Unknown

Dataset Information

0

EGCG functions through estrogen receptor-mediated activation of ADAM10 in the promotion of non-amyloidogenic processing of APP.

ABSTRACT: Estrogen depletion following menopause has been correlated with an increased risk of developing Alzheimer's disease (AD). We previously explored the beneficial effect of (-)-epigallocatechin-3-gallate (EGCG) on AD mice and found increased non-amyloidogenic processing of amyloid precursor protein (APP) through the ?-secretase a disintegrin and metallopeptidase domain 10 (ADAM10). Our results in this study suggest that EGCG-mediated enhancement of non-amyloidogenic processing of APP is mediated by the maturation of ADAM10 via an estrogen receptor-? (ER?)/phosphoinositide 3-kinase/Ak-transforming dependent mechanism, independent of furin-mediated ADAM10 activation. These data support prior assertions that central selective ER modulation could be a therapeutic target for AD and support the use of EGCG as a well-tolerated alternative to estrogen therapy in the prophylaxis and treatment of this disease.

SUBMITTER: Fernandez JW 

PROVIDER: S-EPMC2981607 | biostudies-literature | 2010 Oct

REPOSITORIES: biostudies-literature

Json Xml
altmetric image

Publications

EGCG functions through estrogen receptor-mediated activation of ADAM10 in the promotion of non-amyloidogenic processing of APP.

Fernandez Jamie Winderbaum JW   Rezai-Zadeh Kavon K   Obregon Demian D   Tan Jun J  

FEBS letters 20100917 19

Estrogen depletion following menopause has been correlated with an increased risk of developing Alzheimer's disease (AD). We previously explored the beneficial effect of (-)-epigallocatechin-3-gallate (EGCG) on AD mice and found increased non-amyloidogenic processing of amyloid precursor protein (APP) through the α-secretase a disintegrin and metallopeptidase domain 10 (ADAM10). Our results in this study suggest that EGCG-mediated enhancement of non-amyloidogenic processing of APP is mediated by  ...[more]

Similar Datasets

Unknown Targeting Amyloidogenic Processing of APP in Alzheimer's Disease.
| S-EPMC7418514 | biostudies-literature
Unknown 5-HT4 receptors constitutively promote the non-amyloidogenic pathway of APP cleavage and interact with ADAM10.
| S-EPMC3547471 | biostudies-literature
Unknown Increased amyloidogenic processing of transgenic human APP in X11-like deficient mouse brain.
| S-EPMC2949864 | biostudies-other
Unknown Increased amyloidogenic APP processing in APOE ɛ4-negative individuals with cerebral β-amyloidosis.
| S-EPMC4786682 | biostudies-other
Unknown Complex formation of APP with GABAB receptors links axonal trafficking to amyloidogenic processing.
| S-EPMC6430795 | biostudies-literature
Unknown Pharmacological Inhibition of Amyloidogenic APP Processing and Knock-Down of APP in Primary Human Macrophages Impairs the Secretion of Cytokines.
| S-EPMC7494750 | biostudies-literature
Unknown C-terminal 37 residues of LRP promote the amyloidogenic processing of APP independent of FE65.
| S-EPMC2864086 | biostudies-literature
Proteomics Complex formation of APP with GABAB receptors links axonal trafficking to amyloidogenic processing
2019-11-13 | PXD012487 | Pride
Unknown Role of RanBP9 on amyloidogenic processing of APP and synaptic protein levels in the mouse brain.
| S-EPMC3336780 | biostudies-literature
Unknown Involvement of receptor tyrosine kinase Tyro3 in amyloidogenic APP processing and ?-amyloid deposition in Alzheimer's disease models.
| S-EPMC3372537 | biostudies-literature