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].

References