Evidence map›Paper›PMID 41193595›Full record

ArticleScientific reports2025

Homeostatic response of phospholipid pathways to PCYT2 deficiency and impaired de Novo synthesis of phosphatidylethanolamine.

Roya Iraji, Michaela St Germain, Sophie Grapentine, Leanne Perreira, Laila Schenkel, Sara Al-Douri, Lyn M Hillyer, Clara E Cho, David W L Ma, Marica Bakovic

Abstract read
In one paragraph

Article in Scientific reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

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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

1 citing paper in PubMed.

  1. Article
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

10 authors.

Roya IrajiDepartment of Human Health and Nutritional Sciences, University of Guelph, Guelph, Canada.
Michaela St GermainDepartment of Human Health and Nutritional Sciences, University of Guelph, Guelph, Canada.
Sophie GrapentineDepartment of Human Health and Nutritional Sciences, University of Guelph, Guelph, Canada.
Leanne PerreiraDepartment of Human Health and Nutritional Sciences, University of Guelph, Guelph, Canada.
Laila SchenkelDepartment of Human Health and Nutritional Sciences, University of Guelph, Guelph, Canada.
Sara Al-DouriDepartment of Human Health and Nutritional Sciences, University of Guelph, Guelph, Canada.
Lyn M HillyerDepartment of Human Health and Nutritional Sciences, University of Guelph, Guelph, Canada.
Clara E ChoDepartment of Human Health and Nutritional Sciences, University of Guelph, Guelph, Canada.
David W L MaDepartment of Human Health and Nutritional Sciences, University of Guelph, Guelph, Canada.
Marica BakovicDepartment of Human Health and Nutritional Sciences, University of Guelph, Guelph, Canada. mbakovic@uoguelph.ca.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

PCYT2 is the key regulatory enzyme in the biosynthesis of phosphatidylethanolamine (PE) via the CDP-ethanolamine Kennedy pathway. Deficiencies in this gene have been linked to metabolic, neurological, and cardiac disorders; however, most studies report that PE levels remain unchanged. This study aimed to identify the metabolic mechanisms that preserve PE levels when its synthesis is impaired in PCYT2-knockdown human fibroblasts. We investigated alternative pathways that could compensate for reduced PE synthesis, including phosphatidylcholine (PC) and PE base-exchange to phosphatidylserine (PS), followed by PE resynthesis via PS decarboxylation. These pathways were individually assessed using [14 C]-ethanolamine, [3 H]-choline, and [3 H]-serine, and correlated with the expression and activity of the base-exchange genes PTSS1, PTSS2, and the PS decarboxylase PISD. The base-exchange activity was not significantly altered and mitochondrial PS decarboxylation was inhibited, indicating that these routes do not compensate for reduced PE synthesis in PCYT2-deficient cells. Chronic choline treatment increased ethanolamine and choline transport and upregulated the choline/ethanolamine transporter CTL1, yet PC synthesis and base-exchange activity remained unchanged, demonstrating that choline supplementation does not affect PE sythesis. Instead, PE homeostasis was maintained through reduced degradation and extensive phospholipid remodeling via the Lands' cycle, as evidenced by broad changes in fatty acid composition and increased phospholipid unsaturation. Remodeling extended beyond PC, PE, and PS to include phosphatidylinositol and sphingomyelin. These metabolic adaptations led to elevated reactive oxygen species production and enhanced mitochondrial fusion without significantly affecting autophagy or cell viability. Our findings suggest that in the absence of PCYT2 activity, PE levels are preserved primarily through reduced degradation and remodeling, rather than through alternative biosynthetic pathways.

Indexed as

HomeostasisPhosphatidylethanolaminesPhospholipidsCholineEthanolamineFibroblastsHumansMitochondriaPhosphatidylcholinesRNA NucleotidyltransferasesTransferases (Other Substituted Phosphate Groups)CholineEthanolamineEthanolamine-phosphate cytidylyltransferasePhosphatidylcholinesphosphatidylethanolaminePhosphatidylethanolaminesPhospholipidsRNA NucleotidyltransferasesTransferases (Other Substituted Phosphate Groups)CDP-ethanolamine kennedy pathwayFatty acidsPCYT2PhosphatidylethanolaminePhospholipids

Identifiers

PMID41193595
PMCPMC12589596

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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.