Evidence map›Paper›PMID 38758542›Full record

ArticleMolecular and cellular biology2024

Deactivation of the Unfolded Protein Response Aggravated Renal AA Amyloidosis in HSF1 Deficiency Mice.

Wei Liu, Shunjie Xia, Fang Yao, Jia Huo, Junqiao Qian, Xiaomeng Liu, Langning Bai, Yu Song, Jinze Qian

Abstract read
In one paragraph

Article in Molecular and cellular biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

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2citing papers in PubMed
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1 · What the graph read from it

What it found

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2 · The registry

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3 · Its place in the literature

Who cites it

2 citing papers in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

9 authors.

Wei LiuDepartment of Pathology, Key Laboratory of Kidney Diseases of Hebei Province, Hebei Medical University, Shijiazhuang, China.ORCID 0009-0001-4084-3542
Shunjie XiaDepartment of Pathology, Key Laboratory of Kidney Diseases of Hebei Province, Hebei Medical University, Shijiazhuang, China.
Fang YaoDepartment of Pathology, Key Laboratory of Kidney Diseases of Hebei Province, Hebei Medical University, Shijiazhuang, China.ORCID 0000-0002-7272-9138
Jia HuoDepartment of Osteopathy, Third Hospital of Hebei Medical University, Shijiazhuang, China.ORCID 0000-0002-2392-6936
Junqiao QianDepartment of Oral Surgery, Hebei Key Laboratory of Stomatology, Hebei Clinical Research Center for Oral Diseases, School and Hospital of Stomatology, Hebei Medical University, Shijiazhuang, China.
Xiaomeng LiuDepartment of Pathology, Key Laboratory of Kidney Diseases of Hebei Province, Hebei Medical University, Shijiazhuang, China.
Langning BaiDepartment of Pathology, Key Laboratory of Kidney Diseases of Hebei Province, Hebei Medical University, Shijiazhuang, China.
Yu SongDepartment of Biochemistry, Hebei Medical University, Shijiazhuang, China.
Jinze QianDepartment of Pathology, Key Laboratory of Kidney Diseases of Hebei Province, Hebei Medical University, Shijiazhuang, China.ORCID 0000-0002-7260-8985

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Systemic amyloid A (AA) amyloidosis, which is considered the second most common form of systemic amyloidosis usually takes place several years prior to the occurrence of chronic inflammation, generally involving the kidney. Activated HSF1, which alleviated unfolded protein response (UPR) or enhanced HSR, is the potential therapeutic target of many diseases. However, the effect of HSF1 on AA amyloidosis remains unclear. This study focused on evaluating effect of HSF1 on AA amyloidosis based on HSF1 knockout mice. As a result, aggravated amyloid deposits and renal dysfunction have been found in HSF1 knockout mice. In progressive AA amyloidosis, HSF1 deficiency enhances serum amyloid A production might to lead to severe AA amyloid deposition in mice, which may be related to deactivated unfolded protein response as well as enhanced inflammation. Thus, HSF1 plays a significant role on UPR related pathway impacting AA amyloid deposition, which can mitigate amyloidogenic proteins from aggregation pathologically and is the possible way for intervening with the pathology of systemic amyloid disorder. In conclusion, HSF1 could not only serve as a new target for AA amyloidosis treatment in the future, but HSF1 knockout mice also can be considered as a valuable novel animal model for renal AA amyloidosis.

Indexed as

AmyloidosisHeat Shock Transcription FactorsKidneyMice, KnockoutUnfolded Protein ResponseAnimalsDisease Models, AnimalKidney DiseasesMiceMice, Inbred C57BLSerum Amyloid A ProteinHeat Shock Transcription FactorsHsf1 protein, mouseSerum Amyloid A ProteinAA amyloidosisHSF1 deficiencymice modelmicroarrayunfolded protein response

Identifiers

PMID38758542
PMCPMC11123510

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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.