{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,29]],"date-time":"2026-04-29T06:30:28Z","timestamp":1777444228367,"version":"3.51.4"},"reference-count":5,"publisher":"SAGE Publications","issue":"6","license":[{"start":{"date-parts":[[2017,1,23]],"date-time":"2017-01-23T00:00:00Z","timestamp":1485129600000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/journals.sagepub.com\/page\/policies\/text-and-data-mining-license"}],"content-domain":{"domain":["journals.sagepub.com"],"crossmark-restriction":true},"short-container-title":["Ann Clin Biochem"],"published-print":{"date-parts":[[2017,11]]},"abstract":"\n Background<\/jats:title>\n We investigated the in\u00a0vitro effects of various phospholipids as emulsifiers on the hydrolysing activities of lipoprotein lipase (LPL) Arg243His against triolein as substrate. LPL Arg243His, identified in a patient with hyperchylomicronaemia, displays severely diminished activity for triolein when emulsified with Triton X-100.<\/jats:p>\n <\/jats:sec>\n \n Methods<\/jats:title>\n Lipolytic activities of plasma obtained by heparin injection from a homozygous patient with LPL Arg243His were analysed using triolein emulsified with phosphatidylcholine (PC), phosphatidylethanolamine (PE), phosphatidylserine (PS), phosphatidylinositol (PI), lysophosphatidylcholine (LPC), or Triton X-100 as substrates.<\/jats:p>\n <\/jats:sec>\n \n Results<\/jats:title>\n The hydrolysing activities of the patient\u2019s plasma for triolein emulsified with PC, PE, PS, PI, LPC and Triton X-100 were 9.22\u2009\u00b1\u20091.06\u2009 \u03bcmol\/ml\/h\/ngLPL, 2.94\u2009\u00b1\u20091.60\u2009 \u03bcmol\/ml\/h\/ng LPL, 3.72\u2009\u00b1\u20091.63\u2009 \u03bcmol\/ml\/h\/ng LPL, 3.40\u2009\u00b1\u20091.20\u2009 \u03bcmol\/ml\/h\/ngLPL, 3.72\u2009\u00b1\u20091.96\u2009 \u03bcmol\/ml\/h\/ngLPL and 7.80\u2009\u00b1\u20094.48\u2009 \u03bcmol\/ml\/h\/ng LPL, respectively. Thus, the specific activities of the patient\u2019s LPL determined with triolein emulsified with PC were significantly higher than those with PE, PS, PI or LPC as emulsifiers. Relative to the activities of normal plasma measured with PC, PE, PS, PI and LPC as emulsifiers, the mutant\u2019s activities were 49.1\u2009\u00b1\u20095.2%, 44.1\u2009\u00b1\u20095.7%, 31.7\u2009\u00b1\u200912.6%, 19.2\u2009\u00b1\u20096.9% and 23.8\u2009\u00b1\u200911.3%, respectively. Using PC, PE, PS, PI and LPC as emulsifiers, the mutant\u2019s activities for triolein-lipolysis relative to normal were significantly increased in comparison to the relative activity measured with the classical emulsifier, Triton X-100 (12.9\u2009\u00b1\u20096.7%).<\/jats:p>\n <\/jats:sec>\n \n Conclusions<\/jats:title>\n Impaired triolein hydrolysis by LPL Arg243His was partially ameliorated by triolein emulsification with phospholipids. The in\u00a0vitro analysis of triolein hydrolysis using various phospholipid emulsifiers may be useful for the further understanding of impaired LPL function.<\/jats:p>\n <\/jats:sec>","DOI":"10.1177\/0004563217693258","type":"journal-article","created":{"date-parts":[[2017,1,24]],"date-time":"2017-01-24T01:25:47Z","timestamp":1485221147000},"page":"712-715","update-policy":"https:\/\/doi.org\/10.1177\/sage-journals-update-policy","source":"Crossref","is-referenced-by-count":0,"title":["Severely impaired activity of lipoprotein lipase Arg243His is partially ameliorated by emulsifying phospholipids in\n in\u00a0vitro<\/i>\n triolein hydrolysis analysis"],"prefix":"10.1177","volume":"54","author":[{"given":"Takashi","family":"Yamaguchi","sequence":"first","affiliation":[{"name":"Center of Diabetes, Endocrinology and Metabolism, Toho University Sakura Medical Center, Sakura, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Takeyoshi","family":"Murano","sequence":"additional","affiliation":[{"name":"Department