{"id":{"repo_id":"aachen","oai_identifier":"oai:publications.rwth-aachen.de:52599"},"canonical_url":"https://search.dev.ndltd.org/etd/aachen/oai:publications.rwth-aachen.de:52599","repository":{"repo_id":"aachen","name":"RWTH Aachen University","base_url":"https://publications.rwth-aachen.de/oai2d"},"display":{"title":"Moesin in Thrombozyten interagiert mit PECAM-1 : Bedeutung für die Atherosklerose und Restenose","abstract":"Moesin is a member of the Ezrin/Radixin/Moesin (ERM) protein family, which is located in cellular protrusions such as filopoda. Members of this family form a cross-link between the actin cytoskeleton and the plasma membrane. They participate in signal transduction between the extrecellular matrix, the cell surface and the cytoplasma. In this study we investigated whether PECAM-1 (platelet endothelial cell adhesion molecule-1) is a membrane-binding partner for moesin in human platelets. The juxta-membrane cytoplasmic domaine of PECAM-1 contains a cluster of positively charged aminoacid-residues similar to the known consensus-sequences of the ERM protein membrane-binding partners CD44 and ICAM-1. PECAM-1 co-localizes with moesin at the cell periphery and in filopodia of glass-activated human patelets. Interestingly PECAM-1 co-localizes with moesin at the tips of the filopodia, as previously described for moesin. Scanning electron microscopy shows the tips of the filopodia containing small flat structures, which are probably engaged in cell adhesion. Furthermore the interaction of moesin with PECAM-1 could be confirmed by immunoprecipitation in thrombin-activated platelets. This interaction does not occur in resting platelets. This study suggests a possible role for moesin in platelet adhesion by linking PECAM-1 to the actin-cytoskeleton. Migrating cells such as smooth muscle cells and fibroblasts of the arterial media in the case of restenosis after PTA use the mechanism of adhesion to form new cell-cell and cell-matrix contacts. Cell migration is a complex process, which is accompanied by changes of the cell-morphology, along with the rearrangement of the cytoskeleton, controlled cell-matrix interaction and changes of the gene-transcription. Proteins such as moesin participate in the signal transduction between the extracellular space and the cytoplasma. Smooth muscle cells do not express moesin in vivo. In the second part of this work we examined the possibility of moesin re-expression in migrating smooth muscle cells during media-restenosis. Moesin could be detected only hours after PTA in porcine carotid artery media tissue and as long as 14 days after PTA in the carotid tissue of rats. Moesin is being re-expressed in dilated media tissue and could be an early marker for the induction of restenosis. The function of the re-expressed moesin is not definitely known yet. It is important to identify membrane-proteins that interact with moesin in these cells to better understand the function of re-expression. This knowledge could be important for the understanding of cell-migration and restenosis and could gain a clinical-therapeutical significance.","abstract_html":"Moesin is a member of the Ezrin/Radixin/Moesin (ERM) protein family, which is located in cellular protrusions such as filopoda. Members of this family form a cross-link between the actin cytoskeleton and the plasma membrane. They participate in signal transduction between the extrecellular matrix, the cell surface and the cytoplasma. In this study we investigated whether PECAM-1 (platelet endothelial cell adhesion molecule-1) is a membrane-binding partner for moesin in human platelets. The juxta-membrane cytoplasmic domaine of PECAM-1 contains a cluster of positively charged aminoacid-residues similar to the known consensus-sequences of the ERM protein membrane-binding partners CD44 and ICAM-1. PECAM-1 co-localizes with moesin at the cell periphery and in filopodia of glass-activated human patelets. Interestingly PECAM-1 co-localizes with moesin at the tips of the filopodia, as previously described for moesin. Scanning electron microscopy shows the tips of the filopodia containing small flat structures, which are probably engaged in cell adhesion. Furthermore the interaction of moesin with PECAM-1 could be confirmed by immunoprecipitation in thrombin-activated platelets. This interaction does not occur in resting platelets. This study suggests a possible role for moesin in platelet adhesion by linking PECAM-1 to the actin-cytoskeleton. Migrating cells such as smooth muscle cells and fibroblasts of the arterial media in the case of restenosis after PTA use the mechanism of adhesion to form new cell-cell and cell-matrix contacts. Cell migration is a complex process, which is accompanied by changes of the cell-morphology, along with the rearrangement of the cytoskeleton, controlled cell-matrix interaction and changes of the gene-transcription. Proteins such as moesin participate in the signal transduction between the extracellular space and the