Publication: Transgenic mice overexpressing both amyloid ß-protein and perlecan in pancreatic acinar cells
Authors
Fukuchi, K. ; Hart, M. ; Yan, Z. ; Hassell, J.R. ; Li, L.
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Publisher
Murcia : F. Hernández
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DOI
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info:eu-repo/semantics/article
Description
Abstract
Heparan sulfate proteoglycans such as
perlecan are thought to facilitate amyloid fibril
formation. Tg3695 mice overexpress perlecan core
protein in many tissues including the brain and pancreas.
Tg13592 mice overexpress the signal plus 99-amino acid
carboxyl terminal sequences (C99) of amyloid ß-protein
precursor in multiple tissues and develop amyloid
deposits in the pancreas. To investigate a role of perlecan
in ß-amyloidosis, we established doubly transgenic mice
by crossing the two lines of transgenic mice. The
expression levels of the two transgenes remained
unchanged in the brain and pancreas and the doubly
transgenic mice did not develop amyloid deposits in the
brain up to 19-months of age. Amyloid load detected by
thioflavine S in the pancreas of the doubly transgenic
mice was not significantly different from that in the
transgenic littermates expressing only C99. Amyloid
load in the pancreas increased during aging. We found a
positive correlation between the Aß-immunoreactive
(non-fibrillar and fibrillar) and thioflavine S-positive
(fibrillar) Aß deposits in the single (C99) but not doubly
transgenic mice. Our results suggest that perlecan does
not independently influence amyloid formation in the
pancreas of the transgenic mice and that there may be
other factors that may modulate amyloid formation
together with perlecan.
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