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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Tie2 is tied at the cell-cell contacts and to extracellular matrix by Angiopoietin-1</title><author><name sortKey="Fukuhara, Shigetomo" sort="Fukuhara, Shigetomo" uniqKey="Fukuhara S" first="Shigetomo" last="Fukuhara">Shigetomo Fukuhara</name><affiliation><nlm:aff id="A1">Department of Structural Analysis, National Cardiovascular Center Research Institute, Fujishirodai 5-7-1, Suita, Osaka 565-8565, Japan.</nlm:aff></affiliation></author><author><name sortKey="Sako, Keisuke" sort="Sako, Keisuke" uniqKey="Sako K" first="Keisuke" last="Sako">Keisuke Sako</name><affiliation><nlm:aff id="A1">Department of Structural Analysis, National Cardiovascular Center Research Institute, Fujishirodai 5-7-1, Suita, Osaka 565-8565, Japan.</nlm:aff></affiliation></author><author><name sortKey="Noda, Kazuomi" sort="Noda, Kazuomi" uniqKey="Noda K" first="Kazuomi" last="Noda">Kazuomi Noda</name><affiliation><nlm:aff id="A1">Department of Structural Analysis, National Cardiovascular Center Research Institute, Fujishirodai 5-7-1, Suita, Osaka 565-8565, Japan.</nlm:aff></affiliation></author><author><name sortKey="Nagao, Kaori" sort="Nagao, Kaori" uniqKey="Nagao K" first="Kaori" last="Nagao">Kaori Nagao</name><affiliation><nlm:aff id="A1">Department of Structural Analysis, National Cardiovascular Center Research Institute, Fujishirodai 5-7-1, Suita, Osaka 565-8565, Japan.</nlm:aff></affiliation></author><author><name sortKey="Miura, Koichi" sort="Miura, Koichi" uniqKey="Miura K" first="Koichi" last="Miura">Koichi Miura</name><affiliation><nlm:aff id="A1">Department of Structural Analysis, National Cardiovascular Center Research Institute, Fujishirodai 5-7-1, Suita, Osaka 565-8565, Japan.</nlm:aff></affiliation></author><author><name sortKey="Mochizuki, Naoki" sort="Mochizuki, Naoki" uniqKey="Mochizuki N" first="Naoki" last="Mochizuki">Naoki Mochizuki</name><affiliation><nlm:aff id="A1">Department of Structural Analysis, National Cardiovascular Center Research Institute, Fujishirodai 5-7-1, Suita, Osaka 565-8565, Japan.</nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">19293632</idno><idno type="pmc">2679245</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2679245</idno><idno type="RBID">PMC:2679245</idno><idno type="doi">10.3858/emm.2009.41.3.016</idno><date when="2009">2009</date><idno type="wicri:Area/Pmc/Corpus">004C51</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">004C51</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Tie2 is tied at the cell-cell contacts and to extracellular matrix by Angiopoietin-1</title><author><name sortKey="Fukuhara, Shigetomo" sort="Fukuhara, Shigetomo" uniqKey="Fukuhara S" first="Shigetomo" last="Fukuhara">Shigetomo Fukuhara</name><affiliation><nlm:aff id="A1">Department of Structural Analysis, National Cardiovascular Center Research Institute, Fujishirodai 5-7-1, Suita, Osaka 565-8565, Japan.</nlm:aff></affiliation></author><author><name sortKey="Sako, Keisuke" sort="Sako, Keisuke" uniqKey="Sako K" first="Keisuke" last="Sako">Keisuke Sako</name><affiliation><nlm:aff id="A1">Department of Structural Analysis, National Cardiovascular Center Research Institute, Fujishirodai 5-7-1, Suita, Osaka 565-8565, Japan.</nlm:aff></affiliation></author><author><name sortKey="Noda, Kazuomi" sort="Noda, Kazuomi" uniqKey="Noda K" first="Kazuomi" last="Noda">Kazuomi Noda</name><affiliation><nlm:aff id="A1">Department of Structural Analysis, National Cardiovascular Center Research Institute, Fujishirodai 5-7-1, Suita, Osaka 565-8565, Japan.</nlm:aff></affiliation></author><author><name sortKey="Nagao, Kaori" sort="Nagao, Kaori" uniqKey="Nagao K" first="Kaori" last="Nagao">Kaori Nagao</name><affiliation><nlm:aff id="A1">Department of Structural Analysis, National Cardiovascular Center Research Institute, Fujishirodai 5-7-1, Suita, Osaka 565-8565, Japan.