<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>288(8)</volume><submitter>Pan Q</submitter><pubmed_abstract>We investigated whether a synthetic tetrameric branched peptide based on the conserved TFLK motif from mammary-associated serum amyloid A3 (M-SAA3) is more efficient than the monomeric peptide at up-regulating MUC3 expression and examined the possible mechanism(s) and biological significance of this process. We used standard solid-phase methods to synthesize a tetrameric branched peptide (sequence GWLTFLKAAG) containing a trilysine core, termed the TFLK-containing 10-mer BP. The aberrant expression of transcription factors was analyzed using a transcription factor protein/DNA array. MUC3 and relevant transcription factors were detected using real-time PCR and/or Western blots. The luciferase assay, EMSA, and ChIP assays were used to analyze the activity of the human MUC3 promoter. The bact</pubmed_abstract><journal>The Journal of biological chemistry</journal><pagination>5407-16</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC3581376</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Enhanced membrane-tethered mucin 3 (MUC3) expression by a tetrameric branched peptide with a conserved TFLK motif inhibits bacteria adherence.</pubmed_title><pmcid>PMC3581376</pmcid><pubmed_authors>Chen L</pubmed_authors><pubmed_authors>Peng Z</pubmed_authors><pubmed_authors>Song L</pubmed_authors><pubmed_authors>Li X</pubmed_authors><pubmed_authors>Liu Y</pubmed_authors><pubmed_authors>Yang Y</pubmed_authors><pubmed_authors>He Y</pubmed_authors><pubmed_authors>Wang R</pubmed_authors><pubmed_authors>Tian Y</pubmed_authors><pubmed_authors>Chen W</pubmed_authors><pubmed_authors>Mao X</pubmed_authors><pubmed_authors>Pan Q</pubmed_authors><pubmed_authors>Zhu R</pubmed_authors><pubmed_authors>Ye J</pubmed_authors></additional><is_claimable>false</is_claimable><name>Enhanced membrane-tethered mucin 3 (MUC3) expression by a tetrameric branched peptide with a conserved TFLK motif inhibits bacteria adherence.</name><description>We investigated whether a synthetic tetrameric branched peptide based on the conserved TFLK motif from mammary-associated serum amyloid A3 (M-SAA3) is more efficient than the monomeric peptide at up-regulating MUC3 expression and examined the possible mechanism(s) and biological significance of this process. We used standard solid-phase methods to synthesize a tetrameric branched peptide (sequence GWLTFLKAAG) containing a trilysine core, termed the TFLK-containing 10-mer BP. The aberrant expression of transcription factors was analyzed using a transcription factor protein/DNA array. MUC3 and relevant transcription factors were detected using real-time PCR and/or Western blots. The luciferase assay, EMSA, and ChIP assays were used to analyze the activity of the human MUC3 promoter. The bact</description><dates><release>2013-01-01T00:00:00Z</release><publication>2013 Feb</publication><modification>2025-04-25T21:58:53.296Z</modification><creation>2019-03-27T01:05:13Z</creation></dates><accession>S-EPMC3581376</accession><cross_references><pubmed>23316049</pubmed><doi>10.1074/jbc.M112.408245</doi><doi>10.1074/jbc.m112.408245</doi></cross_references></HashMap>