Cells · 2021
The Mechanism of Asparagine Endopeptidase in the Progression of Malignant Tumors: A Review.
СтатьяПоддержка исследования: вне правительства СШАОбзорНазвание и аннотация: Перевод пока не подготовлен
Обработка статьи · этапы, ошибки и управление
Загрузка состояния…
Ошибки и ограничения
История · было → стало
Состояние обновляется каждые 5 секунд, пока блок открыт. Процент показывается только там, где известен объём работы. Пауза останавливает продолжение этапа; текущий запрос к источнику может завершиться.
Zhang Wenrui, Lin Yingying
Аннотация
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.
Предметные рубрики MeSH
AnimalsBreast NeoplasmsCarcinoma, Ovarian EpithelialCatalytic DomainCysteine EndopeptidasesDisease ProgressionExtracellular MatrixFemaleGene Expression Regulation, NeoplasticHumansIntegrin alphaVbeta3Matrix Metalloproteinase 2Matrix Metalloproteinase 9Neoplasm MetastasisOvarian NeoplasmsPeptidesPhosphatidylinositol 3-KinasesRisk FactorsStomach NeoplasmsTumor Suppressor Protein p53Asparaginyl Endopeptidase