Department of Neurosurgery, Ren Ji Hospital, School of Medicine, Shanghai JiaoTong University, Shanghai 200127, China.
Cells. 2021 May 10;10(5):1153. doi: 10.3390/cells10051153.
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.
天冬酰胺内肽酶（AEP），也称为凝乳蛋白酶，是目前唯一已知的特异性切割哺乳动物基因组中天冬酰胺残基肽键的半胱氨酸蛋白酶。自 2003 年以来，AEP 已被报道广泛表达于多种癌中，被认为是一种潜在的治疗靶点。在随后的几年中，研究人员深入研究了 AEP 的底物和 AEP 在部分肿瘤中的作用机制。随着 P53、整合素 αvβ3、MMP-2 和 MMP-9 等底物蛋白的鉴定，AEP 在癌中的生化机制也更加精确。本综述将阐明 AEP 在乳腺癌、神经胶质瘤、胃癌和上皮性卵巢癌进展中的可能机制。本综述还将讨论针对这些癌中 AEP 抑制剂（AEPI）的靶向治疗的可行性。
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