{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,7]],"date-time":"2025-11-07T19:09:38Z","timestamp":1762542578476,"version":"build-2065373602"},"reference-count":63,"publisher":"Ovid Technologies (Wolters Kluwer Health)","issue":"12","content-domain":{"domain":["www.ahajournals.org"],"crossmark-restriction":true},"short-container-title":["ATVB"],"published-print":{"date-parts":[[2016,12]]},"abstract":"<jats:sec>\n                    <jats:title>Objective\u2014<\/jats:title>\n                    <jats:p>We examined the function of ABCA1 (ATP-binding cassette transporter A1) in ApoA-I (apolipoprotein A-I) mobilization of cholesterol microdomains deposited into the extracellular matrix by cholesterol-enriched macrophages. We have also determined whether an ApoA-I mimetic peptide without and with complexing to sphingomyelin can mobilize macrophage-deposited cholesterol microdomains.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Approach and Results\u2014<\/jats:title>\n                    <jats:p>\n                      Extracellular cholesterol microdomains deposited by cholesterol-enriched macrophages were detected with a monoclonal antibody, 58B1. ApoA-I and an ApoA-I mimetic peptide 5A mobilized cholesterol microdomains deposited by ABCA1\n                      <jats:sup>+\/+<\/jats:sup>\n                      macrophages but not by ABCA1\n                      <jats:sup>\u2212\/\u2212<\/jats:sup>\n                      macrophages. In contrast, ApoA-I mimetic peptide 5A complexed with sphingomyelin could mobilize cholesterol microdomains deposited by ABCA1\n                      <jats:sup>\u2212\/\u2212<\/jats:sup>\n                      macrophages.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Conclusions\u2014<\/jats:title>\n                    <jats:p>Our findings show that a unique pool of extracellular cholesterol microdomains deposited by macrophages can be mobilized by both ApoA-I and an ApoA-I mimetic peptide but that mobilization depends on macrophage ABCA1. It is known that ABCA1 complexes ApoA-I and ApoA-I mimetic peptide with phospholipid, a cholesterol-solubilizing agent, explaining the requirement for ABCA1 in extracellular cholesterol microdomain mobilization. Importantly, ApoA-I mimetic peptide already complexed with phospholipid can mobilize macrophage-deposited extracellular cholesterol microdomains even in the absence of ABCA1.<\/jats:p>\n                  <\/jats:sec>","DOI":"10.1161\/atvbaha.116.308334","type":"journal-article","created":{"date-parts":[[2016,10,6]],"date-time":"2016-10-06T23:10:42Z","timestamp":1475795442000},"page":"2283-2291","update-policy":"https:\/\/doi.org\/10.1161\/crossmarkpolicy","source":"Crossref","is-referenced-by-count":21,"title":["ABCA1 (ATP-Binding Cassette Transporter A1) Mediates ApoA-I (Apolipoprotein A-I) and ApoA-I Mimetic Peptide Mobilization of Extracellular Cholesterol Microdomains Deposited by Macrophages"],"prefix":"10.1161","volume":"36","author":[{"given":"Xueting","family":"Jin","sequence":"first","affiliation":[{"name":"From the Experimental Atherosclerosis Section (X.J., Y.L., H.S.K.) and Lipoprotein Metabolism Section (D.S., B.V., A.T.R.), National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD; and Department of Structural Biology, Weizmann Institute of Science, Rehovot, Israel (L.A.)."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Denis","family":"Sviridov","sequence":"additional","affiliation":[{"name":"From the Experimental Atherosclerosis Section (X.J., Y.L., H.S.K.) and Lipoprotein Metabolism Section (D.S., B.V., A.T.R.), National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD; and Department of Structural Biology, Weizmann Institute of Science, Rehovot, Israel (L.A.)."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ying","family":"Liu","sequence":"additional","affiliation":[{"name":"From the Experimental Atherosclerosis Section (X.J., Y.L., H.S.K.) and Lipoprotein Metabolism Section (D.S., B.V., A.T.R.), National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD; and Department of Structural Biology, Weizmann Institute of Science, Rehovot, Israel (L.A.)."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Boris","family":"Vaisman","sequence":"additional","affiliation":[{"name":"From the Experimental Atherosclerosis Section (X.J., Y.L., H.S.K.) and Lipoprotein Metabolism Section (D.S., B.V., A.T.R.), National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD; and Department of Structural Biology, Weizmann Institute of Science, Rehovot, Israel (L.A.)."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Lia","family":"Addadi","sequence":"additional","affiliation":[{"name":"From the Experimental Atherosclerosis Section (X.J., Y.L., H.S.K.) and Lipoprotein Metabolism Section (D.S., B.V., A.T.R.), National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD; and Department of Structural Biology, Weizmann Institute of Science, Rehovot, Israel (L.A.)."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Alan T.","family":"Remaley","sequence":"additional","affiliation":[{"name":"From the Experimental Atherosclerosis Section (X.J., Y.L., H.S.K.) and Lipoprotein Metabolism Section (D.S., B.V., A.T.R.), National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD; and Department of Structural Biology, Weizmann Institute of Science, Rehovot, Israel (L.A.)."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Howard S.","family":"Kruth","sequence":"additional","affiliation":[{"name":"From the Experimental Atherosclerosis Section (X.J., Y.L., H.S.K.) and Lipoprotein Metabolism Section (D.S., B.V., A.T.R.), National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD; and Department of Structural Biology, Weizmann Institute of Science, Rehovot, Israel (L.A.)."}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"276","reference":[{"key":"e_1_3_5_2_2","first-page":"201","article-title":"Localization of unesterified cholesterol in human atherosclerotic lesions. 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