[HTML][HTML] The mechanism of asparagine endopeptidase in the progression of malignant tumors: a review
W Zhang, Y Lin - Cells, 2021 - mdpi.com
W Zhang, Y Lin
Cells, 2021•mdpi.comAsparagine 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 …
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 …
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.
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