Document Detail

Disassembly of amyloid beta-protein fibril by basement membrane components.
MedLine Citation:
PMID:  12150206     Owner:  NLM     Status:  MEDLINE    
Amyloid beta-protein (A3) fibril in senile plaque may be related to the pathogenesis of Alzheimer's disease (AD). Basement membrane (BM) components are associated with the plaques in AD brain. It suggests that the BM components may play an important role in the deposition of the plaque. We investigated the potential of BM components, such as type IV collagen (collagen IV) and entactin, to induce disassembly of preformed Abeta1-42 (Abeta42) fibrils in direct comparison to laminin. Thioflavin T assays revealed that these BM components disrupted preformed Abeta42 fibrils in a dose-dependent manner. The high concentration of BM components, 100 microg/mL laminin, 50 microg/mL collagen IV and 50 microg/mL entactin, had most effect on disassembly of preformed Abeta42 fibrils (Molar ratio; Abeta42:laminin = 90:1, Abeta42:collagen IV = 34:1, Abeta42:entactin = 20:1). Circular dichroism spectroscopy data indicated that the high concentration of BM components induced structural transition in Abeta42 from beta-sheet to random structures. These results suggest that collagen IV and entactin, as well as laminin, are effective inducers of disassembly of Abeta42 fibrils. The ability of these BM components to induce random structures may be linked to the disassembly of preformed Abeta42 fibrils.
Yoichi Kiuchi; Yoshihiko Isobe; Kiyomi Fukushima; Masaaki Kimura
Related Documents :
6094646 - Pharmacologic review: a review of the literature of ketoconazole therapy in the treatme...
9812326 - Clinical issues surrounding the use of terbutaline sulfate for preterm labor.
16621416 - Identification of novel saponins from edible seeds of japanese horse chestnut (aesculus...
12093316 - Food-drug interactions.
15206986 - Food does not affect the pharmacokinetics of solifenacin, a new muscarinic receptor ant...
19791596 - Differential use of identical food resources by reticulitermes flavipes (isoptera: rhin...
Publication Detail:
Type:  Comparative Study; Journal Article    
Journal Detail:
Title:  Life sciences     Volume:  70     ISSN:  0024-3205     ISO Abbreviation:  Life Sci.     Publication Date:  2002 Apr 
Date Detail:
Created Date:  2002-08-01     Completed Date:  2002-08-13     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0375521     Medline TA:  Life Sci     Country:  England    
Other Details:
Languages:  eng     Pagination:  2421-31     Citation Subset:  IM    
Toxicology Laboratory, Drug Metabolism and Toxicology Research Center, Taisho Pharmaceutical Co, Ltd, Saitama, Japan.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Amyloid beta-Protein / metabolism*
Basement Membrane / chemistry*,  ultrastructure
Circular Dichroism
Collagen Type IV / chemistry,  pharmacology*
Fluorescent Dyes
Laminin / pharmacology*
Membrane Glycoproteins / pharmacology*
Microscopy, Electron
Reg. No./Substance:
0/Amyloid beta-Protein; 0/Collagen Type IV; 0/Fluorescent Dyes; 0/Laminin; 0/Membrane Glycoproteins; 0/Thiazoles; 0/nidogen; 2390-54-7/thioflavin T

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

Previous Document:  Modulation by substrates of the protective effect of cyclosporin A on mitochondrial damage.
Next Document:  Antitumor and antioxidant activity of spin labeled derivatives of podophyllotoxin (GP-1) and congene...