Complement activation by cross-linked truncated and chimeric full-length beta-amyloid.
Neuroreport
; 8(16): 3457-62, 1997 Nov 10.
Article
en En
| MEDLINE
| ID: mdl-9427307
ABSTRACT
The activation of complement by beta-amyloid (A beta) has been implicated in the local inflammatory response in Alzheimer's disease. To assess the structural parameters required for this activation, beta-sheet-containing fibrils of A beta1-28 were induced by low pH and then chemically cross-linked to constrain the beta-sheet conformation. Chimeric A beta peptides with a substituted C-terminal sequence derived from two different transmembrane proteins were also assessed for the ability to form fibrils rich in beta-sheet structure and to activate complement. Both the cross-linked A beta1-28 and the chimeric A beta peptides were strong activators of the classical complement pathway. These results suggest that the C-terminal residues (29-42) of A beta facilitate fibril assembly required for complement activation but do not contain the interaction sites required for complement activation, further supporting the hypothesis that C1q binds to the N-terminal hydrophilic domain of A beta, and that a fibrillar beta-sheet-rich conformation is required for effective binding and activation of C1.
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Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Fragmentos de Péptidos
/
Péptidos beta-Amiloides
/
Activación de Complemento
Límite:
Animals
/
Humans
Idioma:
En
Revista:
Neuroreport
Asunto de la revista:
NEUROLOGIA
Año:
1997
Tipo del documento:
Article
País de afiliación:
Estados Unidos