</nlm:aff></affiliation></author><author><name sortKey="Miura, Koichi" sort="Miura, Koichi" uniqKey="Miura K" first="Koichi" last="Miura">Koichi Miura</name><affiliation><nlm:aff id="A1">Department of Structural Analysis, National Cardiovascular Center Research Institute, Fujishirodai 5-7-1, Suita, Osaka 565-8565, Japan.</nlm:aff></affiliation></author><author><name sortKey="Mochizuki, Naoki" sort="Mochizuki, Naoki" uniqKey="Mochizuki N" first="Naoki" last="Mochizuki">Naoki Mochizuki</name><affiliation><nlm:aff id="A1">Department of Structural Analysis, National Cardiovascular Center Research Institute, Fujishirodai 5-7-1, Suita, Osaka 565-8565, Japan.</nlm:aff></affiliation></author></analytic><series><title level="j">Experimental & Molecular Medicine</title><idno type="ISSN">1226-3613</idno><imprint><date when="2009">2009</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Angiopoietin-1 (Ang1) binds to and activates Tie2 receptor tyrosine kinase. Ang1-Tie2 signal has been proposed to exhibit two opposite roles in the controlling blood vessels. One is vascular stabilization and the other is vascular angiogenesis. There has been no answer to the question as to how Tie2 induces two opposite responses to the same ligand. Our group and Dr. Alitalo's group have demonstrated that trans-associated Tie2 at cell-cell contacts and extracellular matrix (ECM)-anchored Tie2 play distinct roles in the endothelial cells. The complex formation depends on the presence or absence of cell-cell adhesion. Here, we review how Ang1-Tie2 signal regulates vascular maintenance and angiogenesis. We further point to the unanswered questions that must be clarified to extend our knowledge of vascular biology and to progress basic knowledge to the treatment of the diseases in which Ang1-Tie2-mediated signal is central.</p></div></front></TEI><pmc xml:lang="EN" article-type="review-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Exp Mol Med</journal-id><journal-id journal-id-type="publisher-id">EMM</journal-id><journal-title>Experimental & Molecular Medicine</journal-title><issn pub-type="ppub">1226-3613</issn><publisher><publisher-name>Korean Society of Medical Biochemistry and Molecular Biology</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">19293632</article-id><article-id pub-id-type="pmc">2679245</article-id><article-id pub-id-type="doi">10.3858/emm.2009.41.3.016</article-id><article-categories><subj-group subj-group-type="heading"><subject>Review</subject></subj-group></article-categories><title-group><article-title>Tie2 is tied at the cell-cell contacts and to extracellular matrix by Angiopoietin-1</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Fukuhara</surname><given-names>Shigetomo</given-names></name><xref ref-type="aff" rid="A1"></xref></contrib><contrib contrib-type="author"><name><surname>Sako</surname><given-names>Keisuke</given-names></name><xref ref-type="aff" rid="A1"></xref></contrib><contrib contrib-type="author"><name><surname>Noda</surname><given-names>Kazuomi</given-names></name><xref ref-type="aff" rid="A1"></xref></contrib><contrib contrib-type="author"><name><surname>Nagao</surname><given-names>Kaori</given-names></name><xref ref-type="aff" rid="A1"></xref></contrib><contrib contrib-type="author"><name><surname>Miura</surname><given-names>Koichi</given-names></name><xref ref-type="aff" rid="A1"></xref></contrib><contrib contrib-type="author" corresp="yes"><name><surname>Mochizuki</surname><given-names>Naoki</given-names></name><xref ref-type="aff" rid="A1"></xref></contrib></contrib-group><aff id="A1">Department of Structural Analysis, National Cardiovascular Center Research Institute, Fujishirodai 5-7-1, Suita, Osaka 565-8565, Japan.