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Gene Review

APP  -  amyloid beta (A4) precursor protein

Canis lupus familiaris

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High impact information on APP

  • However, deleting the last 42 amino acids (residues 654-695) or changing tyrosine 653 to alanine altered the distribution of cell surface beta APP so that approximately 40-50% of the molecules were inserted apically [1].
  • These results demonstrate that in epithelial cells two independent mechanisms mediate the polarized trafficking of beta APP holoprotein and its major secreted derivative (APPs) and that A beta peptides are derived in part from beta APP holoprotein targeted to the cell surface by a signal that includes tyrosine 653 [1].
  • Moreover, ammonium chloride treatment resulted in the equal secretion of APPs into both compartments, as occurs with other non-membranous, basolaterally secreted proteins, but it did not influence the polarity of cell surface beta APP [1].
  • To understand beta APP trafficking and processing, we analyzed the sorting of beta APP in Madin-Darby canine kidney (MDCK) cells, an epithelial cell known to possess physiologically distinct apical and basolateral plasma membranes [2].
  • APP is involved in Herpes simplex transport article


  1. Polarized sorting of beta-amyloid precursor protein and its proteolytic products in MDCK cells is regulated by two independent signals. Haass, C., Koo, E.H., Capell, A., Teplow, D.B., Selkoe, D.J. J. Cell Biol. (1995) [Pubmed]
  2. Polarized secretion of beta-amyloid precursor protein and amyloid beta-peptide in MDCK cells. Haass, C., Koo, E.H., Teplow, D.B., Selkoe, D.J. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
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