Evidence map›Paper›PMID 18974965›Full record

ArticleJournal of molecular medicine (Berlin, Germany)2009

Lysophosphatidylcholine acyltransferase 1 (LPCAT1) overexpression in human colorectal cancer.

Francisco Mansilla, Kerry-Ann da Costa, Shuli Wang, Mogens Kruhøffer, Tal M Lewin, Torben F Orntoft, Rosalind A Coleman, Karin Birkenkamp-Demtröder

Open access · greenAbstract readMulticenter Study
In one paragraph

Article in Journal of molecular medicine (Berlin, Germany), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.

0numbers the graph read from it
0cells of the map it votes in
75citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

75 citing papers in PubMed, 130 citations in OpenAlex.

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15 more citing papers are in PubMed but not listed here.

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

8 authors at 2 institutions in 2 countries.

Francisco MansillaMolecular Diagnostic Laboratory, Center for Molecular Clinical Cancer Research, Arhus University Hospital/Skejby, 8200, Aarhus, Denmark. Francisco.mansilla@ki.au.dk
Kerry-Ann da Costa
Shuli Wang
Mogens Kruhøffer
Tal M Lewin
Torben F Orntoft
Rosalind A Coleman
Karin Birkenkamp-Demtröder
Aarhus University Hospital · DKUniversity of North Carolina at Chapel Hill · US

Funding

UNIV OF NORTH CAROLINA CLINICAL NUTRITION RESEARCH UNITP30DK056350 · NIDDK · UNIV OF NORTH CAROLINA CHAPEL HILL · PI SUSAN M. SMITH · 1999 to 2026
$31.6M
METABOLISM OF GLYCEROLIPIDS IN LIVERR01DK056598 · NIDDK · UNIV OF NORTH CAROLINA CHAPEL HILL · PI COLEMAN, ROSALIND ANNE · 1999 to 2016
$5.0M
Acyl-CoA Synthetase: Structure, Function and RegulationR01DK059935 · NIDDK · UNIV OF NORTH CAROLINA CHAPEL HILL · PI COLEMAN, ROSALIND ANNE · 2002 to 2015
$4.7M
Barth Syndrome: Identifying the missing enzyme functionR21HL081554 · NHLBI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI LEWIN, TAL M · 2005 to 2006
$393k
Glycerolipid synthesis in liverR56DK056598 · NIDDK · UNIV OF NORTH CAROLINA CHAPEL HILL · PI COLEMAN, ROSALIND ANNE · 2017 to 2017
$228k
NHLBI NIH HHS HL081554NHLBI NIH HHS R21 HL081554NIDDK NIH HHS DK56598NIDDK NIH HHS DK59935NIDDK NIH HHS P30 DK056350NIDDK NIH HHS P30-DK56350NIDDK NIH HHS R01 DK056598NIDDK NIH HHS R01 DK059935NIDDK NIH HHS R56 DK056598
6 · The paper itself

Abstract

The alteration of the choline metabolite profile is a well-established characteristic of cancer cells. In colorectal cancer (CRC), phosphatidylcholine is the most prominent phospholipid. In the present study, we report that lysophosphatidylcholine acyltransferase 1 (LPCAT1; NM_024830.3), the enzyme that converts lysophosphatidylcholine into phosphatidylcholine, was highly overexpressed in colorectal adenocarcinomas when compared to normal mucosas. Our microarray transcription profiling study showed a significant (p < 10(-8)) transcript overexpression in 168 colorectal adenocarcinomas when compared to ten normal mucosas. Immunohistochemical analysis of colon tumors with a polyclonal antibody to LPCAT1 confirmed the upregulation of the LPCAT1 protein. Overexpression of LPCAT1 in COS7 cells localized the protein to the endoplasmic reticulum and the mitochondria and increased LPCAT1 specific activity 38-fold. In cultured cells, overexpressed LPCAT1 enhanced the incorporation of [(14)C]palmitate into phosphatidylcholine. COS7 cells transfected with LPCAT1 showed no growth rate alteration, in contrast to the colon cancer cell line SW480, which significantly (p < 10(-5)) increased its growth rate by 17%. We conclude that LPCAT1 may contribute to total choline metabolite accumulation via phosphatidylcholine remodeling, thereby altering the CRC lipid profile, a characteristic of malignancy.

Indexed as

Gene Expression Regulation, EnzymologicGene Expression Regulation, Neoplastic1-Acylglycerophosphocholine O-AcyltransferaseAdenocarcinomaAdultAgedAnimalsCell Line, TumorChlorocebus aethiopsCholineColorectal NeoplasmsCOS CellsFemaleGene Expression ProfilingHumansMale1-Acylglycerophosphocholine O-AcyltransferaseCholineLpcat1 protein, humanNeoplasm Proteins

Identifiers

PMID18974965
PMCPMC2614561
OpenAlexW2128680328

What OpenQuestion holds

Textmetadata
LicenceTDM
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.