Publication: Cytochemical study of the involvement of cell
organelles in formation and accumulation of fibrillar
amyloid in the pancreas of NORß transgenic mice
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Date
2001
Authors
Dobrogowska, D. H. ; Vorbrodt, A. W. ; Wegiel, J. ; Wang, K. C. ; Shoji, M. ; Mondadori, C. ; Polatis, G. ; Giovanni, A. ; Wisniewski, H. M.
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Publisher
F. Hernández y Juan F. Madrid. Universidad de Murcia: Departamento de Biología Celular e Histología
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DOI
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info:eu-repo/semantics/article
Description
Abstract
Ph osphatase ultrastructural cytoc hemistry
was used to evalu ate the participation of cytopl asmic
orga nell es in the accumulation of fibrillar amyloid /3
(A13) in exocrine acinar cells and in macrophages of the
pancreas of transgenic mice overexpressing a carboxyterminal fragment of A/3 protein prec urso r (A/3PP).
Nu cleosid e diph os phata se (N DPase) and glucose-6-
ph os ph atase (G6Pase) we re used as cy toc hemi cal
markers of the endopl asmi c reti culum (ER), thi amine
pyroph osphatase (TPPase) as a ma rke r of th e Golgi
apparatu s (GA), and acid phosph atase (AcPase) as a
marker of Iysosomes. Monoclonal antibody 4G8 raised
aga inst the 17-24 aa sequence of human A/3 protein was
used for immunogold loca li za tion of fibrill ar A/3. The
results of this study indicate that the fo rmation of A13 in
acinar cells occurs directl y in the vacuolar areas of the
rough ER (RER) without evident participati on of the
elements of the GA, whereas an intimate structural
relation with primary Iysosomes suggests their role in
modification or digestion of the deposited amyloid.
In macrophagcs, fibrillar amyloid was prese nt in
numerous cytoplasmic vacuoles located frequ entl y in
close proximit y to fl attened saccul es of the ER. This
structural pattern revea led simil arity to that observed
prev iously in mi croglial cells producing fibrill ar PrP
amyloid in scrapi e-infected mice and A/3 in brains of
human eld erl y pati ents and in Alzheimer's type brain
pathology.
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Citation
Histology and histopathology, Vol. 16, nº 4 (2001)
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