Evidence map›Paper›PMID 38275747›Full record

ArticleBiomolecules2023

Lipopolysaccharide Stimulates A549 Cell Migration through p-Tyr 42 RhoA and Phospholipase D1 Activity.

Shohel Mahmud, Amir Hamza, Yoon-Beom Lee, Jung-Ki Min, Rokibul Islam, Oyungerel Dogsom, Jae-Bong Park

Open access · goldAbstract read
In one paragraph

Article in Biomolecules, 2023. 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
0.3field-weighted citation impact, top 35% 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

1 citing paper in PubMed, 2 citations in OpenAlex.

  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

7 authors at 1 institution in 3 countries.

Shohel MahmudDepartment of Biochemistry, College of Medicine, Hallym University, Hallymdaehag-Gil 1, Chuncheon 24252, Kangwon-do, Republic of Korea.ORCID 0009-0005-3580-9859
Amir HamzaDepartment of Biochemistry, College of Medicine, Hallym University, Hallymdaehag-Gil 1, Chuncheon 24252, Kangwon-do, Republic of Korea.
Yoon-Beom LeeDepartment of Biochemistry, College of Medicine, Hallym University, Hallymdaehag-Gil 1, Chuncheon 24252, Kangwon-do, Republic of Korea.
Jung-Ki MinDepartment of Biochemistry, College of Medicine, Hallym University, Hallymdaehag-Gil 1, Chuncheon 24252, Kangwon-do, Republic of Korea.
Rokibul IslamDepartment of Biochemistry, College of Medicine, Hallym University, Hallymdaehag-Gil 1, Chuncheon 24252, Kangwon-do, Republic of Korea.
Oyungerel DogsomDepartment of Biochemistry, College of Medicine, Hallym University, Hallymdaehag-Gil 1, Chuncheon 24252, Kangwon-do, Republic of Korea.ORCID 0000-0001-8210-3182
Jae-Bong ParkDepartment of Biochemistry, College of Medicine, Hallym University, Hallymdaehag-Gil 1, Chuncheon 24252, Kangwon-do, Republic of Korea.
Hallym University · KR

Funding

National Research Foundation of Korea RS-2023-00208724National Research Foundation of Korea RS-2023-00217013
6 · The paper itself

Abstract

Cell migration is a crucial contributor to metastasis, a critical process associated with the mortality of cancer patients. The initiation of metastasis is triggered by epithelial-mesenchymal transition (EMT), along with the changes in the expression of EMT marker proteins. Inflammation plays a significant role in carcinogenesis and metastasis. Lipopolysaccharide (LPS), a typical inflammatory agent, promoted the generation of superoxide through the activation of p-Tyr42 RhoA, Rho-dependent kinase 2 (ROCK2), and the phosphorylation of p47phox. In addition, p-Tyr42 RhoA activated phospholipase D1 (PLD1), with PLD1 and phosphatidic acid (PA) being involved in superoxide production. PA also regulated the expression of EMT proteins. Consequently, we have identified MHY9 (Myosin IIA, NMIIA) as a PA-binding protein in response to LPS. MYH9 also contributed to cell migration and the alteration in the expression of EMT marker proteins. Co-immunoprecipitation revealed the formation of a complex involving p-Tyr42 RhoA, PLD1, and MYH9. These proteins were found to be distributed in both the cytosol and nucleus. In addition, we have found that p-Tyr42 RhoA PLD1 and MYH9 associate with the ZEB1 promoter. The suppression of ZEB1 mRNA levels was achieved through the knockdown of RhoA, PLD1, and MYH9 using si-RNAs. Taken together, we propose that p-Tyr42 RhoA and PLD1, responsible for producing PA, and PA-bound MYH9 are involved in the regulation of ZEB1 expression, thereby promoting cell migration.

Indexed as

LipopolysaccharidesPhospholipase DSignal TransductionCell MovementHumansPhosphatidic AcidsrhoA GTP-Binding ProteinSuperoxidesLipopolysaccharidesPhosphatidic AcidsPhospholipase Dphospholipase D1rhoA GTP-Binding ProteinRHOA protein, humanSuperoxidescell migrationMYH9PLD1p-Tyr42 RhoAZEB1

Identifiers

PMID38275747
PMCPMC10813223
OpenAlexW4390013590

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.