Parallel Intralysosomal Amyloid Fibrils, a Possible Result of Phagocytosis

Gruys, E.; Castaño, María Fabiola Toro

doi:10.1177/030098587701400413

Cited by 6 publications

(6 citation statements)

References 21 publications

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“…Intracellular formation of amyloid as intralysosomal parallel fibrillar arrangement was also shown by Gruys (1975) in the macrophage-like cells and reticular interstitial cells of the medulla of the bovine kidney. However, in a later study, this author, in collaboration with Castano (1977) pointed out that intralysosomal amyloid may occur in parallel fibrillar arrangement as the possible result of phagocytosis; this is not, therefore, a definite indication of amyloid production by the cell.…”

Section: Discussionmentioning

confidence: 94%

Multicentric Amyloid Containing Cutaneous Trabecular Carcinoma

Abaci

Zak

1979

J Cutan Pathol

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Section: Discussionmentioning

confidence: 94%

Multicentric Amyloid Containing Cutaneous Trabecular Carcinoma

Abaci

Zak

1979

J Cutan Pathol

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“…The Same argument can be raised for horse AA-amyloid. In bovine A A amyloidosis intralysosomal I (AL-amyloid) and (B) Horse S(AA-amyloid) (Gruys and Castano 1977) was shown to be the result of phagocytosis (Gruys 1979). Studies using induced phagocytosis of bovine amyloid in rats and studies of casein-induced amyloid in hamsters (Gruys and Castano 1977;Gruys, Timmermans and van Ederen 1979) revealed parallel intralysosomal fibrils in the rat and deposits without intracellular amyloid in the hamsters.…”

Section: Discussionmentioning

confidence: 99%

“…In bovine A A amyloidosis intralysosomal I (AL-amyloid) and (B) Horse S(AA-amyloid) (Gruys and Castano 1977) was shown to be the result of phagocytosis (Gruys 1979). Studies using induced phagocytosis of bovine amyloid in rats and studies of casein-induced amyloid in hamsters (Gruys and Castano 1977;Gruys, Timmermans and van Ederen 1979) revealed parallel intralysosomal fibrils in the rat and deposits without intracellular amyloid in the hamsters. Cleavage of the protein A A precursor, SAA, by mononuclear surface serine esterases was found (Lavie, Zucker-Franklin and Franklin 1978;Lavie, Zucker-Franklin and Franklin 1980), although amyloid fibrils were not formed in vitro.…”

Section: Discussionmentioning

confidence: 99%

Amyloid in the horse: A report of nine cases

Andel

Gruys

Kroneman

et al. 1988

Equine Veterinary Journal

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Out of approximately 16,000 horses referred for clinical examination, nine had amyloidosis. Six of these horses had localised amyloid deposits in the wall of the nasal meatus and ventral turbinates associated with epistaxis. Horse 1 also developed malignant histiolymphocytic lymphosarcomas. The amyloid deposits were potassium permanganate-resistant and tryptophan-positive. Gel filtration of solubilised amyloid fibrils from Horse 1 revealed a major retarded fraction with an apparent molecular weight of 20 kD. This protein had an amino acid composition similar to human AL-amyloid proteins and horse immunoglobulin light chains. On Western blot a strong cross-reaction was observed between horse lgGza light chains and the Horse 1 amyloid. Horses 7 to 9 had suppurative verminous aneurysm, tuberculosis and an adrenal cortical adenoma, respectively, and had generalised amyloid deposits in liver and spleen. These amyloid deposits were found to be potassium permanganatesensitive and positive for tryptophan. Gel filtration of solubilised amyloid fibrils from Horse 8 revealed a major retarded fraction (protein AA) with an apparent molecular weight of 10 kD. Immunoperoxidase-antiperoxidase staining showed the localised deposits to be negative or only weakly positive with antisera against bovine, hamster, dog and human protein AA and to be positive with anti-horse-one amyloid protein. The generalised deposits were found to be positive with the antisera against allogenic protein AA. The results of the potassium permanganate incubation, biochemistry, immunoblotting and immunochemistry, indicate that the localised amyloid of Horse 1 and most likely the amyloid of Horses 2 to 6, is of the AL-type. The generalised amyloid deposits were found to be of the AA type. Scrapie prions aggregate to form amyloid-like birefringent rods. Cell. 35,349-358. scnrrl/. .J. I~~~~~~~~~~~~. ' 20. SMI.

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“…The first studies (with immunoglobulin light chain proteins and insulin) were under lysosomal pH and proteolytic conditions. Parallel-aligned intralysosomal amyloid, however, also developed in rats after phagocytosis of injected bovine fibril suspensions (Gruys and Castaño, 1977).…”

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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Parallel Intralysosomal Amyloid Fibrils, a Possible Result of Phagocytosis

Cited by 6 publications

References 21 publications

Multicentric Amyloid Containing Cutaneous Trabecular Carcinoma

Multicentric Amyloid Containing Cutaneous Trabecular Carcinoma

Amyloid in the horse: A report of nine cases

Protein folding pathology in domestic animals

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