Evidence map›Paper›PMID 37156995›Full record

ArticleGenes and immunity2023

Identification of heat shock protein family A member 5 (HSPA5) targets involved in nonalcoholic fatty liver disease.

Aliya Rehati, Buzukela Abuduaini, Zhao Liang, Dong Chen, Fangping He

Open access · hybridAbstract read
In one paragraph

Article in Genes and immunity, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed, 1 pooled it
4.0field-weighted citation impact, top 6% 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

15 citing papers in PubMed, 1 synthesis or guideline pooled it, 26 citations in OpenAlex.

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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

5 authors at 1 institution in 1 country.

Aliya RehatiDepartment of Gastroenterology, The First Affiliated Hospital of Xinjiang Medical University, Urumqi, 830054, Xinjiang, China.
Buzukela AbuduainiDepartment of Intensive Care Unit, The First Affiliated Hospital of Xinjiang Medical University, 393 South Li Yu Shan Road, Urumqi, 830054, Xinjiang, China. 3222576375@qq.com.ORCID 0000-0003-4259-6220
Zhao LiangDepartment of General Surgery, The First Affiliated Hospital of Xinjiang Medical University, Urumqi, 830054, Xinjiang, China.
Dong ChenABLife BioBigData Institute, Wuhan, 430075, Hubei, China.
Fangping HeDepartment of Gastroenterology, The First Affiliated Hospital of Xinjiang Medical University, Urumqi, 830054, Xinjiang, China. 814262308@qq.com.ORCID 0009-0006-8517-5791
Xinjiang Medical University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Heat shock protein family A (Hsp70) member 5 (HSPA5) is an endoplasmic reticulum chaperone, which regulates cell metabolism, particularly lipid metabolism. While HSPA5's role in regulating cell function is well described, HSPA5 binding to RNA and its biological function in nonalcoholic fatty liver disease (NAFLD) is still lacking. In the present study, the ability of HSPA5 to modulate alternative splicing (AS) of cellular genes was assessed using Real-Time PCR on 89 NAFLD-associated genes. RNA immunoprecipitation coupled to RNA sequencing (RIP-Seq) assays were also performed to identify cellular mRNAs bound by HSPA5. We obtained the HSPA5-bound RNA profile in HeLa cells and peak calling analysis revealed that HSPA5 binds to coding genes and lncRNAs. Moreover, RIP-Seq assays demonstrated that HSPA5 immunoprecipitates specific cellular mRNAs such as EGFR, NEAT1, LRP1 and TGFß1, which are important in the pathology of NAFLD. Finally, HSPA5 binding sites may be associated with splicing sites. We used the HOMER algorithm to search for motifs enriched in coding sequence (CDs) peaks, which identified over-representation of the AGAG motif in both sets of immunoprecipitated peaks. HSPA5 regulated genes at the 5'UTR alternative splicing and introns and in an AG-rich sequence-dependent manner. We propose that the HSPA5-AGAG interaction might play an important role in regulating alternative splicing of NAFLD-related genes. This report is the first to demonstrate that HSPA5 regulated pre-RNA alternative splicing, stability, or translation and affected target protein(s) via binding to lncRNA and mRNA linked to NAFLD.

Indexed as

Non-alcoholic Fatty Liver DiseaseEndoplasmic Reticulum Chaperone BiPHeat-Shock ProteinsHeLa CellsHumansRNA, MessengerEndoplasmic Reticulum Chaperone BiPHeat-Shock ProteinsRNA, Messenger

Identifiers

PMID37156995
PMCPMC10266971
OpenAlexW4375955923

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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.