Evidence map›Paper›PMID 32678070›Full record

ArticleAging2020

Acetylation-mediated degradation of HSD17B4 regulates the progression of prostate cancer.

Huichao Huang, Ruijie Liu, Yahui Huang, Yilu Feng, Ying Fu, Lin Chen, Zhuchu Chen, Yi Cai, Ye Zhang, Yongheng Chen

Open access · greenAbstract read
In one paragraph

Article in Aging, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.3field-weighted citation impact, top 22% 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

18 citing papers in PubMed, 22 citations in OpenAlex.

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  13. Effects of High-Fat Diet on Cardiovascular Protein Expression in Mice Based on Proteomics.Diabetes, metabolic syndrome and obesity : targets and therapy · 2023
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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

10 authors at 4 institutions in 2 countries.

Huichao HuangDepartment of Oncology, NHC Key Laboratory of Cancer Proteomics, XiangYa Hospital, Central South University, Changsha 410008, China.
Ruijie LiuDepartment of Oncology, NHC Key Laboratory of Cancer Proteomics, XiangYa Hospital, Central South University, Changsha 410008, China.
Yahui HuangDepartment of Pathology, XuChang Central Hospital, XuChang 461670, China.
Yilu FengDepartment of Oncology, NHC Key Laboratory of Cancer Proteomics, XiangYa Hospital, Central South University, Changsha 410008, China.
Ying FuDepartment of Oncology, NHC Key Laboratory of Cancer Proteomics, XiangYa Hospital, Central South University, Changsha 410008, China.
Lin ChenMolecular and Computational Biology Program, Departments of Biological Sciences and Chemistry, University of Southern California, Los Angeles, CA 90089, USA.
Zhuchu ChenDepartment of Oncology, NHC Key Laboratory of Cancer Proteomics, XiangYa Hospital, Central South University, Changsha 410008, China.
Yi CaiDepartment of Urology, XiangYa Hospital, Central South University, Changsha 410008, China.
Ye ZhangDepartment of Oncology, NHC Key Laboratory of Cancer Proteomics, XiangYa Hospital, Central South University, Changsha 410008, China.
Yongheng ChenDepartment of Oncology, NHC Key Laboratory of Cancer Proteomics, XiangYa Hospital, Central South University, Changsha 410008, China.
Central South University · CNXiangya Hospital Central South University · CNUniversity of Southern California · USXuzhou Central Hospital · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Steroidogenic enzymes are crucial in prostate cancer (PCa) progression. 17β-Hydroxysteroid dehydrogenase type 4 (HSD17B4), encoded by HSD17B4, lacks catalytic capacity in androgen metabolism. Now the detailed role and molecular mechanism of PCa development are largely unknown. Here we showed that the expression of HSD17B4 was increased in PCa tissues compared to paired paratumor tissues. HSD17B4 knockdown in PCa cells significantly suppressed its proliferation, migration and invasion, while overexpressing HSD17B4 had opposite effects. Mechanistically, we found that the protein level of HSD17B4 was regulated by its acetylation at lysine 669(K669). Dihydroxytestosterone (DHT) treatment increased HSD17B4 acetylation and then promoted its degradation via chaperone-mediated autophagy (CMA). SIRT3 directly interacted with HSD17B4 to inhibit its acetylation and enhance its stability. In addition, we identified CREBBP as a regulator of the K669 acetylation and degradation of HSD17B4, affecting PC cell proliferation, migration and invasion. Notably, in PCa tissues and paired paratumor tissues, the level of HSD17B4 was negatively correlated with its K669 acetylation. Taken together, this study identified a novel role of HSD17B4 in PCa progression and suggested that HSD17B4 and its upstream regulators may be potential therapeutic targets for PCa intervention.

Indexed as

AcetylationAnimalsCell Line, TumorCell MovementCell ProliferationCREB-Binding ProteinDisease ProgressionGene Expression Regulation, NeoplasticGene Knockdown TechniquesHumansLysineMaleMiceMice, KnockoutNeoplasm InvasivenessPeroxisomal Multifunctional Protein-2CREB-Binding ProteinCREBBP protein, humanHSD17B4 protein, humanLysinePeroxisomal Multifunctional Protein-2Sirt3 protein, mouseSirtuin 3Testosterone17β-Hydroxysteroid dehydrogenase type 4 (HSD17B4)acetylationchaperone-mediated autophagyprostate cancersteroidogenic enzymes

Identifiers

PMID32678070
PMCPMC7425433
OpenAlexW3043242106

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.