{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,19]],"date-time":"2026-10-19T01:43:49Z","timestamp":1792374229536,"version":"4.4.0"},"reference-count":51,"publisher":"Ovid Technologies (Wolters Kluwer Health)","issue":"9","content-domain":{"domain":["www.ahajournals.org"],"crossmark-restriction":true},"short-container-title":["JAHA"],"published-print":{"date-parts":[[2018,5]]},"abstract":"<jats:sec xml:lang=\"en\">\n                    <jats:title>Background<\/jats:title>\n                    <jats:p xml:lang=\"en\">Phospholipid transfer protein (PLTP) is one of the major modulators of lipoprotein metabolism and atherosclerosis development; however, little is known about the regulation of PLTP. The effect of hepatic prodomain of furin (profurin) expression on PLTP processing and function is investigated.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec xml:lang=\"en\">\n                    <jats:title>Methods and Results<\/jats:title>\n                    <jats:p xml:lang=\"en\">We used adenovirus expressing profurin in mouse liver to evaluate PLTP activity, mass, and plasma lipid levels. We coexpressed PLTP and profurin in human hepatoma cell line cells and studied their interaction. We found profurin expression significantly reduced plasma lipids, plasma PLTP activity, and mass in all tested mouse models, compared with controls. Moreover, the expression of profurin dramatically reduced liver PLTP activity and protein level. We further explored the mechanism using in\u00a0vivo and ex\u00a0vivo approaches. We found that profurin can interact with intracellular PLTP and promote its ubiquitination and proteasomal degradation, resulting in less PLTP secretion from the hepatocytes. Furin does not cleave PLTP; instead, it forms a complex with PLTP, likely through its prodomain.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec xml:lang=\"en\">\n                    <jats:title>Conclusions<\/jats:title>\n                    <jats:p xml:lang=\"en\">Our study reveals that hepatic PLTP protein is targeted for proteasomal degradation by profurin expression, which could be a novel posttranslational mechanism underlying PLTP regulation.<\/jats:p>\n                  <\/jats:sec>","DOI":"10.1161\/jaha.118.008526","type":"journal-article","created":{"date-parts":[[2018,4,21]],"date-time":"2018-04-21T05:20:11Z","timestamp":1524288011000},"update-policy":"https:\/\/doi.org\/10.1161\/crossmarkpolicy","source":"Crossref","is-referenced-by-count":7,"title":["Prodomain of Furin Promotes Phospholipid Transfer Protein Proteasomal Degradation in Hepatocytes"],"prefix":"10.1161","volume":"7","author":[{"given":"Yang","family":"Yu","sequence":"first","affiliation":[{"name":"Department of Cell Biology, State University of New York Downstate Medical Center, Brooklyn, NY"},{"name":"Key Laboratory of Atherosclerosis in Universities of Shandong and Institute of Atherosclerosis, Taishan Medical University, Taian, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xia","family":"Lei","sequence":"additional","affiliation":[{"name":"Department of Cell Biology, State University of New York Downstate Medical Center, Brooklyn, NY"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hui","family":"Jiang","sequence":"additional","affiliation":[{"name":"Department of Cell Biology, State University of New York Downstate Medical Center, Brooklyn, NY"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zhiqiang","family":"Li","sequence":"additional","affiliation":[{"name":"Department of Cell Biology, State University of New York Downstate Medical Center, Brooklyn, NY"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"John W. 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