Evidence map›Paper›PMID 39878157›Full record

ArticleCancer biology & therapy2025

Caspase 3-specific cleavage of ubiquitin-specific peptidase 48 enhances drug-induced apoptosis in AML.

Zhanglin Zhang, Xiang Lin, Yaling Yang, Xuemei Wang, Yi Wang, Xianbao Huang, Miao Hong, Wei Gao, Hua He, M James You and 2 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Cancer biology & therapy, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. 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

12 authors.

Zhanglin ZhangNational & Local Joint Engineering Research Center of Biodiagnosis and Biotherapy, Department of Hematology, Precision Medical Institute, The Second Affiliated Hospital of Xi'an Jiaotong University, Xi'an, Shaanxi, China.ORCID 0000-0001-8720-8266
Xiang LinDepartments of Blood Transfusion, Institute of Transfusion, Jiangxi Key Laboratory of Transfusion, The First Affiliated Hospital, Jiangxi Medical College, Nanchang University, Nanchang, China.
Yaling YangDepartment of Hematopathology, The University of Texas, MD Anderson Cancer Center, Houston, TX, USA.
Xuemei WangDepartments of Blood Transfusion, Institute of Transfusion, Jiangxi Key Laboratory of Transfusion, The First Affiliated Hospital, Jiangxi Medical College, Nanchang University, Nanchang, China.
Yi WangDepartment of Hematopathology, The University of Texas, MD Anderson Cancer Center, Houston, TX, USA.
Xianbao HuangDepartment of Hematology, The First Affiliated Hospital, Jiangxi Medical College, Nanchang University, Nanchang, China.
Miao HongDepartments of Blood Transfusion, Institute of Transfusion, Jiangxi Key Laboratory of Transfusion, The First Affiliated Hospital, Jiangxi Medical College, Nanchang University, Nanchang, China.
Wei GaoDepartment of Hematopathology, The University of Texas, MD Anderson Cancer Center, Houston, TX, USA.
Hua HeDepartment of Hematopathology, The University of Texas, MD Anderson Cancer Center, Houston, TX, USA.
M James YouDepartment of Hematopathology, The University of Texas, MD Anderson Cancer Center, Houston, TX, USA.
Yi YangNational & Local Joint Engineering Research Center of Biodiagnosis and Biotherapy, Department of Hematology, Precision Medical Institute, The Second Affiliated Hospital of Xi'an Jiaotong University, Xi'an, Shaanxi, China.
Guangyao KongNational & Local Joint Engineering Research Center of Biodiagnosis and Biotherapy, Department of Hematology, Precision Medical Institute, The Second Affiliated Hospital of Xi'an Jiaotong University, Xi'an, Shaanxi, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Dysfunction or dysregulation of deubiquitination is closely related to the initiation and development of multiple cancers. Targeted regulation of deubiquitination has been recognized as an important strategy in tumor therapy. However, the mechanism by which drugs regulate deubiquitinase is not clear. Here, we identified ubiquitin-specific peptidase 48 (USP48), a member of the ubiquitin-specific protease family highly expressed in various tumors, as a specific substrate for the activated caspase-3. During drug induced apoptosis of AML cells, activated caspase-3 cleaves USP48 through recognizing the conservative motif DEQD located at 611-614 sites of human USP48. Subsequent analysis showed that the cleavage USP48 N-terminal fragment which contains catalytic active domain is easily degraded by ubiquitination. Meanwhile knockdown experiment showed that inhibiting the expression of USP48 could also promotes apoptosis and enhance the efficacy of chemotherapy drugs. Altogether, these results suggest that targeting USP48 may represent a novel therapeutic strategy in AML.

Indexed as

Antineoplastic AgentsApoptosisCaspase 3Leukemia, Myeloid, AcuteUbiquitin-Specific ProteasesCell Line, TumorHumansUbiquitinationAntineoplastic AgentsCaspase 3Ubiquitin-Specific ProteasesAMLapoptosiscaspase 3deubiquitinationUSP48

Identifiers

PMID39878157
PMCPMC11781246

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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.