Document Detail

Beta amyloid peptide: from different aggregation forms to the activation of different biochemical pathways.
MedLine Citation:
PMID:  19305989     Owner:  NLM     Status:  MEDLINE    
Amyloid beta peptide (Abeta) is the major component of amyloid plaques in the brain of individuals affected by Alzheimer's disease (AD). The formation of the plaques is due to an overproduction of Abeta by APP processing, its precursor, and to its ability to convert under specific conditions from its soluble form into highly ordered fibrillar aggregates. Although neuronal degeneration occurs near the amyloid plaques, some studies have suggested that intermediates such as protofibrils or simple oligomers are also involved in AD pathogenesis and even appear to be the more dangerous species in the onset of the pathology. Further, toxic properties of aggregates of different size have been investigated and the obtained results support the hypothesis that different aggregate sizes can induce different degeneration pathways. In the present review some of the knowledge about the biochemical routes of Abeta processing and production and the relationship among Abeta and oxidative stress, metal homeostasis, inflammatory process, and cell death are summarized. Moreover, current strategies addressing both fibrillogenesis process and different Abeta altered biochemical pathways utilized for therapies are described.
Marta Di Carlo
Related Documents :
17332749 - Gxxxg motifs within the amyloid precursor protein transmembrane sequence are critical f...
10510309 - Common structural features determine the effectiveness of carvedilol, daunomycin and ro...
15537629 - A sequence within the first transmembrane domain of pen-2 is critical for pen-2-mediate...
22285789 - Adipokinetic hormones (akhs) of sphingid lepidoptera, including the identification of a...
19502709 - A new function of human htra2 as an amyloid-beta oligomerization inhibitor.
18726569 - Analysis of abeta interactions using proteinchip technology.
16263269 - Glutathione transferases: new functions.
9382849 - Hla-do is a negative modulator of hla-dm-mediated mhc class ii peptide loading.
8206929 - Two pairs of oppositely charged amino acids from jun and fos confer heterodimerization ...
Publication Detail:
Type:  Journal Article     Date:  2009-03-21
Journal Detail:
Title:  European biophysics journal : EBJ     Volume:  39     ISSN:  1432-1017     ISO Abbreviation:  Eur. Biophys. J.     Publication Date:  2010 May 
Date Detail:
Created Date:  2010-04-29     Completed Date:  2010-08-10     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  8409413     Medline TA:  Eur Biophys J     Country:  Germany    
Other Details:
Languages:  eng     Pagination:  877-88     Citation Subset:  IM    
Istituto di Biomedicina ed Immunologia Molecolare, Consiglio Nazionale delle Ricerche, via Ugo La Malfa 153, Palermo, Italy.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Alzheimer Disease / chemically induced*
Amyloid / metabolism*
Amyloid beta-Protein / toxicity*
Amyloid beta-Protein Precursor / metabolism
Cell Death / drug effects
Cells, Cultured
Inflammation / metabolism
Mice, Transgenic
Nerve Degeneration / chemically induced*
Neurons / drug effects*,  pathology,  physiology
Peptide Fragments / metabolism
Receptors, Cell Surface / metabolism
tau Proteins / pharmacology
Reg. No./Substance:
0/Amyloid; 0/Amyloid beta-Protein; 0/Amyloid beta-Protein Precursor; 0/Peptide Fragments; 0/Receptors, Cell Surface; 0/protease nexins; 0/tau Proteins

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  The venous hinge-an objective sign for the diagnosis and follow-up of treatment in patients with int...
Next Document:  Reminiscences of work with Alex Hope: the movement of water and ions in giant algal cells, 1963-1967...