Evidence map›Paper›PMID 25707358›Full record

ArticleBiochimica et biophysica acta2015

Oligomeric state regulated trafficking of human platelet-activating factor acetylhydrolase type-II.

Elizabeth S Monillas, Jeffrey L Caplan, Anastasia F Thévenin, Brian J Bahnson

Abstract read
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In one paragraph

Article in Biochimica et biophysica acta, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Article
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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.

Elizabeth S MonillasDepartment of Chemistry & Biochemistry, University of Delaware, Newark, DE 19716, USA.
Jeffrey L CaplanDepartment of Biological Sciences, University of Delaware, Newark, DE 19716, USA.
Anastasia F ThéveninDepartment of Chemistry & Biochemistry, University of Delaware, Newark, DE 19716, USA.
Brian J BahnsonDepartment of Chemistry & Biochemistry, University of Delaware, Newark, DE 19716, USA. Electronic address: bahnson@udel.edu.

Funding

Predictive Modeling & Optimal Control Framework for Model-Based Epidemic Response in DelawareP20GM103446 · NIGMS · UNIVERSITY OF DELAWARE · PI Anjana Narayan Bhat · 2012 to 2026
$67.2M
TOWARDS SOLID-STATE NMR STRUCTURES OF GPCRSP20RR015588 · NCRR · UNIVERSITY OF DELAWARE · PI LENHOFF, ABRAHAM M · 2000 to 2009
$18.2M
CHEMISTRY-BIOLOGY INTERFACE PREDOCTORAL TRAININGT32GM008550 · NIGMS · UNIVERSITY OF DELAWARE · PI BAHNSON, BRIAN J · 1994 to 2018
$5.0M
COBRE on Membrane Protein Production and CharacterizationP30GM103519 · NIGMS · UNIVERSITY OF DELAWARE · PI LENHOFF, ABRAHAM M · 2012 to 2014
$3.3M
Structure and Interfacial Function of Platelet Activating Factor AcetylhydrolaseR01HL084366 · NHLBI · UNIVERSITY OF DELAWARE · PI BAHNSON, BRIAN J · 2007 to 2011
$1.7M
NCRR NIH HHS P20 RR015588NHLBI NIH HHS 5R01HL084366NHLBI NIH HHS R01 HL084366NIGMS NIH HHS 8P30GM103519NIGMS NIH HHS P20 GM103446NIGMS NIH HHS P30 GM103519NIGMS NIH HHS T32 GM008550
6 · The paper itself

Abstract

The intracellular enzyme platelet-activating factor acetylhydrolase type-II (PAFAH-II) hydrolyzes platelet-activating factor and oxidatively fragmented phospholipids. PAFAH-II in its resting state is mainly cytoplasmic, and it responds to oxidative stress by becoming increasingly bound to endoplasmic reticulum and Golgi membranes. Numerous studies have indicated that this enzyme is essential for protecting cells from oxidative stress induced apoptosis. However, the regulatory mechanism of the oxidative stress response by PAFAH-II has not been fully resolved. Here, changes to the oligomeric state of human PAFAH-II were investigated as a potential regulatory mechanism toward enzyme trafficking. Native PAGE analysis in vitro and photon counting histogram within live cells showed that PAFAH-II is both monomeric and dimeric. A Gly-2-Ala site-directed mutation of PAFAH-II demonstrated that the N-terminal myristoyl group is required for homodimerization. Additionally, the distribution of oligomeric PAFAH-II is distinct within the cell; homodimers of PAFAH-II were localized to the cytoplasm while monomers were associated to the membranes of the endoplasmic reticulum and Golgi. We propose that the oligomeric state of PAFAH-II drives functional protein trafficking. PAFAH-II localization to the membrane is critical for substrate acquisition and effective oxidative stress protection. It is hypothesized that the balance between monomer and dimer serves as a regulatory mechanism of a PAFAH-II oxidative stress response.

Indexed as

1-Alkyl-2-acetylglycerophosphocholine EsteraseCytoplasmHEK293 CellsHumansModels, MolecularOxidative StressProtein MultimerizationProtein TransportTissue Distribution1-Alkyl-2-acetylglycerophosphocholine EsteraseMyristoylationOligomeric stateOxidative stressPeripheral membrane proteinPhospholipase A2Trafficking

Identifiers

PMID25707358
PMCPMC4380869

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Registered trials

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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.