Webb7 aug. 2024 · Cathepsin D (CatD) is a soluble aspartic protease that is overexpressed and secreted in high amounts by breast cancer cells [ 1, 2 ]. In primary breast carcinomas, the expression of this protein correlates with tumor progression and metastasis, therefore, it has been proposed as a marker of poor prognosis [ 3 ]. Webb1 sep. 1998 · Cathepsin D trafficking is altered in cancer cells, leading to increased secretion of the pro-enzyme, which can be reinternalized by the same cancer cells and by stromal cells. We studied pro-cathepsin D endocytosis in two human breast cancer cell lines (MDA-MB231, MCF-7) and in human normal fibroblasts. Pro-enzyme uptake was …
Combined exposure to benzo (a - ScienceDirect
Webb12 mars 2024 · ZLDI-8 is a novel inhibitor for Notch activating/cleaving enzyme ADAM-17. In particular, ZLDI-8 inhibits the cleavage of NOTCH protein. ZLDI-8 also decreases the expression of pro-survival and anti-apoptosis regulators, Survivin and cIAP1/2 (known as a cellular inhibitor of apoptosis 1/2), two downstream proteins in the Notch pathway. Webb1 okt. 2010 · Pro-cath-D binds to residues 349-394 of the β chain of LRP1, and is the first ligand of the extracellular domain of LRP1β to be identified. We show that pro-cath-D … grocery walker mn
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Webb10 sep. 2013 · Pagano M, Capony F and Rochefort H: Pro-cathepsin D can activate in vitro pro-cathepsin B secreted by ovarian cancers. C R Acad Sci III. 309:7–12. 1989.(In French). 42. Nishimura Y, Kawabata T, Furuno K and Kato K: Evidence that aspartic proteinase is involved in the proteolytic processing event of procathepsin L in lysosomes. Webb14 apr. 2024 · Combined exposure to benzo(a)pyrene and dibutyl phthalate aggravates pro-inflammatory macrophage polarization in spleen via pyroptosis involving cathepsin B Author links open overlay panel Mingdan You a 1 , Yawen Song a 1 , Jing Chen a 1 , Yining Liu a , Wenyan Chen a , Yanli Cen a , Xiaodeng Zhao b , Zhongfa Tao b , Ganghong Yang c d Webb1 aug. 1993 · In all experiments these antibodies recognized specifically procathepsin D. Procathepsin D from human milk was partially activated at low pH. The activity was monitored using hemoglobin 14C proteolytic assay, and it was abolished by pepstatin A--a specific inhibitor of aspartic proteinases. file link configuration tool