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Gene Review

APP  -  amyloid beta (A4) precursor protein

Gallus gallus

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Disease relevance of APP

  • Although L-type voltage-dependent calcium channels (VDCC) have been implicated in A beta toxicity, the effect of L-type VDCC on APP secretion has not previously been examined [1].

Psychiatry related information on APP

  • These findings suggest that RER and its derivatives may offer a novel approach to enhancing the neuroprotective effects of APP and alleviating the effects of memory loss in the early stages of Alzheimer's disease [2].

High impact information on APP

  • Porcine brain membranes, on the other hand, possessed two orders of the APP-binding sites, a high affinity component (Kd = 4.24 x 10(-9) M) and a low affinity component (Kd = 3.08 x 10(-7) M) [3].
  • The binding sites were highly specific for PYY and APP as well as for NPY and PPP, coupled to a guanine nucleotide regulatory protein, and distributed in various brain areas, including the cerebellum [3].
  • Membranes from chick brain and liver possessed highly specific avian PP (APP)-binding sites, while those from chick whole pancreas and proventricular and duodenal mucosa exhibited little or no specific [125I]iodo-APP binding [4].
  • The binding process to chick brain membranes retained specificity for intact APP1-36, as unlabeled bovine PP1-36 (BPP1-36) inhibited specific binding of [125I]iodo-APP by 50% at a concentration of 7 X 10(-9) M (10 times the IC50 level of unlabeled APP) [4].
  • The antiprotease bacitracin was capable of virtually complete degradation inhibition, but its presence failed to increase APP binding by kidney membranes [4].

Biological context of APP

  • Chick brain membranes, on the other hand, possessed two orders of APP binding sites, a high affinity site (Kd = 3.3 X 10(-10) M) and a low affinity site (Kd = 1.8 X 10(-7) M) [4].
  • Amino acid sequences containing the palindromic tripeptide RER, matching amino acids 328-330 of the amyloid precursor protein APP, when injected intracerebrally prior to or just after training, protect against memory loss induced by amyloid-beta (A beta) in a one-trial passive avoidance task in the young chick [2].

Anatomical context of APP

  • Chick kidney membranes degraded more [125I]iodo-APP than any other chicken tissue [4].
  • Does the third pancreatic hormone (APP) play a trophic role in the growth of the embryonic chick proventriculus [5]?
  • Biological evaluation of the third pancreatic hormone (APP): hepatocyte and adipocyte effects [6].

Associations of APP with chemical compounds

  • Since the N-terminal residues of FMRFamide and LPLRFamide are not homologous with equivalent residues of APP or NPY, our results indicate that only Arg-Tyr-NH2 or Arg-Phe-NH2 sequences are necessary for binding of the carboxy terminus peptides of the PP family [7].
  • APP release was least affected by SRIF addition to the media, although depression by high glucose occurred [8].
  • Quail in two of the four compartments were given vitamin C (ascorbyl-2-polyphosphate, APP, 1 g L-ascorbic acid/L) solution for 48 h, whereas the other birds received untreated tap water as usual before they were tested at 23 days of age [9].
  • Araldite sections of formalin-fixed pancreas from chicks at hatching were treated by an indirect immuno-enzyme technique to reveal cells containing APP, somatostatin, glucagon and insulin [10].

Other interactions of APP

  • The antibody used is C-terminal-specific and shows slight but significant (1-2%) cross-reactivity with chicken pancreatic polypeptide (APP) [11].
  • At 15-min intervals, the tissue cubes were transferred to fresh media and samples of each medium measured for insulin, glucagon, and APP [8].
  • Since certain published observations point to the possible occurrence of APP and somatostatin in the same cells, consecutive sections were stained for these hormones [10].


  1. A beta peptides and calcium influence secretion of the amyloid protein precursor from chick sympathetic neurons in culture. Mok, S.S., Clippingdale, A.B., Beyreuther, K., Masters, C.L., Barrow, C.J., Small, D.H. J. Neurosci. Res. (2000) [Pubmed]
  2. The peptide sequence Arg-Glu-Arg, present in the amyloid precursor protein, protects against memory loss caused by A beta and acts as a cognitive enhancer. Mileusnic, R., Lancashire, C.L., Rose, S.P. Eur. J. Neurosci. (2004) [Pubmed]
  3. Characterization of the receptors for peptide-YY and avian pancreatic polypeptide in chicken and pig brains. Inui, A., Okita, M., Miura, M., Hirosue, Y., Nakajima, M., Inoue, T., Oya, M., Baba, S. Endocrinology (1990) [Pubmed]
  4. In vitro binding and degradation of avian pancreatic polypeptide by chicken and rat tissues. Adamo, M.L., Dyckes, D.F., Hazelwood, R.L. Endocrinology (1983) [Pubmed]
  5. Does the third pancreatic hormone (APP) play a trophic role in the growth of the embryonic chick proventriculus? Laurentz, D.A., Hazelwood, R.L. Proc. Soc. Exp. Biol. Med. (1979) [Pubmed]
  6. Biological evaluation of the third pancreatic hormone (APP): hepatocyte and adipocyte effects. McCumbee, W.D., Hazelwood, R.L. Gen. Comp. Endocrinol. (1977) [Pubmed]
  7. Recognition of neuropeptides FMRFamide and LPLRFamide by chicken cerebellum avian pancreatic polypeptide binding sites. Ganeshan, K., Perlman, M.O., Perlman, J.M., Adamo, M.L., Hazelwood, R.L., Dyckes, D.F. Proc. Soc. Exp. Biol. Med. (1987) [Pubmed]
  8. In vitro release of pancreatic hormones following 99% pancreatectomy in the chicken. Hazelwood, R.L., Cieslak, S.R. Gen. Comp. Endocrinol. (1989) [Pubmed]
  9. Timidity in Japanese quail: effects of vitamin C and divergent selection for adrenocortical response. Jones, R.B., Satterlee, D.G., Cadd, G.G. Physiol. Behav. (1999) [Pubmed]
  10. An immunocytochemical study of the distribution of pancreatic endocrine cells in chicks, with special reference to the relationship between pancreatic polypeptide and somatostatin-immunoreactive cells. Rawdon, B.B., Andrew, A. Histochemistry (1979) [Pubmed]
  11. FMRFamide-like immunoreactivity in rat brain: development of a radioimmunoassay and its application in studies of distribution and chromatographic properties. Dockray, G.J., Williams, R.G. Brain Res. (1983) [Pubmed]
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