Animal models for reactive amyloidosis

Gruys, E.; Snel, F. W. J. J.

doi:10.1016/s0950-3579(05)80117-7

Cited by 48 publications

(28 citation statements)

References 45 publications

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“…3,9,[11][12][13][14][15][16][17][18][19][20][21][22][23][24][25][26][27]. In all, amyloidosis was diagnosed, and the amyloid quantity was evaluated using the regular Congo red (Bennhold's) method.…”

Section: Tissues From Animals With Natural Amyloidosismentioning

confidence: 99%

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An Ancillary Tool for the Diagnosis of Amyloid A Amyloidosis in a Variety of Domestic and Wild Animals

et al. 2005

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Abstract. Immunohistochemistry, the standard method for diagnosing amyloid A (AA) amyloidosis, is limited in animals because it requires a large array of animal-specific anti-AA antibodies, not commercially available. The Shtrasburg method (SH method) is a highly specific and sensitive technique, helping in the diagnosis and determination of AA amyloidosis in humans. The aim of this study is to determine whether the SH method is applicable in the diagnosis of AA amyloidosis in a variety of animals. Tissue samples were obtained from animals suffering from spontaneous or experimentally induced AA amyloidosis (mice, hamsters, guinea pigs, cheetahs, cats, cows, ducks, a dog, a goose, a chicken, and a turaco). Detection of the amyloid and quantitative evaluation were performed using Congo red staining, and specific AA typing was performed by the potassium permanganate technique. The studied tissues were subjected to the SH method, which confirmed the AA nature of the amyloid deposit, by displaying in polyacrylamide gel electrophoresis protein bands consistent with the molecular weight of the species-specific AA, in all the animals examined, except mice, hamsters, and guinea pigs. N-terminal analysis of these bands corroborated their AA origin. We conclude that the SH method may be used as an ancillary simple tool for the diagnosis of AA amyloidosis in a large number of domestic and wild animals. Moreover, our findings further increase the feasibility of applying this method in humans.

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Section: Tissues From Animals With Natural Amyloidosismentioning

confidence: 99%

“…15,20 Amyloid fibrils are usually identified by their unique feature of displaying green birefringence under polarized light 37 after Congo red staining. The amyloid deposit is categorized by its major component, which is determined by the underlying disease.…”

mentioning

confidence: 99%

An Ancillary Tool for the Diagnosis of Amyloid A Amyloidosis in a Variety of Domestic and Wild Animals

et al. 2005

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“…Presumably AEF represents a nidus for the crystallisation of the amyloidogenic acute phase SAA and cytokines with a beta sandwich might be involved in the process of formation of the first nidus (Gruys and Snel, 1994). Further on, misfolded SAA-fragments might accelerate the fibrillogenesis.…”

Section: Fibrillogenesis and The Amyloid Enhancing Factor (Aef)mentioning

confidence: 99%

Protein folding pathology in domestic animals

Gruys

2004

J. Zheijang Univ.-Sci.

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Fibrillar proteins form structural elements of cells and the extracellular matrix. Pathological lesions of fibrillar microanatomical structures, 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 APrP sc -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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“…The initial model was that of feeding mice a diet rich in casein, which includes a k fraction that is amyloidogenic; later, serial injections of azocasein were used; however, these were often unreliable between laboratories, evened somewhat by allowing bacterial growth in the preparations. Similar models used Freund's adjuvant, LPS, and certain infectious agents (e.g., Mycobacterium butyricum) (8). These models were noted to be "biphasic," with an induction-phase notable for the dominance of PAS-positive glycoprotein-rich macrophage preceding the actual appearance of amyloid, initially in a splenic periportal distribution, followed by periportal hepatic deposits, and finally glomerular amyloid.…”

mentioning

confidence: 99%

Amyloid and inflammation

Gorevic¹

2013

Proc. Natl. Acad. Sci. U.S.A.

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Animal models for reactive amyloidosis

Cited by 48 publications

References 45 publications

An Ancillary Tool for the Diagnosis of Amyloid A Amyloidosis in a Variety of Domestic and Wild Animals

An Ancillary Tool for the Diagnosis of Amyloid A Amyloidosis in a Variety of Domestic and Wild Animals

Protein folding pathology in domestic animals

Amyloid and inflammation

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