Low cholesterol stimulates the nonamyloidogenic pathway by its effect on the α-secretase ADAM 10

By E. Kojro, G. Gimpl, S. Lammich, Winfried März, F. Fahrenholz. Proceedings of the National Academy of Sciences of the United States of America, 2001

752 citations recorded by the source corpus.

Subfields: Molecular Biology, Physiology

View Paper: https://www.semanticscholar.org/paper/ff73bbf64add5d945685ee5a08695ad60513d71a

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Citations in the corpus

The ADAMs family of metalloproteases: multidomain proteins with multiple functions. (2003, background): “This has also been shown for ADAM10-dependent processing of amyloid precursor protein (Kojro et al. 2001).”
Trafficking and proteolytic processing of APP. (2012, background): “Lowering cholesterol levels in cultured cells stimulates a-secretase cleavage of APP through mechanisms involving impaired APP endocytosis and increased steadystate levels of ADAM10 (Kojro et al. 2001).”
Amyloidogenic processing of the Alzheimer β-amyloid precursor protein depends on lipid rafts (2003, background): “As expected from results of Kojro et al. (2001), the soluble ectodomain generated by -cleavage was also strongly increased in cholesterol-depleted cells.”
The disintegrin/metalloprotease ADAM 10 is essential for Notch signalling but not for alpha-secretase activity in fibroblasts. (2002, background): “In contrast to previous in vitro studies that clearly favored ADAM 10 as a major a-secretase (30,31,35) responsible for both constitutive and regulated a-cleavage, both fractions of a-secretase activity were preserved in the majority of the ADAM 10-deficient cell lines (albeit at a less constant lev”