Amyloid-beta precursor protein

APP
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesAPP, AAA, ABETA, ABPP, AD1, APPI, CTFgamma, CVAP, PN-II, PN2, amyloid beta precursor protein, preA4, alpha-sAPP
External IDsOMIM: 104760; MGI: 88059; HomoloGene: 56379; GeneCards: APP; OMA:APP - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001198823
NM_001198824
NM_001198825
NM_001198826
NM_007471

RefSeq (protein)

NP_001185752
NP_001185753
NP_001185754
NP_001185755
NP_031497

Location (UCSC)Chr 21: 25.88 – 26.17 MbChr 16: 84.75 – 84.97 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse
(a) A low magnification image immediately after co-injection of red negatively charged and green glycine-conjugated beads showing the injection site, marked with an oil droplet, appearing as a round yellow sphere. Overlap of red and green fluorescence produces a yellow image. (b) At 50 min after injection, the red carboxylated beads have progressed in the anterograde direction (to the right) while the green glycine-conjugated beads have made no progress. (c)–(e) An axon co-injected with red APP-C beads and green glycine beads and imaged for 100 frames at 4 s intervals at 40× magnification. (c) Red channel (left) first frame; (center) 50 frames superimposed; (right) all 100 frames superimposed. Note the progression of individual beads towards the right, anterograde, side of the injection site heading towards the presynaptic terminal. (d) Two images of the green channel from the same video sequence; (left) first frame; (center) 100 frames superimposed. Note the lack of significant movement of the green glycine beads. (e) Both red and green channels from 100 frames superimposed of the same video as in (c) and (d). (f) Single bead trajectories at high magnification from a set of superimposed frames showing movements of beads.

Amyloid-beta precursor protein (APP) is an integral membrane protein expressed in many tissues and concentrated in the synapses of neurons. It functions as a cell surface receptor[5] and has been implicated as a regulator of synapse formation,[6] neural plasticity,[7] antimicrobial activity,[8] and iron export.[9] It is coded for by the gene APP and regulated by substrate presentation.[10] APP is best known as the precursor molecule whose proteolysis generates amyloid beta (Aβ), a polypeptide containing 37 to 49 amino acid residues, whose amyloid fibrillar form is the primary component of amyloid plaques found in the brains of Alzheimer's disease patients.

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000142192Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000022892Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ "Amyloid-beta precursor protein". Retrieved 10 January 2021.
  6. ^ Priller C, Bauer T, Mitteregger G, Krebs B, Kretzschmar HA, Herms J (Jul 2006). "Synapse formation and function is modulated by the amyloid precursor protein". The Journal of Neuroscience. 26 (27): 7212–21. doi:10.1523/JNEUROSCI.1450-06.2006. PMC 6673945. PMID 16822978.
  7. ^ Turner PR, O'Connor K, Tate WP, Abraham WC (May 2003). "Roles of amyloid precursor protein and its fragments in regulating neural activity, plasticity and memory". Progress in Neurobiology. 70 (1): 1–32. doi:10.1016/S0301-0082(03)00089-3. PMID 12927332. S2CID 25376584.
  8. ^ Moir RD, Lathe R, Tanzi RE (2018). "The antimicrobial protection hypothesis of Alzheimer's disease". Alzheimer's & Dementia. 14 (12): 1602–1614. doi:10.1016/j.jalz.2018.06.3040. PMID 30314800.
  9. ^ Duce JA, Tsatsanis A, Cater MA, James SA, Robb E, Wikhe K, Leong SL, Perez K, Johanssen T, Greenough MA, Cho HH, Galatis D, Moir RD, Masters CL, McLean C, Tanzi RE, Cappai R, Barnham KJ, Ciccotosto GD, Rogers JT, Bush AI (Sep 2010). "Iron-export ferroxidase activity of β-amyloid precursor protein is inhibited by zinc in Alzheimer's disease". Cell. 142 (6): 857–67. doi:10.1016/j.cell.2010.08.014. PMC 2943017. PMID 20817278.
  10. ^ Wang H, Kulas JA, Wang C, Holtzman DM, Ferris HA, Hansen SB (17 August 2021). "Regulation of beta-amyloid production in neurons by astrocyte-derived cholesterol". Proceedings of the National Academy of Sciences. 118 (33): e2102191118. Bibcode:2021PNAS..11802191W. doi:10.1073/pnas.2102191118. PMC 8379952. PMID 34385305.