<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>133(3)</volume><submitter>Zhao Z</submitter><pubmed_abstract>Secreted platelet protein disulfide isomerases, PDI, ERp57, ERp5, and ERp72, have important roles as positive regulators of platelet function and thrombosis. Thioredoxin-related transmembrane protein 1 (TMX1) was the first described transmembrane member of the protein disulfide isomerase family of enzymes. Using a specific antibody, the recombinant extracellular domain of TMX1 (rTMX1) protein, a knockout mouse model, and a thiol-labeling approach, we examined the role of TMX1 in platelet function and thrombosis. Expression of TMX1 on the platelet surface increased with thrombin stimulation. The anti-TMX1 antibody increased platelet aggregation induced by convulxin and thrombin, as well as potentiated platelet ATP release. In contrast, rTMX1 inhibited platelet aggregation and ATP release. T</pubmed_abstract><journal>Blood</journal><pagination>246-251</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC6337875</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>The transmembrane protein disulfide isomerase TMX1 negatively regulates platelet responses.</pubmed_title><pmcid>PMC6337875</pmcid><pubmed_authors>Chen F</pubmed_authors><pubmed_authors>Essex DW</pubmed_authors><pubmed_authors>Yang A</pubmed_authors><pubmed_authors>Zhao Z</pubmed_authors><pubmed_authors>Wu Y</pubmed_authors><pubmed_authors>Zhou J</pubmed_authors></additional><is_claimable>false</is_claimable><name>The transmembrane protein disulfide isomerase TMX1 negatively regulates platelet responses.</name><description>Secreted platelet protein disulfide isomerases, PDI, ERp57, ERp5, and ERp72, have important roles as positive regulators of platelet function and thrombosis. Thioredoxin-related transmembrane protein 1 (TMX1) was the first described transmembrane member of the protein disulfide isomerase family of enzymes. Using a specific antibody, the recombinant extracellular domain of TMX1 (rTMX1) protein, a knockout mouse model, and a thiol-labeling approach, we examined the role of TMX1 in platelet function and thrombosis. Expression of TMX1 on the platelet surface increased with thrombin stimulation. The anti-TMX1 antibody increased platelet aggregation induced by convulxin and thrombin, as well as potentiated platelet ATP release. In contrast, rTMX1 inhibited platelet aggregation and ATP release. T</description><dates><release>2019-01-01T00:00:00Z</release><publication>2019 Jan</publication><modification>2025-04-21T15:08:39.82Z</modification><creation>2025-04-21T15:08:39.82Z</creation></dates><accession>S-EPMC6337875</accession><cross_references><pubmed>30425049</pubmed><doi>10.1182/blood-2018-04-844480</doi></cross_references></HashMap>