<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Todorovic V</submitter><funding>NCI NIH HHS</funding><funding>NIAMS NIH HHS</funding><pagination>351-61</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC2830845</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>9(2)</volume><pubmed_abstract>The ability of cells to modulate interactions with each other and the substrate is essential for epithelial tissue remodeling during processes such as wound healing and tumor progression. However, despite strides made in the field of proteomics, proteins involved in adhesion have been difficult to study. Here, we report a method for the enrichment and analysis of proteins associated with the basal surface of the cell and its underlying matrix. The enrichment involves deroofing the cells with 20 mM ammonium hydroxide and the removal of cytosolic and organellar proteins by stringent water wash. Proteomic profiling was achieved by LC-FTMS, which allowed comparison of differentially expressed or shared proteins under different cell states. First, we analyzed and compared the basal cell compone</pubmed_abstract><journal>Molecular &amp; cellular proteomics : MCP</journal><pubmed_title>Detection of differentially expressed basal cell proteins by mass spectrometry.</pubmed_title><pmcid>PMC2830845</pmcid><funding_grant_id>F32 AR055444</funding_grant_id><funding_grant_id>R01 AR041836</funding_grant_id><funding_grant_id>R01 AR43380</funding_grant_id><funding_grant_id>T32 CA070085</funding_grant_id><funding_grant_id>R01 AR043380</funding_grant_id><funding_grant_id>P30 AR057216</funding_grant_id><funding_grant_id>R01 CA122151</funding_grant_id><funding_grant_id>R01 AR41836</funding_grant_id><pubmed_authors>Todorovic V</pubmed_authors><pubmed_authors>Desai BV</pubmed_authors><pubmed_authors>Yin T</pubmed_authors><pubmed_authors>Mrksich M</pubmed_authors><pubmed_authors>Patterson MJ</pubmed_authors><pubmed_authors>Eigenheer RA</pubmed_authors><pubmed_authors>Green KJ</pubmed_authors><pubmed_authors>Amargo EV</pubmed_authors></additional><is_claimable>false</is_claimable><name>Detection of differentially expressed basal cell proteins by mass spectrometry.</name><description>The ability of cells to modulate interactions with each other and the substrate is essential for epithelial tissue remodeling during processes such as wound healing and tumor progression. However, despite strides made in the field of proteomics, proteins involved in adhesion have been difficult to study. Here, we report a method for the enrichment and analysis of proteins associated with the basal surface of the cell and its underlying matrix. The enrichment involves deroofing the cells with 20 mM ammonium hydroxide and the removal of cytosolic and organellar proteins by stringent water wash. Proteomic profiling was achieved by LC-FTMS, which allowed comparison of differentially expressed or shared proteins under different cell states. First, we analyzed and compared the basal cell compone</description><dates><release>2010-01-01T00:00:00Z</release><publication>2010 Feb</publication><modification>2025-04-21T18:43:51.17Z</modification><creation>2019-03-27T00:28:59Z</creation></dates><accession>S-EPMC2830845</accession><cross_references><pubmed>19955077</pubmed><doi>10.1074/mcp.M900358-MCP200</doi><doi>10.1074/mcp.m900358-mcp200</doi></cross_references></HashMap>