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Details for messenger / hormone: abeta42

EndoNet ID: ENH00356

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  • amyloid intracellular domain 50
  • Gamma-CTF(50)
  • amyloid intracellular domain 57
  • Gamma-CTF(57)
  • amyloid intracellular domain 59
  • Gamma-CTF(59)
  • Beta-APP40
  • protease nexin-II
  • cerebral vascular amyloid peptide
  • PreA4
  • APPI
  • ABPP
  • Alzheimer disease amyloid protein
  • amyloid beta A4 protein
  • abeta42
  • beta-amyloid protein 42
  • beta-APP42
  • APPbeta peptide 42aa
  • beta-APP
  • amyloid beta peptide 42

General information

  • Neurotoxic; part of cerebral plaque in Alzheimer's disease.
  • Ubiquilin 1 modulates amyloid precursor protein trafficking and Abeta secretion. [1]
  • Abeta42 and Abeta40 have opposing effects on amyloid deposition: Abeta42 promotes amyloid deposition but Abeta40 inhibits it. [2]
  • beta-Amyloid(1-42) binds to alpha7 nicotinic acetylcholine receptor with high affinity. [3]
  • Amyloid beta protein 40 (Abeta40) and 42 (Abeta42), major components of senile plaque amyloids, are physiological peptides present in the brain, cerebrospinal fluid (CSF) and plasma. [4]
  • Metallothionein-III antagonizes the neurotoxic and neurotrophic effects of amyloid beta peptides. [5]


Hormone function

  • metabolism
    • cell metabolism

    Chemical classification

    • hormone
      • genome-encoded
        • cytokines



    Links to other resources

    UniProt P05067
    Ensembl ENST00000346798
    KEGG hsa:351
    • Anatomical structure: brain

      Influenced by:

      • thrombin receptor
        in brain
        • The amyloid beta-protein (A beta) and protease nexin-2/amyloid beta-protein precursor (PN-2/A beta PP) are major constituents of senile plaques and cerebrovascular deposits in individuals with Alzheimer's disease and related disorders. It has been suggested that the coagulation protease thrombin may process A beta PP in a manner leading to the formation of A beta. [6]
        • Effects of thrombin on the secretion and processing of PN-2/A beta PP and the production of A beta in a cellular system. [6]
        • thrombin does not directly contribute to A beta formation, its proteolysis of secreted PN-2/A beta PP may disrupt regions near the carboxyl terminus of the secreted proteins that account for their neuroprotective and cell adhesive properties. [6]
        • Thrombin was found to proteolyze secreted forms of A beta PP proteins and, through activation of its cell surface receptor, induce secretion of PN-2/A beta PP in certain cell types resulting in decreased levels of soluble A beta. These findings demonstrate that thrombin causes nonamyloidogenic processing of ApPP in cultured cells. [6]
    • Anatomical structure: cerebrospinal_fluid


    lung Present
    monocyte Present
    • monocyte activation
    neutrophil granulocyte Present