Evidence map›Paper›PMID 24535284›Full record

ReviewCurrent opinion in lipidology2014

Perilipin 5, a lipid droplet protein adapted to mitochondrial energy utilization.

Alan R Kimmel, Carole Sztalryd

Open access · greenAbstract readReview
In one paragraph

Review in Current opinion in lipidology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 82 papers.

0numbers the graph read from it
0cells of the map it votes in
82citing papers in PubMed
5.8field-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

82 citing papers in PubMed, 122 citations in OpenAlex.

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  7. Integrated Transcriptomic and Proteomic Analysis RevealsAnimals : an open access journal from MDPI · 2026
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22 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

2 authors at 2 institutions in 1 country.

Alan R KimmelaLaboratory of Cellular and Developmental Biology (50/3351), National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland bThe Geriatric Research, Education and Clinical Center, Baltimore Veterans Affairs Healthcare Center, Division of Endocrinology, Department of Medicine, School of Medicine, University of Maryland, Baltimore, Maryland, USA.
Carole Sztalryd
National Institutes of Health · USUniversity of Maryland, Baltimore · US

Funding

SIGNALING PATHWAYS IN CONTROL OF GROWTH AND DEVELOPMENTZIADK075040 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI KIMMEL, ALAN R · 2009 to 2025
$23.9M
Research BaseP30DK072488 · NIDDK · UNIVERSITY OF MARYLAND BALTIMORE · PI MITCHELL, BRAXTON D, TAYLOR, SIMEON I. · 2005 to 2019
$17.3M
Role of PAT proteins in ectopic fat depositionR01DK075017 · NIDDK · UNIVERSITY OF MARYLAND BALTIMORE · PI SZTALRYD, CAROLE A · 2007 to 2011
$1.4M
Intramural NIH HHSNIDDK NIH HHS 1R01 DK075017NIDDK NIH HHS DK072488NIDDK NIH HHS P30 DK072488NIDDK NIH HHS R01 DK075017
6 · The paper itself

Abstract

purpose of reviewWe summarize recent mechanistic and physiological studies related to the role of perilipin 5 (Plin5) in regulating lipid droplet accumulation and protection to fatty acids in tissues with high lipid oxidative metabolism. RECENT

findingsPlin5 is a lipid droplet targeting protein that promotes association of lipid droplets with mitochondria and is most highly expressed in oxidative tissues, including cardiac and skeletal muscle. Recent in-vivo and in-vitro data indicate an important role for Plin5 in the regulation of cardiac lipid storage and function. Targeted overexpression of Plin5 in heart causes steatosis, mild mitochondria dysfunction, and hypertrophy in cardiac tissue, but without affecting cardiac function. In contrast, whole body ablation of Plin5 (Plin5  mice) reduces cardiac lipid droplet formation, increases cardiac fatty acid oxidation, and promotes cardiac dysfunction; cardiac defects can be prevented with antioxidative therapy. These data suggest a cytoprotective role for Plin5 to promote lipid storage but to limit fatty acid toxicity, parameters critical for tissues with high lipid oxidative metabolism. SUMMARY: In-vivo and in-vitro data suggest that Plin5 is part of a cell-adaptive response to high lipid oxidative metabolism to protect lipid droplet storage against neutral lipases and, so, limit fatty acid accumulation. Although the specific mechanisms that underlie Plin5 lipid droplet storage protection in oxidative tissues remain to be fully elucidated, Plin5 provides a basis for the novel cytoprotective nature of lipid droplets.

Indexed as

Energy MetabolismLipid MetabolismAnimalsHumansIntracellular Signaling Peptides and ProteinsMitochondriaMuscle ProteinsOrganellesPerilipin-5ProteinsIntracellular Signaling Peptides and Proteinslipid storage droplet protein 5, mouseMuscle ProteinsPerilipin-5Plin5 protein, mouseProteins

Identifiers

PMID24535284
PMCPMC4517968
OpenAlexW1984578729

What OpenQuestion holds

Textmetadata
LicenceTDM
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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.