amyloid beta precursor protein
Last updated 18 Jul 2023
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The APP gene provides instructions for making a protein called amyloid precursor protein. This protein is found in many tissues and organs, including the brain and spinal cord (central nervous system). Little is known about the function of amyloid precursor protein. Researchers speculate that it may bind to other proteins on the surface of cells or help cells attach to one another. Studies suggest that in the brain, it helps direct the movement (migration) of nerve cells (neurons) during early development.
Normal function
The APP gene provides instructions for making a protein called amyloid precursor protein. This protein is found in many tissues and organs, including the brain and spinal cord (central nervous system). Little is known about the function of amyloid precursor protein. Researchers speculate that it may bind to other proteins on the surface of cells or help cells attach to one another. Studies suggest that in the brain, it helps direct the movement (migration) of nerve cells (neurons) during early development.
Amyloid precursor protein is cut by enzymes to create smaller fragments (peptides), some of which are released outside the cell. Two of these fragments are called soluble amyloid precursor protein (sAPP) and amyloid beta (β) peptide. Recent evidence suggests that sAPP has growth-promoting properties and may play a role in the formation of neurons in the brain both before and after birth. The sAPP peptide may also control the function of certain other proteins by turning off (inhibiting) their activity. Amyloid β peptide is likely involved in the ability of neurons to change and adapt over time (plasticity). Other functions of sAPP and amyloid β peptide are under investigation.
Conditions referring to this gene or chromosome
Other names
A4_HUMAN
AAA
ABETA
ABPP
AD1
amyloid beta (A4) precursor protein
amyloid beta-peptide
amyloid beta-protein precursor
amyloid precursor protein
APPI
cerebral vascular amyloid peptide
CVAP
PN-II
PN2
protease nexin 2
protease nexin-II
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Further reading and references
- amyloid beta precursor protein; MedlinePlus, National Library of Medicine.
- Bornebroek M, De Jonghe C, Haan J, Kumar-Singh S, Younkin S, Roos R, Van Broeckhoven C. Hereditary cerebral hemorrhage with amyloidosis Dutch type (AbetaPP 693): decreased plasma amyloid-beta 42 concentration. Neurobiol Dis. 2003 Dec;14(3):619-23. doi: 10.1016/j.nbd.2003.08.019.
- Caille I, Allinquant B, Dupont E, Bouillot C, Langer A, Muller U, Prochiantz A. Soluble form of amyloid precursor protein regulates proliferation of progenitors in the adult subventricular zone. Development. 2004 May;131(9):2173-81. doi: 10.1242/dev.01103. Epub 2004 Apr 8.
- Conti L, Cattaneo E. Controlling neural stem cell division within the adult subventricular zone: an APPealing job. Trends Neurosci. 2005 Feb;28(2):57-9. doi: 10.1016/j.tins.2004.11.005.
- Cordy JM, Hooper NM, Turner AJ. The involvement of lipid rafts in Alzheimer's disease. Mol Membr Biol. 2006 Jan-Feb;23(1):111-22. doi: 10.1080/09687860500496417.
- Edwards-Lee T, Ringman JM, Chung J, Werner J, Morgan A, St George Hyslop P, Thompson P, Dutton R, Mlikotic A, Rogaeva E, Hardy J. An African American family with early-onset Alzheimer disease and an APP (T714I) mutation. Neurology. 2005 Jan 25;64(2):377-9. doi: 10.1212/01.WNL.0000149761.70566.3E.
- Fernandez-Madrid I, Levy E, Marder K, Frangione B. Codon 618 variant of Alzheimer amyloid gene associated with inherited cerebral hemorrhage. Ann Neurol. 1991 Nov;30(5):730-3. doi: 10.1002/ana.410300516.
- Hardy J, Selkoe DJ. The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science. 2002 Jul 19;297(5580):353-6. doi: 10.1126/science.1072994.
- Harman D. Alzheimer's disease pathogenesis: role of aging. Ann N Y Acad Sci. 2006 May;1067:454-60. doi: 10.1196/annals.1354.065.
- Kerr ML, Small DH. Cytoplasmic domain of the beta-amyloid protein precursor of Alzheimer's disease: function, regulation of proteolysis, and implications for drug development. J Neurosci Res. 2005 Apr 15;80(2):151-9. doi: 10.1002/jnr.20408.
- Levy E, Prelli F, Frangione B. Studies on the first described Alzheimer's disease amyloid beta mutant, the Dutch variant. J Alzheimers Dis. 2006;9(3 Suppl):329-39. doi: 10.3233/jad-2006-9s337.
- Maat-Schieman M, Roos R, van Duinen S. Hereditary cerebral hemorrhage with amyloidosis-Dutch type. Neuropathology. 2005 Dec;25(4):288-97. doi: 10.1111/j.1440-1789.2005.00631.x.
- Majersik JJ, Skalabrin EJ. Single-gene stroke disorders. Semin Neurol. 2006 Feb;26(1):33-48. doi: 10.1055/s-2006-933307.
- Obici L, Demarchi A, de Rosa G, Bellotti V, Marciano S, Donadei S, Arbustini E, Palladini G, Diegoli M, Genovese E, Ferrari G, Coverlizza S, Merlini G. A novel AbetaPP mutation exclusively associated with cerebral amyloid angiopathy. Ann Neurol. 2005 Oct;58(4):639-44. doi: 10.1002/ana.20571.
- Papassotiropoulos A, Fountoulakis M, Dunckley T, Stephan DA, Reiman EM. Genetics, transcriptomics, and proteomics of Alzheimer's disease. J Clin Psychiatry. 2006 Apr;67(4):652-70. doi: 10.4088/jcp.v67n0418.
- Rocchi A, Pellegrini S, Siciliano G, Murri L. Causative and susceptibility genes for Alzheimer's disease: a review. Brain Res Bull. 2003 Jun 30;61(1):1-24. doi: 10.1016/s0361-9230(03)00067-4.
- Salameh MA, Robinson JL, Navaneetham D, Sinha D, Madden BJ, Walsh PN, Radisky ES. The amyloid precursor protein/protease nexin 2 Kunitz inhibitor domain is a highly specific substrate of mesotrypsin. J Biol Chem. 2010 Jan 15;285(3):1939-49. doi: 10.1074/jbc.M109.057216. Epub 2009 Nov 17.
- Wolfe MS, Guenette SY. APP at a glance. J Cell Sci. 2007 Sep 15;120(Pt 18):3157-61. doi: 10.1242/jcs.03481. No abstract available.
- Zhang H, Ma Q, Zhang YW, Xu H. Proteolytic processing of Alzheimer's beta-amyloid precursor protein. J Neurochem. 2012 Jan;120 Suppl 1(Suppl 1):9-21. doi: 10.1111/j.1471-4159.2011.07519.x. Epub 2011 Nov 28.
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