of Clinical-Laboratory and Experimental-Research Medicine, Toho University Sakura Medical Center, Sakura, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ichiro","family":"Tatsuno","sequence":"additional","affiliation":[{"name":"Center of Diabetes, Endocrinology and Metabolism, Toho University Sakura Medical Center, Sakura, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Nobuyuki","family":"Hiruta","sequence":"additional","affiliation":[{"name":"Department of Clinical-Laboratory and Experimental-Research Medicine, Toho University Sakura Medical Center, Sakura, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Toru","family":"Suzuki","sequence":"additional","affiliation":[{"name":"Department of Diabetes and Metabolism, Tohoku University Hospital, Sendai, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Shojiro","family":"Sawada","sequence":"additional","affiliation":[{"name":"Department of Diabetes and Metabolism, Tohoku University Hospital, Sendai, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Hideki","family":"Katagiri","sequence":"additional","affiliation":[{"name":"Department of Diabetes and Metabolism, Tohoku University Hospital, Sendai, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kohji","family":"Shirai","sequence":"additional","affiliation":[{"name":"Department of Vascular Function, Toho University Sakura Medical Center, Sakura, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Wolfgang J","family":"Schneider","sequence":"additional","affiliation":[{"name":"Department of Medical Biochemistry, Max F. Perutz Laboratories, Medical University of Vienna, Vienna, Austria"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Hideaki","family":"Bujo","sequence":"additional","affiliation":[{"name":"Department of Clinical-Laboratory and Experimental-Research Medicine, Toho University Sakura Medical Center, Sakura, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"179","published-online":{"date-parts":[[2017,1,23]]},"reference":[{"key":"bibr1-0004563217693258","doi-asserted-by":"publisher","DOI":"10.1038\/nrendo.2015.26"},{"key":"bibr2-0004563217693258","doi-asserted-by":"publisher","DOI":"10.1016\/j.atherosclerosis.2005.02.025"},{"key":"bibr3-0004563217693258","doi-asserted-by":"publisher","DOI":"10.2169\/internalmedicine.55.5239"},{"key":"bibr4-0004563217693258","doi-asserted-by":"publisher","DOI":"10.1172\/JCI115507"},{"key":"bibr5-0004563217693258","doi-asserted-by":"crossref","first-page":"473","DOI":"10.1016\/S0021-9258(18)52459-5","volume":"266","author":"Dichek HL","year":"1991","journal-title":"J Biol Chem"}],"container-title":["Annals of Clinical Biochemistry: International Journal of Laboratory Medicine"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/journals.sagepub.com\/doi\/pdf\/10.1177\/0004563217693258","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/journals.sagepub.com\/doi\/full-xml\/10.1177\/0004563217693258","content-type":"application\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/journals.sagepub.com\/doi\/pdf\/10.1177\/0004563217693258","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,4,28]],"date-time":"2026-04-28T12:23:09Z","timestamp":1777378989000},"score":1,"resource":{"primary":{"URL":"http:\/\/journals.sagepub.com\/doi\/10.1177\/0004563217693258"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2017,1,23]]},"references-count":5,"journal-issue":{"issue":"6","published-print":{"date-parts":[[2017,11]]}},"alternative-id":["10.1177\/0004563217693258"],"URL":"https:\/\/doi.org\/10.1177\/0004563217693258","relation":{},"ISSN":["0004-5632","1758-1001"],"issn-type":[{"value":"0004-5632","type":"print"},{"value":"1758-1001","type":"electronic"}],"subject":[],"published":{"date-parts":[[2017,1,23]]}}}