Disease relevance of IAPP

• The in vivo deposition of amyloid fibrils is a hallmark of many devastating diseases known as the amyloidoses [1].
• Molecular epidemiology of unilateral amyloid arthropathy in broiler breeders associated with Enterococcus faecalis [2].
• Inactivated E. faecalis, chicken anemia virus and reovirus did not cause amyloid arthropathy after intra-articular inoculation [3].

Psychiatry related information on IAPP

• A heparin-binding domain in the amyloid protein precursor of Alzheimer's disease is involved in the regulation of neurite outgrowth [4].
• 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 [5].

High impact information on IAPP

• Alternative polyadenylation of the amyloid protein precursor mRNA regulates translation [6].
• The effect of cholesterol and monosialoganglioside (GM1) on the release and aggregation of amyloid beta-peptide from liposomes prepared from brain membrane-like lipids [7].
• The zinc finger protein CTCF binds to the APBbeta domain of the amyloid beta-protein precursor promoter. Evidence for a role in transcriptional activation [8].
• The Src-homology region 3 domain of chicken alpha-spectrin (Spc-SH3) is a small two-state folding protein, which has never been described to form amyloid fibrils under any condition investigated so far [9].
• We show here that the mutation of asparagine 47 to alanine at the distal loop, which destabilises similarly the native and folding transition states of the domain, induces the formation of amyloid fibrils under mild acid conditions [9].

Chemical compound and disease context of IAPP

• In conclusion, it was observed that vitamin A enhanced the development of amyloid arthropathy and there were positive associations between amyloidosis, increased levels of serum amyloid A and increased numbers of tissue infiltrating macrophages [10].

Biological context of IAPP

• Amyloid formation in vitro may also complicate production of proteins in the biotechnology industry [1].
• Comparison of the amount of insoluble aggregate, the secondary structure, and fibrillogenicity has shown that the N-linked glycosylation could prevent amyloid fibril formation of amyloidogenic chicken cystatin secreted in yeast cells without affecting its inhibitory activities [11].
• Analysis of differential gene expression supports a role for amyloid precursor protein and a protein kinase C substrate (MARCKS) in long-term memory [12].
• 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 [5].

Anatomical context of IAPP

• These findings indicate that a local increment in neuronal AChE concentration at the mammalian hippocampus, such as those present in amyloid deposits, may play a role in triggering neuropathological and behavioral changes such as those observed in AD brains [13].
• Amyloid beta peptide is not a candidate for the neurotrophic activities released from chromaffin cells [14].
• In the present study we have investigated the possibility that amyloid beta peptide (A beta P) generated from beta APP may have survival supporting effects for neurons from embryonic chick ciliary (CG) and dorsal root ganglia (DRG) [14].
• Inflammatory and degenerative changes in the articular cartilage and adjoining tissues result in an increase of highly sulphated GAGs, which are considered to enhance deposition of SAA as amyloid [15].
• Ultrastructurally, bundles of amyloid fibrils were seen in invaginations of synoviocytes and chondrocytes [15].

Associations of IAPP with chemical compounds

• The sequence contained within the two polyadenylation sites used in the 3' untranslated region of the amyloid protein precursor mRNA was also able to increase the production of the chicken lysozyme or the chloramphenicol acetyl transferase, as demonstrated by in vivo translation of different chimeric mRNAs obtained by in vitro transcription [6].
• The dissociation and reassociation processes of amyloid protofibrils initiated by pressure-jump have been monitored with real-time (1)H NMR spectroscopy using an intrinsically denatured disulfide-deficient variant of hen lysozyme [16].
• 0. A red shift of the Congo red absorption spectrum caused by the precipitation of the fully reduced HEWL in the presence of 90% (v/v) ethanol is typical of the presence of amyloid aggregation [17].
• Effects of sodium azide on the secretion of soluble amyloid-beta precursor protein and the accumulation of beta-amyloid(1-40) in cultured chick neurons [18].
• Methylprednisolone had a more successful inhibitory effect on amyloid arthropathy than pentoxyfylline [10].

Other interactions of IAPP

• Moreover, from the analysis of amyloid aggregation of the reduced lysozymes, it was suggested that the disruption of the residual structure in denatured state by W62G mutation deterred the formation of the amyloid fibrils of lysozyme [19].

Analytical, diagnostic and therapeutic context of IAPP

• Differential scanning calorimetry experiments under conditions of amyloid formation have allowed the identification of different thermal transitions corresponding to conformational and aggregation processes as well as to the high-temperature disaggregation and unfolding of the amyloid fibrils [9].
• Immunogold electron microscopy failed to reveal signs of intracellular amyloid formation [15].
• Induction of amyloid arthropathy in chickens was carried out using a single intravenous injection of Enterococcus faecalis cultures [15].
• An animal model of amyloid arthropathy is presented, as are studies on the pathogenesis of arthropathic and amyloidogenic E. faecalis infections in brown layers [20].

References