</aff><author-notes><corresp>Corresponding author: Tel, 81-6-6833-5012; Fax, 81-6-6835-5461; <email>nmochizu@ri.ncvc.go.jp</email></corresp></author-notes><pub-date pub-type="ppub"><day>31</day><month>3</month><year>2009</year></pub-date><pub-date pub-type="epub"><day>31</day><month>3</month><year>2009</year></pub-date><volume>41</volume><issue>3</issue><fpage>133</fpage><lpage>139</lpage><history><date date-type="accepted"><day>29</day><month>1</month><year>2009</year></date></history><permissions><copyright-statement>Copyright © 2009 Korean Society of Medical Biochemistry and Molecular Biology</copyright-statement><copyright-year>2009</copyright-year></permissions><abstract><p>Angiopoietin-1 (Ang1) binds to and activates Tie2 receptor tyrosine kinase. Ang1-Tie2 signal has been proposed to exhibit two opposite roles in the controlling blood vessels. One is vascular stabilization and the other is vascular angiogenesis. There has been no answer to the question as to how Tie2 induces two opposite responses to the same ligand. Our group and Dr. Alitalo's group have demonstrated that trans-associated Tie2 at cell-cell contacts and extracellular matrix (ECM)-anchored Tie2 play distinct roles in the endothelial cells. The complex formation depends on the presence or absence of cell-cell adhesion. Here, we review how Ang1-Tie2 signal regulates vascular maintenance and angiogenesis. We further point to the unanswered questions that must be clarified to extend our knowledge of vascular biology and to progress basic knowledge to the treatment of the diseases in which Ang1-Tie2-mediated signal is central.</p></abstract><kwd-group><kwd>angiopoietin-1</kwd><kwd>angiostatic proteins</kwd><kwd>cell movement</kwd><kwd>cell proliferation</kwd><kwd>extracellular signal-regulated MAP kinases</kwd><kwd>neovacularizaton, pathologic</kwd><kwd>neovascularization, physiologic</kwd><kwd>proto-oncogene proteins c-akt</kwd><kwd>receptor, TIE-2</kwd></kwd-group></article-meta></front><floats-wrap><fig id="F1" position="float"><label>Figure 1</label><caption><p>Schematic illustration of two opposite functions mediated by angiopoietin-1 (Ang1)-Tie2 signaling. Ang1-Tie2 regulates both angiostasis and angiogenesis. In the mature vessels, vascular endothelial cells are supported by pericytes or vascular smooth muscle cells (VSMCs) that release Ang1. In clear contrast, it is reported that Ang1-Tie2 signal is required for developmental and pathological angiogenesis in which inter-endothelial cell adhesions are disrupted by vascular endothelial growth factor (VEGF).</p></caption><graphic xlink:href="emm-41-133-g001"></graphic></fig><fig id="F2" position="float"><label>Figure 2</label><caption><p>Distinct roles of trans-associated Tie2 for vascular quiescence and extracellular matrix (ECM)-anchored Tie2 for angiogenesis. Transassociated-Tie2 at the cell-cell contacts preferentially activated AKT and upregulates Krüppel-like factor 2 (KLF2) transcription factor, resulting in cell survival and resistance to inflammation by VEGF. On the other hand, ECM-anchored Tie2 induces ERK activation preferable for cell migration and proliferation once cell-cell adhesions are disrupted by VEGF or other signaling. Therefore, Tie2-expressing cells that dissociate from surrounding endothelial cells contribute to angiogenesis.</p></caption><graphic xlink:href="emm-41-133-g002"></graphic></fig><fig id="F3" position="float"><label>Figure 3</label><caption><p>Unsolved questions in Ang-Tie signaling. The role of Ang1-Ang4 as well as angiopoietin-like factors (Angptl) and their specific receptors must be identified to clearly understand Ang-Tie signaling. Additionally, we need to know when and where Ang-Tie family members are expressed and activated during angiogenesis (e.g. during intersomitic vessel (ISV) formation after sprouting from dorsal aorta (DA)). Furthermore, it would be interesting to examine the involvement of M1 macrophages in inflammatory angiogenesis. To test this possibility, it should be clarified whether Tie receptors are expressed in M1 macrophages and whether Ang2 activates M1 macrophages.</p></caption><graphic xlink:href="emm-41-133-g003"></graphic></fig></floats-wrap></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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