Putative function of ADAM9, ADAM10, and ADAM17 as APP alpha-secretase
- PMID: 12535668
- DOI: 10.1016/s0006-291x(02)02999-6
Putative function of ADAM9, ADAM10, and ADAM17 as APP alpha-secretase
Abstract
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. Several studies have suggested that ADAM9, ADAM10, and ADAM17 are candidate alpha-secretases belonging to the ADAM (a disintegrin and metalloprotease) family, which are membrane-anchored cell surface proteins. In this comparative study of ADAM9, ADAM10, and ADAM17, we examined the physiological role of ADAMs by expressing these ADAMs in COS-7 cells, and both "constitutive" and "regulated" alpha-secretase activities of these ADAMs were determined. We tried to suppress the expression of these ADAMs in human glioblastoma A172 cells, which contain large amounts of endogenous alpha-secretase, by lipofection of the double-stranded RNA (dsRNA) encoding each of these ADAMs. The results indicate that ADAM9, ADAM10, and ADAM17 catalyze alpha-secretory cleavage and therefore act as alpha-secretases in A172 cells. This is the first report that to suggest the endogenous alpha-secretase is composed of several ADAM enzymes.
Similar articles
-
ADAMs family members as amyloid precursor protein alpha-secretases.J Neurosci Res. 2003 Nov 1;74(3):342-52. doi: 10.1002/jnr.10737. J Neurosci Res. 2003. PMID: 14598310 Review.
-
Enhancement of alpha-secretase cleavage of amyloid precursor protein by a metalloendopeptidase nardilysin.J Neurochem. 2007 Sep;102(5):1595-1605. doi: 10.1111/j.1471-4159.2007.04685.x. Epub 2007 Jun 7. J Neurochem. 2007. PMID: 17555553
-
A secreted form of human ADAM9 has an alpha-secretase activity for APP.Biochem Biophys Res Commun. 2002 May 3;293(2):800-5. doi: 10.1016/S0006-291X(02)00302-9. Biochem Biophys Res Commun. 2002. PMID: 12054541
-
Coordinated expression of beta-amyloid precursor protein and the putative beta-secretase BACE and alpha-secretase ADAM10 in mouse and human brain.J Neurochem. 2000 Nov;75(5):2133-43. doi: 10.1046/j.1471-4159.2000.0752133.x. J Neurochem. 2000. PMID: 11032903
-
The search for alpha-secretase and its potential as a therapeutic approach to Alzheimer s disease.Curr Med Chem. 2002 Jun;9(11):1107-19. doi: 10.2174/0929867023370121. Curr Med Chem. 2002. PMID: 12052175 Review.
Cited by
-
Persistent inflammation and neuronal loss in the mouse brain induced by a modified form of attenuated herpes simplex virus type I.Virol Sin. 2023 Feb;38(1):108-118. doi: 10.1016/j.virs.2022.11.008. Epub 2022 Nov 24. Virol Sin. 2023. PMID: 36436797 Free PMC article.
-
The Notch ligand Delta1 is sequentially cleaved by an ADAM protease and gamma-secretase.Proc Natl Acad Sci U S A. 2003 Jun 24;100(13):7638-43. doi: 10.1073/pnas.1230693100. Epub 2003 Jun 6. Proc Natl Acad Sci U S A. 2003. PMID: 12794186 Free PMC article.
-
The selective beta1-adrenoceptor antagonist nebivolol is a potential oestrogen receptor agonist with neuroprotective abilities.Br J Pharmacol. 2010 Mar;159(6):1264-73. doi: 10.1111/j.1476-5381.2009.00610.x. Epub 2010 Feb 1. Br J Pharmacol. 2010. PMID: 20128815 Free PMC article.
-
Amyloid precursor protein (APP) and amyloid β (Aβ) interact with cell adhesion molecules: Implications in Alzheimer's disease and normal physiology.Front Cell Dev Biol. 2022 Jul 26;10:969547. doi: 10.3389/fcell.2022.969547. eCollection 2022. Front Cell Dev Biol. 2022. PMID: 35959488 Free PMC article. Review.
-
A TAG on to the neurogenic functions of APP.Cell Adh Migr. 2008 Jan-Mar;2(1):2-8. doi: 10.4161/cam.2.1.5790. Epub 2008 Jan 25. Cell Adh Migr. 2008. PMID: 19262125 Free PMC article. Review.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases
Miscellaneous
