A disintegrin-metalloproteinase prevents amyloid plaque formation and hippocampal defects in an Alzheimer disease mouse model.

By R. Postina, Anja Schroeder, I. Dewachter, J. Bohl, U. Schmitt, E. Kojro, Claudia Prinzen, K. Endres, C. Hiemke, M. Blessing and 5 more. Journal of Clinical Investigation, 2004

642 citations recorded by the source corpus.

Subfields: Molecular Biology, Pharmacology, Physiology

View Paper: https://www.semanticscholar.org/paper/d693ffcbd012393ade6725277207dbdef14d34dc

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Citations in the corpus

Trafficking and proteolytic processing of APP. (2012, background): “Thus, up-regulation of a-secretase activity to promote anti-amyloidogenic processing of APP is potentially of therapeutic value (Postina et al. 2004).”
Animal models of Alzheimer's disease and frontotemporal dementia (2008, background): “Expression of the α-secretase ADAM10 in APP transgenic mice also reduced Aβ formation, ameliorated behavioural deficits and enhanced LTP impairment, providing in vivo evidence for ADAM10 as a functional α-secretas”
Ionizing radiation reduces ADAM10 expression in brain microvascular endothelial cells undergoing stress-induced senescence (2017, background): “In contrast, www.aging‐us.com 1256 AGING BACE-1 cleavage of APP results in the eventual production of toxic Aβ peptides.”
An Overview of APP Processing Enzymes and Products (2010, positive): “However, in a mouse model of AD ADAM 10 overexpression has been shown to reduce Aβ production and plaque deposition in addition to lessening cognitive deficits (Postina et al., 2004).”
Amyloid Precursor Protein Processing and Alzheimer’s Disease (2011, background): “Indeed, increased expression of ADAM 10 or SIRT1, a regulator of ADAM 10 gene expression, in a mouse model of AD significantly attenuated Aβ deposition and cognitive deficits (Donmez et al. 2010; Postina et al. 2004).”
The ADAM metalloproteinases (2008, background): “However, overexpression of functional ADAM-10 in neurons in transgenic mice that also overexpress human APP led to increased production of APPsa and reduced amyloid plaque formation and overall cognitive deficits (Postina et al., 2004) .”
ADAMs as mediators of EGF receptor transactivation by G protein-coupled receptors. (2006, background): “Furthermore, it was reported that in ADAM10 transgenic mice, the formation of amyloid -peptide is reduced and their deposition in plaques was prevented (78), suggesting a protective effect of ADAMs activated by GPCRs against Alzheimer’s disease.”
The disintegrin/metalloproteinase ADAM10 is essential for the establishment of the brain cortex (2010, background): “Overexpression of ADAM10 in an Alzheimer’s mouse model resulted in a decrease in -amyloid deposition and cognitive deficits (Postina et al., 2004) but since transgenic overexpression of proteins creates a highly unphysiological situation, formal proof that ADAM10 is the crucial neuronal -secretase…”
ADAM10 is the physiologically relevant, constitutive α‐secretase of the amyloid precursor protein in primary neurons (2010, background): “In fact, a lack of competition between constitutive a- and b-secretase cleavage in the adult brain comes from a study, where a dominant-negative ADAM10 mutant decreased APPsa, but did not alter APPsb levels in a transgenic mouse brain (Postina et al, 2004).”