Results 181 to 190 of about 27,826 (225)

Regulation of α- and β-secretase activity by oxysterols: Cerebrosterol stimulates processing of APP via the α-secretase pathway

Biochemical and Biophysical Research Communications, 2007
The cholesterol 24-hydroxylase encoded by the gene CYP46 is expressed almost exclusively in central nervous system (CNS) neurons and catalyzes the formation of 24S-hydroxycholesterol (24S-OHC) from cholesterol. This conversion corresponds to a major pathway for excretion of excess cholesterol from the brain.
D, Famer, S, Meaney, M, Mousavi, A, Nordberg, I, Björkhem, M, Crisby   +5 more
openaire   +2 more sources

The alpha secretase ADAM10: A metalloprotease with multiple functions in the brain

Progress in Neurobiology, 2015
Proteins belonging to the 'A Disintegrin And Metalloproteinase' (ADAM) family are membrane-anchored proteases that are able to cleave the extracellular domains of several membrane-bound proteins in a process known as 'ectodomain shedding'. In the central nervous system, ADAM10 has attracted the most attention, since it was described as the amyloid ...
Saftig, Paul, Lichtenthaler, Stefan
openaire   +2 more sources

α-Secretase Activation – An Approach to Alzheimer’s Disease Therapy

Neurodegenerative Diseases, 2006
The nonamyloidogenic pathway of processing the amyloid precursor protein (APP) involves the cleavage within the amyloid-β peptide sequence, and thus precludes amyloid-β formation. The identification of a member of the disintegrin and metalloproteinase family, ADAM10, as an α-secretase that prevents plaque formation and hippocampal deficits in vivo gave
Falk, Fahrenholz, Rolf, Postina
openaire   +2 more sources

ADAMs family members as amyloid precursor protein α‐secretases

Journal of Neuroscience Research, 2003
AbstractIn the non‐amyloidogenic pathway, the Alzheimer's amyloid precursor protein (APP) is cleaved within the amyloid‐β domain by α‐secretase precluding deposition of intact amyloid‐β peptide. The large ectodomain released from the cell surface by the action of α‐secretase has several neuroprotective properties.
Allinson, Tobias M. J., Parkin, Edward T., Turner, Anthony J., Hooper, Nigel M.   +3 more
openaire   +2 more sources

Levels of beta-secretase BACE and alpha-secretase ADAM10 mRNAs in Alzheimer hippocampus.

Neuroreport, 2002
The amyloid cascade hypothesis suggests that amyloid precursor protein (APP) proteolytic processing is a key event in the pathogenesis of Alzheimer's disease (AD). The enzymes beta-site APP cleaving enzyme (BACE) and A disintegrin and metalloproteinase 10 (ADAM10) play an important role in APP proteolysis.
GATTA LB, ALBERTINI A, RAVID R, FINAZZI, Dario   +3 more
openaire   +2 more sources

gamma-Secretase can cleave amyloid precursor protein fragments independent of alpha- and beta-secretase pre-cutting.

International journal of molecular medicine, 2004
Abeta is the major component of amyloid in the brain in Alzheimer's disease and is derived from an amyloid precursor protein (APP) by the sequential proteolytic processing of two putative proteases, called beta- and gamma-secretase. To clarify the mechanism of gamma-secretase processing, we created constructs contained the C-terminal domain of APP and ...
Hideaki, Kume, Yoshiki, Sekijima, Kei, Maruyama, Fuyuki, Kametani   +3 more
openaire   +1 more source

Iron Levels Modulate α‐Secretase Cleavage of Amyloid Precursor Protein

Journal of Neurochemistry, 1995
Abstract: The amyloid precursor protein (APP) is a membrane‐spanning glycoprotein that is the source of βA4 peptides, which aggregate in Alzheimer's disease to form senile plaques. APP is cleaved within the βA4 sequence to release a soluble N‐terminal derivative (APPsol), which has a wide range of trophic and protective functions.
S, Bodovitz, M T, Falduto, D E, Frail, W L, Klein   +3 more
openaire   +2 more sources

Putative function of ADAM9, ADAM10, and ADAM17 as APP -secretase

Biochemical and Biophysical Research Communications, 2003
The putative alpha-secretase cleaves the amyloid precursor protein (APP) of Alzheimer's disease in the middle of the amyloid beta peptide (Abeta) domain. It is generally thought that the alpha-secretase pathway mitigates Abeta formation in the normal brain.
Masashi, Asai, Chinatsu, Hattori, Beáta, Szabó, Noboru, Sasagawa, Kei, Maruyama, Sei-ichi, Tanuma, Shoichi, Ishiura   +6 more
openaire   +2 more sources

Genetics and pathology of alpha-secretase site AβPP mutations in the understanding of Alzheimer's disease

Journal of Alzheimer's Disease, 2006
Development of therapeutics begins with delineating the precise disease pathology along with a reasonable understanding of the sequence of events responsible for the development of disease, or disease pathogenesis. For Alzheimer's disease (AD), the classical pathology is now known for quite some time; however, the disease pathogenesis has eluded our ...
Van Broeckhoven, Christine, Kumar-Singh, Samir   +1 more
openaire   +3 more sources

Cryptotanshinione upregulates α-secretase by activation PI3K pathway in cortical neurons

Brain Research, 2010
The amyloid precursor protein (APP) is cleaved enzymatically by nonamyloidogenic and amyloidogenic pathways. alpha-Secretase cleaves APP within beta amyloid protein (Abeta) sequence, resulting in the release of a secreted fragment of APP (sAPPalpha) and precluding Abeta generation.
Zhengrong, Mei, Bing, Situ, Xiangping, Tan, Shiming, Zheng, Fangyan, Zhang, Pengke, Yan, Peiqing, Liu   +6 more
openaire   +2 more sources