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Journal of Zhejiang University SCIENCE A 2004 Vol.5 No.10 P.1226-1238


Protein folding pathology in domestic animals

Author(s):  GRUYS E.

Affiliation(s):  Section of Domestic Animal Pathology, Department of Pathobiology, Faculty of Veterinary Medicine, Utrecht University, Utrecht, The Netherlands

Corresponding email(s):   e.gruys@vet.uu.nl

Key Words:  Extracellular fibrils, Amyloid, Amyloid enhancing factor, Prion, PrP, Spongiform encephalopathy, Alzheimer&rsquo, s disease

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GRUYS E.. Protein folding pathology in domestic animals[J]. Journal of Zhejiang University Science A, 2004, 5(10): 1226-1238.

@article{title="Protein folding pathology in domestic animals",
author="GRUYS E.",
journal="Journal of Zhejiang University Science A",
publisher="Zhejiang University Press & Springer",

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%T Protein folding pathology in domestic animals
%J Journal of Zhejiang University SCIENCE A
%V 5
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%@ 1869-1951
%D 2004
%I Zhejiang University Press & Springer
%DOI 10.1631/jzus.2004.1226

T1 - Protein folding pathology in domestic animals
J0 - Journal of Zhejiang University Science A
VL - 5
IS - 10
SP - 1226
EP - 1238
%@ 1869-1951
Y1 - 2004
PB - Zhejiang University Press & Springer
ER -
DOI - 10.1631/jzus.2004.1226

Fibrillar proteins form structural elements of cells and the extracellular matrix. Pathological lesions of fibrillar microanatomical struc tures, or secondary fibrillar changes in globular proteins are well known. A special group concerns histologically amorphous deposits, amyloid. The major characteristics of amyloid are: apple green birefringence after Congo red staining of histological sections, and non-branching 7-10 nm thick fibrils on electron microscopy revealing a high content of cross beta pleated sheets. About 25 different types of amyloid have been characterised. In animals, AA-amyloid is the most frequent type. Other types of amyloid in animals represent: AIAPP (in cats), AApoAI, AApoAII, localised AL-amyloid, amyloid in odontogenic or mammary tumors and amyloid in the brain. In old dogs Aβ and in sheep AprPsc-amyloid can be encountered. AA-amyloidosis is a systemic disorder with a precursor in blood, acute phase serum amyloid A (SAA). In chronic inflammatory processes AA-amyloid can be deposited. A rapid crystallization of SAA to amyloid fibrils on small beta-sheeted fragments, the ‘amyloid enhancing factor’ (AEF), is known and the AEF has been shown to penetrate the enteric barrier. amyloid fibrils can aggregate from various precursor proteins in vitro in particular at acidic pH and when proteolytic fragments are formed. Molecular chaperones influence this process. Tissue data point to amyloid fibrillogenesis in lysosomes and near cell surfaces. A comparison can be made of the fibrillogenesis in prion diseases and in enhanced AA-amyloidosis. In the reactive form, acute phase SAA is the supply of the precursor protein, whereas in the prion diseases, cell membrane proteins form a structural source. Aβ-amyloid in brain tissue of aged dogs showing signs of dementia forms a canine counterpart of senile dementia of the Alzheimer type (ccSDAT) in man. Misfolded proteins remain potential food hazards. Developments concerning prevention of amyloidogenesis and therapy of amyloid deposits are shortly commented.

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