Evidence map›Paper›PMID 8601635›Full record

ArticleThe Journal of clinical investigation1996

Pancreatic carboxyl ester lipase: a circulating enzyme that modifies normal and oxidized lipoproteins in vitro.

R Shamir, W J Johnson, K Morlock-Fitzpatrick, R Zolfaghari, L Li, E Mas, D Lombardo, D W Morel, E A Fisher

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of clinical investigation, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
5.0field-weighted citation impact, top 4% 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

23 citing papers in PubMed, 74 citations in OpenAlex.

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  6. Farnesoid X Receptor and Its Ligands Inhibit the Function of Platelets.Arteriosclerosis, thrombosis, and vascular biology · 2016
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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

9 authors at 4 institutions in 2 countries.

R ShamirDepartment of Biochemistry, Medical College of Pennsylvania and Hahnemann University, Philadelphia, 19129, USA.
W J Johnson
K Morlock-Fitzpatrick
R Zolfaghari
L Li
E Mas
D Lombardo
D W Morel
E A Fisher
Drexel University · USAix-Marseille Université · FRHahnemann University Hospital · USIcahn School of Medicine at Mount Sinai · US

Funding

TISSUE CULTURE CORE LABORATORYP01HL022633 · NHLBI · MCP HAHNEMANN UNIVERSITY · PI LUND-KATZ, SISSEL · 1985 to 2013
$26.1M
HYDROYSIS OF VITAMIN A ESTERS IN LIVERR01DK044498 · NIDDK · U.S. DEPARTMENT OF AGRICULTURE · PI HARRISON, EARL HOWARD · 1992 to 2007
$1.6M
NHLBI NIH HHS HL-07443NHLBI NIH HHS HL-22633NIDDK NIH HHS DK-44498
6 · The paper itself

Abstract

Pancreatic carboxyl ester lipase (CEL) hydrolyzes cholesteryl esters (CE), triglycerides (TG), and lysophospholipids, with CE and TG hydrolysis stimulated by cholate. Originally thought to be confined to the gastrointestinal system, CEL has been reported in the plasma of humans and other mammals, implying its potential in vivo to modify lipids associated with LDL, HDL (CE, TG), and oxidized LDL (lysophosphatidylcholine, lysoPC). We measured the concentration of CEL in human plasma as 1.2+/-0.5 ng/ml (in the range reported for lipoprotein lipase). Human LDL and HDL3 reconstituted with radiolabeled lipids were incubated with purified porcine CEL without or with cholate (10 or 100 microM, concentrations achievable in systemic or portal plasma, respectively). Using a saturating concentration of lipoprotein-associated CE (4 microM), with increasing cholate concentration there was an increase in the hydrolysis of LDL- and HDL3-CE; at 100 microM cholate, the present hydrolysis per hour was 32+/-2 and 1.6+/-0.1, respectively, indicating that CEL interaction varied with lipoprotein class. HDL3-TG hydrolysis was also observed, but was only approximately 5-10% of that for HDL3-CE at either 10 or 100 microM cholate. Oxidized LDL (OxLDL) is enriched with lysoPC, a proatherogenic compound. After a 4-h incubation with CEL, the lysoPC content of OxLDL was depleted 57%. Colocalization of CEL in the vicinity of OxLDL formation was supported by demonstrating in human aortic homogenate a cholate-stimulated cholesteryl ester hydrolytic activity inhibited by anti-human CEL IgG. We conclude that CEL has the capability to modify normal human LDL and HDL composition and structure and to reduce the atherogenicity of OxLDL by decreasing its lysoPC content.

Indexed as

AnimalsAorta, ThoracicCarboxylesteraseCarboxylic Ester HydrolasesCholesterol EstersFemaleHumansHydrolysisIn Vitro TechniquesLipoproteinsLipoproteins, HDLLipoproteins, LDLLysophosphatidylcholinesMaleOxidation-ReductionPancreasCarboxylesteraseCarboxylic Ester HydrolasesCholesterol EstersLipoproteinsLipoproteins, HDLLipoproteins, LDLLysophosphatidylcholinesTriglycerides

Identifiers

PMID8601635
PMCPMC507234
OpenAlexW2008039790

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.