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We showed that angiopoietin\u20101 (ang1) also interacts with integrins on cardiac myocytes (CMs) to increase survival. Because ang1 monomers bind and activate integrins (not tie2), we determined their function\n                    <jats:italic>in vivo<\/jats:italic>\n                    . We examined monomer and multimer expressions during physiological and pathological cardiac remodeling and overexpressed ang1 monomers in phenylephrine\u2010induced cardiac hypertrophy. Cardiac ang1 levels (mRNA, protein) increased during postnatal development and decreased with phenylephrine\u2010induced cardiac hypertrophy, whereas tie2 phosphorylations were unchanged. We found that most or all of the changes during cardiac remodeling were in monomers, offering an explanation for unchanged tie2 activity. Heart tissue contains abundant ang1 monomers and few multimers (Western blotting). We generated plasmids that produce ang1 monomers (ang1\u2013256), injected them into mice, and confirmed cardiac expression (immunohistochemistry, RT\u2010PCR). Ang1 monomers localize to CMs, smooth muscle cells, and endothelial cells. In phenylephrine\u2010induced cardiac hypertrophy, ang1\u2013256 reduced left ventricle (LV)\/tibia ratios, fetal gene expressions (atrial and brain natriuretic peptides, skeletal actin, \u03b2\u2010myosin heavy chain), and fibrosis (collagen III), and increased LV prosurvival signaling (akt, MAPK\n                    <jats:sub>p42\/44<\/jats:sub>\n                    ), and AMPK\n                    <jats:sub>T172<\/jats:sub>\n                    . However, tie2 phosphorylations were unchanged. Ang1\u2013256 increased integrin\u2010linked kinase, a key regulator of integrin signaling and cardiac health. Collectively, these results suggest a role for ang1 monomers in cardiac remodeling.\u2014Dallabrida, S. M., Ismail, N. S., Pravda, E. A., Parodi, E. M., Dickie, R., Durand, E. M., Lai, J., Cassiola, F., Rogers, R. A., Rupnick, M. A. Integrin binding angiopoietin\u20101 monomers reduce cardiac hypertrophy.\n                    <jats:italic>FASEB J.<\/jats:italic>\n                    22, 3010\u20133023 (2008)\n                  <\/jats:p>","DOI":"10.1096\/fj.07-100966","type":"journal-article","created":{"date-parts":[[2008,5,23]],"date-time":"2008-05-23T21:21:32Z","timestamp":1211577692000},"page":"3010-3023","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":40,"title":["Integrin binding angiopoietin\u20101 monomers reduce cardiac hypertrophy"],"prefix":"10.1096","volume":"22","author":[{"given":"Susan M.","family":"Dallabrida","sequence":"first","affiliation":[{"name":"Division of Vascular Biology Children's Hospital Boston Massachusetts USA"},{"name":"Harvard Medical School Affiliates Boston Massachusetts USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Nesreen S.","family":"Ismail","sequence":"additional","affiliation":[{"name":"Division of Vascular Biology Children's Hospital Boston Massachusetts USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Elke A.","family":"Pravda","sequence":"additional","affiliation":[{"name":"Division of Vascular Biology Children's Hospital Boston Massachusetts USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Emily M.","family":"Parodi","sequence":"additional","affiliation":[{"name":"Division of Vascular Biology Children's Hospital Boston Massachusetts USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Renee","family":"Dickie","sequence":"additional","affiliation":[{"name":"Harvard School of Public Health, Harvard University Boston Massachusetts USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ellen M.","family":"Durand","sequence":"additional","affiliation":[{"name":"Division of Vascular Biology Children's Hospital Boston Massachusetts USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jean","family":"Lai","sequence":"additional","affiliation":[{"name":"Harvard School of Public Health, Harvard University Boston Massachusetts USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Flavia","family":"Cassiola","sequence":"additional","affiliation":[{"name":"Division of Vascular Biology Children's Hospital Boston Massachusetts USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Rick A.","family":"Rogers","sequence":"additional","affiliation":[{"name":"Division of Vascular Biology Children's Hospital Boston Massachusetts USA"},{"name":"Harvard School of Public Health, Harvard University Boston Massachusetts USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Maria A.","family":"Rupnick","sequence":"additional","affiliation":[{"name":"Division of Vascular Biology Children's Hospital Boston Massachusetts USA"},{"name":"Harvard Medical School Affiliates Boston Massachusetts USA"},{"name":"Chemical Engineering Department Massachusetts Institute of Technology Cambridge Massachusetts USA"},{"name":"Division of Cardiovascular Medicine Brigham and Women's Hospital Boston Massachusetts USA"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2008,5,23]]},"reference":[{"key":"e_1_2_5_2_1","first-page":"1471","article-title":"tek, a novel tyrosine kinase gene located on mouse chromosome 4, is expressed in endothelial cells and their presumptive precursors","volume":"7","author":"Dumont D. 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