{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,11,6]],"date-time":"2026-11-06T17:22:48Z","timestamp":1793985768120,"version":"4.8.0"},"reference-count":40,"publisher":"Ovid Technologies (Wolters Kluwer Health)","issue":"8","license":[{"start":{"date-parts":[[2023,9,29]],"date-time":"2023-09-29T00:00:00Z","timestamp":1695945600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"content-domain":{"domain":["www.ahajournals.org"],"crossmark-restriction":true},"short-container-title":["Circulation Research"],"published-print":{"date-parts":[[2023,9,29]]},"abstract":"<jats:sec>\n                    <jats:title>BACKGROUND:<\/jats:title>\n                    <jats:p>\n                      The\n                      <jats:italic>ADAMTS7<\/jats:italic>\n                      locus was genome-wide significantly associated with coronary artery disease. Lack of the ECM (extracellular matrix) protease ADAMTS-7 (A disintegrin and metalloproteinase-7) was shown to reduce atherosclerotic plaque formation. Here, we sought to identify molecular mechanisms and downstream targets of ADAMTS-7 mediating the risk of atherosclerosis.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>METHODS:<\/jats:title>\n                    <jats:p>\n                      Targets of ADAMTS-7 were identified by high-resolution mass spectrometry of atherosclerotic plaques from Apoe\n                      <jats:sup>\u2212\/\u2212<\/jats:sup>\n                      and Apoe\n                      <jats:sup>\u2212\/\u2212<\/jats:sup>\n                      Adamts7\n                      <jats:sup>\u2212\/\u2212<\/jats:sup>\n                      mice. ECM proteins were identified using solubility profiling. Putative targets were validated using immunofluorescence, in vitro degradation assays, coimmunoprecipitation, and F\u00f6rster resonance energy transfer\u2013based protein-protein interaction assays.\n                      <jats:italic>ADAMTS7<\/jats:italic>\n                      expression was measured in fibrous caps of human carotid artery plaques.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>RESULTS:<\/jats:title>\n                    <jats:p>\n                      In humans,\n                      <jats:italic>ADAMTS7<\/jats:italic>\n                      expression was higher in caps of unstable as compared to stable carotid plaques. Compared to Apoe\n                      <jats:sup>\u2212\/\u2212<\/jats:sup>\n                      mice, atherosclerotic aortas of Apoe\n                      <jats:sup>\u2212\/\u2212<\/jats:sup>\n                      mice lacking Adamts-7 (Apoe\n                      <jats:sup>\u2212\/\u2212<\/jats:sup>\n                      Adamts7\n                      <jats:sup>\u2212\/\u2212<\/jats:sup>\n                      ) contained higher protein levels of Timp-1 (tissue inhibitor of metalloprotease-1). In coimmunoprecipitation experiments, the catalytic domain of ADAMTS-7 bound to TIMP-1, which was degraded in the presence of ADAMTS-7 in vitro. ADAMTS-7 reduced the inhibitory capacity of TIMP-1 at its canonical target MMP-9 (matrix metalloprotease-9). As a downstream mechanism, we investigated collagen content in plaques of Apoe\n                      <jats:sup>\u2212\/\u2212<\/jats:sup>\n                      and Apoe\n                      <jats:sup>\u2212\/\u2212<\/jats:sup>\n                      Adamts7\n                      <jats:sup>\u2212\/\u2212<\/jats:sup>\n                      mice after a Western diet. Picrosirius red staining of the aortic root revealed less collagen as a readout of higher MMP-9 activity in Apoe\n                      <jats:sup>\u2212\/\u2212<\/jats:sup>\n                      as compared to Apoe\n                      <jats:sup>\u2212\/\u2212<\/jats:sup>\n                      Adamts7\n                      <jats:sup>\u2212\/\u2212<\/jats:sup>\n                      mice. To facilitate high-throughput screening for ADAMTS-7 inhibitors with the aim of decreasing TIMP-1 degradation, we designed a F\u00f6rster resonance energy transfer\u2013based assay targeting the ADAMTS-7 catalytic site.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>CONCLUSIONS:<\/jats:title>\n                    <jats:p>ADAMTS-7, which is induced in unstable atherosclerotic plaques, decreases TIMP-1 stability reducing its inhibitory effect on MMP-9, which is known to promote collagen degradation and is likewise associated with coronary artery disease. Disrupting the interaction of ADAMTS-7 and TIMP-1 might be a strategy to increase collagen content and plaque stability for the reduction of atherosclerosis-related events.<\/jats:p>\n                  <\/jats:sec>","DOI":"10.1161\/circresaha.123.322737","type":"journal-article","created":{"date-parts":[[2023,9,7]],"date-time":"2023-09-07T05:00:27Z","timestamp":1694062827000},"page":"674-686","update-policy":"https:\/\/doi.org\/10.1161\/crossmarkpolicy","source":"Crossref","is-referenced-by-count":54,"title":["ADAMTS-7 Modulates Atherosclerotic Plaque Formation by Degradation of TIMP-1"],"prefix":"10.1161","volume":"133","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-3532-9271","authenticated-orcid":true,"given":"M. Amin","family":"Sharifi","sequence":"first","affiliation":[{"name":"Department of Cardiology, German Heart Centre Munich, Technical University of Munich, Germany (M.A.S., T.A.D., A.M., M.v.S., J.H., P.M., J.W., B.S., H.B.S., H.S., T.K.)."},{"name":"German Centre for Cardiovascular Research (DZHK e.V.), partner site Munich Heart Alliance, Germany (M.A.S., T.A.D., M.v.S., J.H., P.M., J.W., L.M., J.B., H.B.S., H.S., T.K.)."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0356-5571","authenticated-orcid":true,"given":"Michael","family":"Wierer","sequence":"additional","affiliation":[{"name":"Department of Proteomics and Signal Transduction, Max-Planck Institute of Biochemistry, Martinsried, Germany (M.W., M.M.)."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tan An","family":"Dang","sequence":"additional","affiliation":[{"name":"Department of Cardiology, German Heart Centre Munich, Technical University of Munich, Germany (M.A.S., T.A.D., A.M., M.v.S., J.H., P.M., J.W., B.S., H.B.S., H.S., T.K.)."},{"name":"German Centre for Cardiovascular Research (DZHK e.V.), partner site Munich Heart Alliance, Germany (M.A.S., T.A.D., M.v.S., J.H., P.M., J.W., L.M., J.B., H.B.S., H.S., T.K.)."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jelena","family":"Milic","sequence":"additional","affiliation":[{"name":"Division of Vascular Biology, Institute for Stroke and Dementia Research, Ludwig Maximilian University of Munich, Germany (J.M., J.B.)."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6513-5406","authenticated-orcid":true,"given":"Aldo","family":"Moggio","sequence":"additional","affiliation":[{"name":"Department of Cardiology, German Heart Centre Munich, Technical University of Munich, Germany (M.A.S., T.A.D., A.M., M.v.S., J.H., P.M., J.W., B.S., H.B.S., H.S., 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