cytoplasma. Smooth muscle cells do not express moesin in vivo. In the second part of this work we examined the possibility of moesin re-expression in migrating smooth muscle cells during media-restenosis. Moesin could be detected only hours after PTA in porcine carotid artery media tissue and as long as 14 days after PTA in the carotid tissue of rats. Moesin is being re-expressed in dilated media tissue and could be an early marker for the induction of restenosis. The function of the re-expressed moesin is not definitely known yet. It is important to identify membrane-proteins that interact with moesin in these cells to better understand the function of re-expression. This knowledge could be important for the understanding of cell-migration and restenosis and could gain a clinical-therapeutical significance.","abstract_has_math":false,"creators":["Seifert, Kerstin"],"institution":"Publikationsserver der RWTH Aachen University","degree_name":null,"degree_level":null,"degree_discipline":null,"degree_department":null,"school":null,"contributors":["vom Dahl, Jürgen"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2003,"date_issued":"2003","date_published":"2003","updated_at":"2026-07-30T19:41:00Z","subjects":["info:eu-repo/classification/ddc/610","Medizin","Moesin","ERM","Aktin","PECAM-1","Thrombozyten","Zytoskelett","Restenose","Reexpression"],"languages":["ger"],"rights":["info:eu-repo/semantics/openAccess"],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["https://publications.rwth-aachen.de/search?p=id:%22RWTH-CONV-114812%22"],"render_values":[{"text":"https://publications.rwth-aachen.de/search?p=id:%22RWTH-CONV-114812%22","href":"https://publications.rwth-aachen.de/search?p=id:%22RWTH-CONV-114812%22","code":true}]}]},"links":{"outbound_url":"https://publications.rwth-aachen.de/record/52599","outbound_label":"Repository record","outbound_source":"dc:identifier"},"source_record":{"url":"https://publications.rwth-aachen.de/oai2d?verb=GetRecord&metadataPrefix=oai_dc&identifier=oai%3Apublications.rwth-aachen.de%3A52599","prefix":"oai_dc"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["vom Dahl, Jürgen"]},{"key":"dc:creator","label":"Author","values":["Seifert, Kerstin"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:coverage","label":"Dc Coverage","values":["DE"]},{"key":"dc:date","label":"Dc Date","values":["2003"]},{"key":"dc:publisher","label":"Institution","values":["Publikationsserver der RWTH Aachen University"]},{"key":"dc:relation","label":"Dc Relation","values":["info:eu-repo/semantics/altIdentifier/urn/urn:nbn:de:hbz:82-opus-6750"]},{"key":"dc:type","label":"Dc Type","values":["info:eu-repo/semantics/doctoralThesis","info:eu-repo/semantics/publishedVersion"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["info:eu-repo/classification/ddc/610","Medizin","Moesin","ERM","Aktin","PECAM-1","Thrombozyten","Zytoskelett","Restenose","Reexpression"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["ger"]},{"key":"dc:rights","label":"Dc Rights","values":["info:eu-repo/semantics/openAccess"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["https://publications.rwth-aachen.de/record/52599","https://publications.rwth-aachen.de/search?p=id:%22RWTH-CONV-114812%22"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["Moesin is a member of the Ezrin/Radixin/Moesin (ERM) protein family, which is located in cellular protrusions such as filopoda. Members of this family form a cross-link between the actin cytoskeleton and the plasma membrane. They participate in signal transduction between the extrecellular matrix, the cell surface and the cytoplasma. In this study we investigated whether PECAM-1 (platelet endothelial cell adhesion molecule-1) is a membrane-binding partner for moesin in human platelets. The juxta-membrane cytoplasmic domaine of PECAM-1 contains a cluster of positively charged aminoacid-residues similar to the known consensus-sequences of the ERM protein membrane-binding partners CD44 and ICAM-1. PECAM-1 co-localizes with moesin at the cell periphery and in filopodia of glass-activated human patelets. Interestingly PECAM-1 co-localizes with moesin at the tips of the filopodia, as previously described for moesin. Scanning electron microscopy shows the tips of the filopodia containing small flat structures, which are probably engaged in cell adhesion. Furthermore the interaction of moesin with PECAM-1 could be confirmed by immunoprecipitation in thrombin-activated platelets. This interaction does not occur in resting platelets. This study suggests a possible role for moesin in platelet adhesion by linking PECAM-1 to the actin-cytoskeleton. Migrating cells such as smooth muscle cells and fibroblasts of the arterial media in the case of restenosis after PTA use the mechanism of adhesion to form new cell-cell and cell-matrix contacts. Cell migration is a complex process, which is accompanied by changes of the cell-morphology, along with the rearrangement of the cytoskeleton, controlled cell-matrix interaction