial carrier homologue, which leads to mitochondrial depolarization.
Not available
S-EPMC1503665 | biostudies-literature
Models,MultiomicsHGF Signaling in Keratinocytes
Cell migration is a complex process that is controlled through the time-sequential feedback regulation of protein signalling and gene regulation. Based on prior knowledge and own experimental data, we developed a large-scale dynamic network describing the onset and maintenance of hepatocyte growth f...
1969 | Cell Collective
TranscriptomicsTime-series of IL-6 stimulated primary mouse hepatocytes
External stimulations of cells by hormones, growth factors or cytokines activate signal transduction pathways that subsequently induce a rearrangement of cellular gene expression. The representation and analysis of changes in the gene response is complicated, and essentially consists of multiple lay...
ORGANISM(S): Mus musculus 
2010-04-07 | E-GEOD-21031 | biostudies-arrayexpress
UnknownT160‐phosphorylated CDK2 defines threshold for HGF dependent proliferation in primary hepatocytes.
Not available
S-EPMC4380929 | biostudies-literature
TranscriptomicsArginine utilization following mycobacteria infection in macrophages is dependent on autocrine-paracrine signaling
Nitric oxide (NO) produced by macrophages (MØs) is toxic to both host tissues and invading pathogens and its regulation is therefore essential to suppress host cytotoxicity. MØ arginase 1 (Arg1) inhibits NO production by competing with NO synthases for arginine, the common substrate of NO synthases ...
ORGANISM(S): Mus musculus 
2010-07-14 | E-GEOD-22935 | biostudies-arrayexpress
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