Evidence map›Paper›PMID 39878319›Full record

ArticleJournal of cellular and molecular medicine2025

LPCAT1, the Enzyme Responsible for Converting LPC to PC, Promotes OPC Differentiation In Vitro.

Qi Shang, Xin Zhang, Yingyan Pu, Junjian Lin, Peng Ma, Yuchen Pan, Ming Zhao, Dingya Sun, Li Cao

Abstract read
In one paragraph

Article in Journal of cellular and molecular medicine, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Article
  3. 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

9 authors.

Qi ShangDepartment of Neurobiology, Key Laboratory of Molecular Neurobiology of the Ministry of Education, Naval Medical University, Shanghai, China.
Xin ZhangDepartment of Neurobiology, Key Laboratory of Molecular Neurobiology of the Ministry of Education, Naval Medical University, Shanghai, China.
Yingyan PuDepartment of Neurobiology, Key Laboratory of Molecular Neurobiology of the Ministry of Education, Naval Medical University, Shanghai, China.
Junjian LinDepartment of Neurobiology, Key Laboratory of Molecular Neurobiology of the Ministry of Education, Naval Medical University, Shanghai, China.
Peng MaDepartment of Anesthesiology, Changzheng Hospital, Naval Medical University, Shanghai, China.
Yuchen PanDepartment of Neurobiology, Key Laboratory of Molecular Neurobiology of the Ministry of Education, Naval Medical University, Shanghai, China.
Ming ZhaoDepartment of Neurology, Naval Specialty Medical Center, Naval Medical University, Shanghai, China.
Dingya SunDepartment of Neurobiology, Key Laboratory of Molecular Neurobiology of the Ministry of Education, Naval Medical University, Shanghai, China.ORCID 0000-0002-6583-4503
Li CaoDepartment of Neurobiology, Key Laboratory of Molecular Neurobiology of the Ministry of Education, Naval Medical University, Shanghai, China.

Funding

National Natural Science Foundation of China 31700924National Natural Science Foundation of China 81871040National Natural Science Foundation of China 82101412
6 · The paper itself

Abstract

Myelin is the key structure for high-speed information transmission and is formed by oligodendrocytes (OLs) which are differentiated from oligodendrocyte precursor cells (OPCs) in the central nervous system. Lipid is the main component of myelin and the role of lipid metabolism-related molecules in myelination attach increasing attention. Lysophosphatidylcholine acyltransferase 1 (LPCAT1) mediates the conversion of lysophosphatidylcholine (LPC) to phosphatidylcholine (PC), and its role in myelination draws our interest as LPC is a classical demyelination inducer and PC is a major component of myelin. In this work, LPCAT1 is found expressed in the oligodendrocyte lineage cells during myelination. In vitro experiments showed that the expression level of LPCAT1 gradually increased along with the differentiation process from OPCs to OLs, and over-expression and interference experiments showed that LPCAT1 promoted OPCs differentiation without affecting their proliferation or apoptosis. Mechanistically, the undertaker of LPCAT1's pro-differentiation role is not PC, but the phosphorylated mTOR which is a key regulator in OPCs differentiation. RNA sequencing analysis showed LPCAT1 promoted the expression of ZBTB20 which is an important transcription factor related to lipid metabolism and regulates mTOR phosphorylation. In vivo, complex myelin tomacula involving multiple axons was formed after conditionally knocking out LPCAT1 in oligodendrocyte lineage cells, but no obvious myelin thickness abnormalities were observed. Our results indicate that LPCAT1 is an important regulator of myelination, and lipid metabolism-related molecules may be new valuable targets for the treatment of diseases with myelin abnormalities.

Indexed as

1-Acylglycerophosphocholine O-AcyltransferaseCell DifferentiationLysophosphatidylcholinesOligodendrocyte Precursor CellsOligodendrogliaPhosphatidylcholinesAnimalsCell ProliferationCells, CulturedMiceMyelin SheathRatsTOR Serine-Threonine KinasesTranscription Factors1-Acylglycerophosphocholine O-AcyltransferaseLysophosphatidylcholinesPhosphatidylcholinesTOR Serine-Threonine KinasesTranscription Factorslipid metabolismLPCAT1myelinationOPCsZBTB20

Identifiers

PMID39878319
PMCPMC11775935

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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.