amyloid-beta-peptides has been researched along with pimagedine* in 3 studies
3 other study(ies) available for amyloid-beta-peptides and pimagedine
| Article | Year |
|---|---|
An investigation into the mechanisms mediating plasma lipoprotein-potentiated beta-amyloid fibrillogenesis.
The toxicity of the beta-amyloid (Abeta) peptide of Alzheimer's disease may relate to its polymerisation state (i.e. fibril content). We have shown previously that plasma lipoproteins, particularly when oxidised, greatly enhance Abeta polymerisation. In the present study the nature of the interactions between both native and oxidised lipoproteins and Abeta1-40 was investigated employing various chemical treatments. The addition of ascorbic acid or the vitamin E analogue, trolox, to lipoprotein/Abeta coincubations failed to inhibit Abeta fibrillogenesis, as did the treatment of lipoproteins with the aldehyde reductant, sodium borohydride. The putative lipid peroxide-derived aldehyde scavenger, aminoguanidine, however, inhibited Abeta-oxidised lipoprotein-potentiated polymerisation, but in a manner consistent with an antioxidant action for the drug. Lipoprotein treatment with the reactive aldehyde 4-hydroxy-2-trans-nonenal enhanced Abeta polymerisation in a concentration-dependent fashion. Incubation of Abeta with lipoprotein fractions from which the apoprotein components had been removed resulted in extents of polymerisation comparable to those observed with Abeta alone. These data indicate that the apoprotein components of plasma lipoproteins play a key role in promoting Abeta polymerisation, possibly via interactions with aldehydes. Topics: Aldehydes; Alzheimer Disease; Amyloid beta-Peptides; Antioxidants; Apolipoproteins; Ascorbic Acid; Biopolymers; Borohydrides; Chromans; Guanidines; Humans; Kinetics; Lipoproteins; Oxidation-Reduction; Peptide Fragments | 2002 |
Amyloid beta-peptide induces nitric oxide production in rat hippocampus: association with cholinergic dysfunction and amelioration by inducible nitric oxide synthase inhibitors.
Topics: Acetylcholine; Amyloid beta-Peptides; Animals; Cerebral Ventricles; Chemotherapy, Cancer, Regional Perfusion; Cholinergic Agents; Guanidines; Hippocampus; Memory Disorders; Microglia; Models, Biological; Nicotine; Nitric Oxide; Nitric Oxide Synthase; Nitric Oxide Synthase Type II; Peptide Fragments; Rats | 2001 |
Influence of advanced glycation end-products and AGE-inhibitors on nucleation-dependent polymerization of beta-amyloid peptide.
Nucleation-dependent polymerization of beta-amyloid peptide, the major component of plaques in patients with Alzheimer's disease, is significantly accelerated by crosslinking through Advanced Glycation End-products (AGEs) in vitro. During the polymerization process, both nucleus formation and aggregate growth are accelerated by AGE-mediated crosslinking. Formation of the AGE-crosslinked amyloid peptide aggregates could be attenuated by the AGE-inhibitors Tenilsetam, aminoguanidine and carnosine. These experimental data, and clinical studies, reporting a marked improvement in cognition and memory in Alzheimer's disease patients after Tenilsetam treatment, suggest that AGEs might play an important role in the etiology or progression of the disease. Thus AGE-inhibitors may generally become a promising drug class for the treatment of Alzheimer's disease. Topics: Alzheimer Disease; Amyloid beta-Peptides; Benzothiazoles; Carnosine; Cognition; Cross-Linking Reagents; Fructose; Glycation End Products, Advanced; Guanidines; Humans; Memory; Neuropeptide Y; Particle Size; Peptide Fragments; Piperazines; Protein Structure, Secondary; Solubility; Temperature; Thiazoles; Thiophenes | 1997 |