The Mechanism of Asparagine Endopeptidase in the Progression of Malignant Tumors: A Review.
Animals
Breast Neoplasms
/ enzymology
Carcinoma, Ovarian Epithelial
/ enzymology
Catalytic Domain
Cysteine Endopeptidases
/ metabolism
Disease Progression
Extracellular Matrix
/ metabolism
Female
Gene Expression Regulation, Neoplastic
Humans
Integrin alphaVbeta3
/ metabolism
Matrix Metalloproteinase 2
/ metabolism
Matrix Metalloproteinase 9
/ metabolism
Neoplasm Metastasis
Ovarian Neoplasms
/ enzymology
Peptides
/ chemistry
Phosphatidylinositol 3-Kinases
/ metabolism
Risk Factors
Stomach Neoplasms
/ enzymology
Tumor Suppressor Protein p53
/ metabolism
asparagine endopeptidase
breast cancer
epithelial ovarian cancer
gastric cancer
glioblastoma
Journal
Cells
ISSN: 2073-4409
Titre abrégé: Cells
Pays: Switzerland
ID NLM: 101600052
Informations de publication
Date de publication:
10 05 2021
10 05 2021
Historique:
received:
20
03
2021
revised:
24
04
2021
accepted:
07
05
2021
entrez:
2
6
2021
pubmed:
3
6
2021
medline:
3
11
2021
Statut:
epublish
Résumé
Asparagine endopeptidase (AEP), also called legumain, is currently the only known cysteine protease that specifically cleaves peptide bonds in asparaginyl residue in the mammalian genome. Since 2003, AEP has been reported to be widely expressed in a variety of carcinomas and is considered a potential therapeutic target. In the following years, researchers intensively investigated the substrates of AEP and the mechanism of AEP in partial tumors. With the identification of substrate proteins such as P53, integrin αvβ3, MMP-2, and MMP-9, the biochemical mechanism of AEP in carcinomas is also more precise. This review will clarify the probable mechanisms of AEP in the progression of breast carcinoma, glioblastoma, gastric carcinoma, and epithelial ovarian carcinoma. This review will also discuss the feasibility of targeted therapy with AEP inhibitor (AEPI) in these carcinomas.
Identifiants
pubmed: 34068767
pii: cells10051153
doi: 10.3390/cells10051153
pmc: PMC8151911
pii:
doi:
Substances chimiques
Integrin alphaVbeta3
0
Peptides
0
TP53 protein, human
0
Tumor Suppressor Protein p53
0
Cysteine Endopeptidases
EC 3.4.22.-
asparaginylendopeptidase
EC 3.4.22.34
MMP2 protein, human
EC 3.4.24.24
Matrix Metalloproteinase 2
EC 3.4.24.24
MMP9 protein, human
EC 3.4.24.35
Matrix Metalloproteinase 9
EC 3.4.24.35
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Review
Langues
eng
Sous-ensembles de citation
IM
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