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Lipoprotein lipase activity and interactions studied in human plasma by isothermal titration calorimetry
Umeå University, Faculty of Medicine, Department of Medical Biosciences. Department of Chemistry, Tallinn University of Technology, Tallinn 12618, Estonia.
Umeå University, Faculty of Medicine, Department of Medical Biosciences.
2017 (English)In: Journal of Lipid Research, ISSN 0022-2275, E-ISSN 1539-7262, Vol. 58, no 1, 279-288 p.Article in journal (Refereed) Published
Abstract [en]

LPL hydrolyzes triglycerides in plasma lipoproteins. Due to the complex regulation mechanism, it has been difficult to mimic the physiological conditions under which LPL acts in vitro. We demonstrate that isothermal titration calorimetry (ITC), using human plasma as substrate, overcomes several limitations of previously used techniques. The high sensitivity of ITC allows continuous recording of the heat released during hydrolysis. Both initial rates and kinetics for complete hydrolysis of plasma lipids can be studied. The heat rate was shown to correspond to the release of fatty acids and was linearly related to the amount of added enzyme, either purified LPL or postheparin plasma. Addition of apoC-III reduced the initial rate of hydrolysis by LPL, but the inhibition became less prominent with time when the lipoproteins were triglyceride poor. Addition of angiopoietinlike protein (ANGPTL) 3 or ANGPTL4 caused reduction of the activity of LPL via a two-step mechanism.(Jlr) We conclude that ITC can be used for quantitative measurements of LPL activity and interactions under in vivo-like conditions, for comparisons of the properties of plasma samples from patients and control subjects as substrates for LPL, as well as for testing of drug candidates developed with the aim to affect the LPL system.

Place, publisher, year, edition, pages
2017. Vol. 58, no 1, 279-288 p.
Keyword [en]
lipolysis, apolipoproteins, angiopoietin-like proteins, triglycerides, very low density lipoprotein, enzymology
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:umu:diva-131652DOI: 10.1194/jlr.D071787ISI: 000392408700024PubMedID: 27845686Scopus ID: 2-s2.0-85009962352OAI: oai:DiVA.org:umu-131652DiVA: diva2:1077365
Available from: 2017-02-27 Created: 2017-02-27 Last updated: 2017-02-27Bibliographically approved

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CiteExportLink to record
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Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
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  • nn-NO
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  • Other locale
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Output format
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