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Alterations in Presenilin 1 Processing by Amyloid-Beta Peptide in the Rat Retina

Alterations in Presenilin 1 Processing by Amyloid-Beta Peptide in the Rat Retina

Helena R Watts, Valerie Vince, Desmond T Walsh, Laura G Bresciani, Stephen M Gentleman, Ling-Sun Jen, Peter J B Anderson

Exp Brain Res. 2007 Jul;181(1):69-77.

PMID: 17333007

Abstract:

Accumulating evidence indicates that mutations in the presenilin 1 (PS1) gene are responsible for most cases of familial Alzheimer's disease (AD). Although its biological functions are not yet fully understood, it appears that PS1 plays a role in the processing and trafficking of the amyloid precursor protein (APP). However, little is known about factors that are involved in regulating the metabolism of PS1 especially in relation to AD pathology. In this study, we have examined the effect of optic nerve crush, intravitreal injection of the inflammatory agent lipopolysaccharide (LPS) or injection of amyloid beta(1-42) (A beta(1-42)) on the expression and processing of PS1 in the rat retina. We found that 48 h after injection of A beta(1-42) there was a dramatic alteration in the banding pattern of PS1 on Western blots, as indicated by marked changes in the levels of expression of some of its C- and N-terminal fragments in retinal homogenates. These results suggest an A beta(1-42)-induced potentiation of a non-specific stress-related but inflammation-independent alteration of processing of PS1 in this in vivo model.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR4248117	Presenilin-1 N-Terminal Peptide			Price

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