Skip to content
DraconiticResearch
Search Sources API
201,818 studies31 sourcesUpdated 6 min ago
Peer-reviewedCC BY 4.0Frontiers in Cell and Developmental Biology

Emerging roles and mechanistic insights of ASRGL1 in tumorigenesis and cancer progression

5 affiliations
  1. 1Changzhou Medical Center, Nanjing Medical University, Changzhou, Jiangsu, China
  2. 2Department of Tumor Biological Treatment, The Third Affiliated Hospital of Soochow University, Changzhou, Jiangsu, China
  3. 3Jiangsu Engineering Research Center for Tumor Immunotherapy, The Third Affiliated Hospital of Soochow University, Changzhou, Jiangsu, China
  4. 4Institute of Cell Therapy, Soochow University, Jiangsu, Changzhou, China
  5. 5The First People’s Hospital of Changzhou, Changzhou, Jiangsu, China

Abstract

Asparaginase and isoaspartyl peptidase 1 (ASRGL1), also known as ALP, CRASH, hASNase3, is a protein encoded by the ASRGL1 gene located at chromosome 11q12.3 in humans. It belongs to the N-terminal nucleophilic (Ntn) hydrolase superfamily and catalyzes the hydrolysis of L-asparagine and isoaspartyl dipeptides, thereby participating in amino acid metabolism and protein homeostasis regulation. In recent years, accumulating evidence has shown that ASRGL1 is aberrantly expressed in multiple human cancers, however, its biological and prognostic implications vary substantially among tumor types and are highly tumor-context dependent. This review systematically summarizes the structure and function of ASRGL1, its expression patterns and clinical relevance, the reported functional roles and proposed mechanisms in tumorigenesis and progression, and discusses its potential as a candidate biomarker for clinical prognosis prediction.

Related

  1. Mitochondria as Key Players in Sarcoma Development, Progression and Drug Resistance: From Mechanistic Insights to New Treatment Opportunities
    Martina Perin, Alberto Lipani, Marco Loffa +3
    BiomoleculesPeer-reviewedCC BY 4.0Full textMolecular biology & gene regulationCrossrefEurope PMC
  2. Mechanistic insights into ENO2-driven glycolysis and tumor progression in hepatocellular carcinoma
    Yan Liu, Xiao-Ran Zhang, Li Dai +5
    PLOS OnePeer-reviewedCC BY 4.0Full textEnzymology & metabolismMolecular biology & gene regulationPLOSPMC
  3. Progress in research on gut microbiota regulation of tumorigenesis, progression, and therapeutic response via inflammatory cytokines
    Yan Liu, Dan Zang, Jun Chen
    Frontiers in ImmunologyPeer-reviewedCC BY 4.0Full textMolecular biology & gene regulationPMCCrossrefEurope PMC
  4. Exercise oncology and tumor sterol metabolism: An emerging mechanistic frontier
    Marc Poirot, Philippe de Médina, Sandrine Silvente-Poirot
    Journal of Sport and Health SciencePeer-reviewedCC BY-NC-ND 4.0Full textGeneral biochemistryCell biologyHAL
  5. Epigenetic plasticity in cancer drug resistance: mechanistic insights and strategies for therapeutic intervention
    Wei Zhao, Jing-xuan Pan
    Acta Pharmacologica SinicaPeer-reviewedLicence not statedFull text1 citedMolecular biology & gene regulationPMC
BibTeX
@article{zeng2026emerging,
  title = {{Emerging roles and mechanistic insights of ASRGL1 in tumorigenesis and cancer progression}},
  author = {Huiping Zeng and Zekang Li and Renhao Geng and Lujun Chen},
  journal = {Frontiers in Cell and Developmental Biology},
  year = {2026},
  month = oct,
  doi = {10.3389/fcell.2026.1955895},
  url = {https://doi.org/10.3389/fcell.2026.1955895},
  note = {CC BY 4.0},
}
RIS
TY  - JOUR
TI  - Emerging roles and mechanistic insights of ASRGL1 in tumorigenesis and cancer progression
AU  - Huiping Zeng
AU  - Zekang Li
AU  - Renhao Geng
AU  - Lujun Chen
PY  - 2026
DA  - 2026/10/21
JO  - Frontiers in Cell and Developmental Biology
DO  - 10.3389/fcell.2026.1955895
UR  - https://doi.org/10.3389/fcell.2026.1955895
AB  - Asparaginase and isoaspartyl peptidase 1 (ASRGL1), also known as ALP, CRASH, hASNase3, is a protein encoded by the ASRGL1 gene located at chromosome 11q12.3 in humans. It belongs to the N-terminal nucleophilic (Ntn) hydrolase superfamily and catalyzes the hydrolysis of L-asparagine and isoaspartyl dipeptides, thereby participating in amino acid metabolism and protein homeostasis regulation. In recent years, accumulating evidence has shown that ASRGL1 is aberrantly expressed in multiple human cancers, however, its biological and prognostic implications vary substantially among tumor types and are highly tumor-context dependent. This review systematically summarizes the structure and function of ASRGL1, its expression patterns and clinical relevance, the reported functional roles and proposed mechanisms in tumorigenesis and progression, and discusses its potential as a candidate biomarker for clinical prognosis prediction.
SN  - 2296-634X
ER  -