<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>12(6)</volume><submitter>Khaghanzadeh N</submitter><pubmed_abstract>Umbelliprenin (Umb), a natural coumarin, has demonstrated anti-tumor activities, both &lt;i>in vitro&lt;/i> and particularly &lt;i>in vivo&lt;/i>, in several types of cancer, including lung cancer. The present study aimed to identify molecular targets of Umb using a high-throughput approach. Lung cancer cell lines, QU-DB (large-cell lung carcinoma) and A549 (adenocarcinoma), were treated with Umb. Differentially-expressed proteins were identified using two-dimensional electrophoresis coupled to mass spectrometry. In the QU-DB cells, differential expression of proteins, including downregulation of the tumorigenic protein heat shock protein 90 kDa and upregulation of the potential anti-tumor proteins Nipsnap1 and glycine-tRNA ligase (GRS), suggested that Umb is a strong anti-tumor compound. In the A549 </pubmed_abstract><journal>Oncology letters</journal><pagination>5295-5302</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC5228441</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Immune-associated proteins with potential &lt;i>in vivo&lt;/i> anti-tumor activities are upregulated in lung cancer cells treated with umbelliprenin: A proteomic approach.</pubmed_title><pmcid>PMC5228441</pmcid><pubmed_authors>Khaghanzadeh N</pubmed_authors><pubmed_authors>Kuramitsu Y</pubmed_authors><pubmed_authors>Ghaderi A</pubmed_authors><pubmed_authors>Mojtahedi Z</pubmed_authors><pubmed_authors>Nakamura K</pubmed_authors></additional><is_claimable>false</is_claimable><name>Immune-associated proteins with potential &lt;i>in vivo&lt;/i> anti-tumor activities are upregulated in lung cancer cells treated with umbelliprenin: A proteomic approach.</name><description>Umbelliprenin (Umb), a natural coumarin, has demonstrated anti-tumor activities, both &lt;i>in vitro&lt;/i> and particularly &lt;i>in vivo&lt;/i>, in several types of cancer, including lung cancer. The present study aimed to identify molecular targets of Umb using a high-throughput approach. Lung cancer cell lines, QU-DB (large-cell lung carcinoma) and A549 (adenocarcinoma), were treated with Umb. Differentially-expressed proteins were identified using two-dimensional electrophoresis coupled to mass spectrometry. In the QU-DB cells, differential expression of proteins, including downregulation of the tumorigenic protein heat shock protein 90 kDa and upregulation of the potential anti-tumor proteins Nipsnap1 and glycine-tRNA ligase (GRS), suggested that Umb is a strong anti-tumor compound. In the A549 </description><dates><release>2016-01-01T00:00:00Z</release><publication>2016 Dec</publication><modification>2025-04-27T00:54:03.859Z</modification><creation>2021-02-20T07:28:28Z</creation></dates><accession>S-EPMC5228441</accession><cross_references><pubmed>28105238</pubmed><doi>10.3892/ol.2016.5352</doi></cross_references></HashMap>