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Appears in Networks 1

In-Edges 3

act(a(CHEBI:Thrombin)) causesNoChange p(HGNC:MAPT, frag("561_685")) View Subject | View Object

Evidence supporting a role for thrombin in tau proteolysis came initially from an in vitro study showing that thrombin degraded recombinant full-length tau from the N-terminus yielding a 25-kDa fragment, while preserving the microtubule binding repeat domain (13). PubMed:24027553

act(a(CHEBI:Thrombin)) increases deg(p(HGNC:MAPT, frag("561_685"))) View Subject | View Object

A later study, however, showed that in N2a neuroblastoma cells expressing a construct of only the tau repeat domain, thrombin cleavage could still occur, indicating additional cleavage sites (15). Similar results were observed in an in vitro assay (15). PubMed:24027553

Out-Edges 2

deg(p(HGNC:MAPT, frag("561_685"))) increases a(HBP:"Tau aggregates") View Subject | View Object

Thrombin cleavage of the repeat domain construct yielded fragments that rapidly aggregated, which closely correlated with toxicity in cell culture (15). These fragments can also induce the aggregation of full-length tau (39). PubMed:24027553

p(HGNC:MAPT, frag("561_685")) increases a(HBP:"Tau aggregates") View Subject | View Object

Overexpressing only the repeat domain of tau containing an FTDP-17 mutation in neuroblastoma cells leads to tau aggregation as well as the appearance of smaller proteolytic fragments. Using the autophagy inhibitor 3-methyladenine (3-MA) to block the formation of autophagosomes led to an increase in both soluble and insoluble tau (94). PubMed:24027553


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If you find BEL Commons useful in your work, please consider citing: Hoyt, C. T., Domingo-Fernández, D., & Hofmann-Apitius, M. (2018). BEL Commons: an environment for exploration and analysis of networks encoded in Biological Expression Language. Database, 2018(3), 1–11.