期刊
NEUROBIOLOGY OF DISEASE
卷 36, 期 2, 页码 233-241出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.nbd.2009.07.015
关键词
alpha-Secretase; Shedding; Prion disease; Neurotoxicity; Gliosis
资金
- Federal Ministry of Education and Research (BMBF)
- Forderkennzeichen [FKZ01GS08130]
Both the cellular prion protein (PrP(c)) and the amyloid precursor protein (APP) are physiologically subjected to complex proteolytic processing events. While for APP the proteinases involved - alpha-, beta- and gamma-secretase - have been identified in vitro and in vivo, the cleavage of PrPc by now has been linked only to the shedding activity of the metalloproteinase ADAM10 and/or ADAM17 in cell culture. Here we show that neuronal overexpression of the alpha-secretase ADAM10 in mice reduces all PrP(c) species detected in the brain instead of leading to enhanced amounts of specific cleavage products of PrP(c). Additionally, the incubation time of mice after scrapie infection is significantly increased in mice moderately overexpressing ADAM10. This indicates that overexpression of ADAM10 rather influences the amount of the cellular prion protein than its processing in vivo. (C) 2009 Elsevier Inc. All rights reserved.
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