and changes of the gene-transcription. Proteins such as moesin participate in the signal transduction between the extracellular space and the cytoplasma. Smooth muscle cells do not express moesin in vivo. In the second part of this work we examined the possibility of moesin re-expression in migrating smooth muscle cells during media-restenosis. Moesin could be detected only hours after PTA in porcine carotid artery media tissue and as long as 14 days after PTA in the carotid tissue of rats. Moesin is being re-expressed in dilated media tissue and could be an early marker for the induction of restenosis. The function of the re-expressed moesin is not definitely known yet. It is important to identify membrane-proteins that interact with moesin in these cells to better understand the function of re-expression. This knowledge could be important for the understanding of cell-migration and restenosis and could gain a clinical-therapeutical significance."]},{"key":"dc:source","label":"Dc Source","values":["Aachen : Publikationsserver der RWTH Aachen University 62 S. : Ill. (2003). = Aachen, Techn. Hochsch., Diss., 2003"]},{"key":"dc:title","label":"Title","values":["Moesin in Thrombozyten interagiert mit PECAM-1 : Bedeutung für die Atherosklerose und Restenose"]}]}],"canonical_facts":{"dc:contributor":["vom Dahl, Jürgen"],"dc:coverage":["DE"],"dc:creator":["Seifert, Kerstin"],"dc:date":["2003"],"dc:description":["Moesin is a member of the Ezrin/Radixin/Moesin (ERM) protein family, which is located in cellular protrusions such as filopoda. Members of this family form a cross-link between the actin cytoskeleton and the plasma membrane. They participate in signal transduction between the extrecellular matrix, the cell surface and the cytoplasma. In this study we investigated whether PECAM-1 (platelet endothelial cell adhesion molecule-1) is a membrane-binding partner for moesin in human platelets. The juxta-membrane cytoplasmic domaine of PECAM-1 contains a cluster of positively charged aminoacid-residues similar to the known consensus-sequences of the ERM protein membrane-binding partners CD44 and ICAM-1. PECAM-1 co-localizes with moesin at the cell periphery and in filopodia of glass-activated human patelets. Interestingly PECAM-1 co-localizes with moesin at the tips of the filopodia, as previously described for moesin. Scanning electron microscopy shows the tips of the filopodia containing small flat structures, which are probably engaged in cell adhesion. Furthermore the interaction of moesin with PECAM-1 could be confirmed by immunoprecipitation in thrombin-activated platelets. This interaction does not occur in resting platelets. This study suggests a possible role for moesin in platelet adhesion by linking PECAM-1 to the actin-cytoskeleton. Migrating cells such as smooth muscle cells and fibroblasts of the arterial media in the case of restenosis after PTA use the mechanism of adhesion to form new cell-cell and cell-matrix contacts. Cell migration is a complex process, which is accompanied by changes of the cell-morphology, along with the rearrangement of the cytoskeleton, controlled cell-matrix interaction and changes of the gene-transcription. Proteins such as moesin participate in the signal transduction between the extracellular space and the cytoplasma. Smooth muscle cells do not express moesin in vivo. In the second part of this work we examined the possibility of moesin re-expression in migrating smooth muscle cells during media-restenosis. Moesin could be detected only hours after PTA in porcine carotid artery media tissue and as long as 14 days after PTA in the carotid tissue of rats. Moesin is being re-expressed in dilated media tissue and could be an early marker for the induction of restenosis. The function of the re-expressed moesin is not definitely known yet. It is important to identify membrane-proteins that interact with moesin in these cells to better understand the function of re-expression. This knowledge could be important for the understanding of cell-migration and restenosis and could gain a clinical-therapeutical significance."],"dc:identifier":["https://publications.rwth-aachen.de/record/52599","https://publications.rwth-aachen.de/search?p=id:%22RWTH-CONV-114812%22"],"dc:language":["ger"],"dc:publisher":["Publikationsserver der RWTH Aachen University"],"dc:relation":["info:eu-repo/semantics/altIdentifier/urn/urn:nbn:de:hbz:82-opus-6750"],"dc:rights":["info:eu-repo/semantics/openAccess"],"dc:source":["Aachen : Publikationsserver der RWTH Aachen University 62 S. : Ill. (2003). = Aachen, Techn. Hochsch., Diss., 2003"],"dc:subject":["info:eu-repo/classification/ddc/610","Medizin","Moesin","ERM","Aktin","PECAM-1","Thrombozyten","Zytoskelett","Restenose","Reexpression"],"dc:title":["Moesin in Thrombozyten interagiert mit PECAM-1 : Bedeutung für die Atherosklerose und Restenose"],"dc:type":["info:eu-repo/semantics/doctoralThesis","info:eu-repo/semantics/publishedVersion"]},"updated_at":"2026-07-30T19:41:00Z"}