Evidence map›Paper›PMID 27845686›Full record

ArticleJournal of lipid research2017

Lipoprotein lipase activity and interactions studied in human plasma by isothermal titration calorimetry.

Mart Reimund, Oleg Kovrov, Gunilla Olivecrona, Aivar Lookene

Open access · hybridAbstract read
In one paragraph

Article in Journal of lipid research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.6field-weighted citation impact, top 14% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

21 citing papers in PubMed, 35 citations in OpenAlex.

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  14. Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8.American journal of physiology. Endocrinology and metabolism · 2021
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 2 countries.

Mart ReimundDepartment of Chemistry, Tallinn University of Technology, Tallinn 12618, Estonia.
Oleg KovrovDepartment of Chemistry, Tallinn University of Technology, Tallinn 12618, Estonia.
Gunilla OlivecronaDepartment of Medical Biosciences, Umeå University, SE-901 87 Umeå, Sweden.
Aivar LookeneDepartment of Chemistry, Tallinn University of Technology, Tallinn 12618, Estonia aivar.lookene@ttu.ee.
Tallinn University of Technology · EEUmeå University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

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 angiopoietin-like protein (ANGPTL)3 or ANGPTL4 caused reduction of the activity of LPL via a two-step mechanism. 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.

Indexed as

CalorimetryAdultAngiopoietin-Like Protein 3Angiopoietin-Like Protein 4Angiopoietin-like ProteinsAngiopoietinsAnimalsApolipoprotein C-IIICattleFatty AcidsFemaleHealthy VolunteersHumansHydrolysisKineticsLipolysisAngiopoietin-Like Protein 3Angiopoietin-Like Protein 4Angiopoietin-like ProteinsAngiopoietinsANGPTL3 protein, humanANGPTL4 protein, humanApolipoprotein C-IIIFatty AcidsLipoprotein LipaseLipoproteins, VLDLTriglyceridesangiopoietin-like proteinsapolipoproteinsenzymologylipolysistriglyceridesvery low density lipoprotein

Identifiers

PMID27845686
PMCPMC5234706
OpenAlexW2553163325

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.