Amyloid Enhancing Factor and Dietary Transmission in Accelerated Amyloid A Amyloidosis

Elliott-Bryant, Rosemary; Cathcart, Edgar S.

doi:10.1006/clin.1998.4555

Cited by 25 publications

(13 citation statements)

References 24 publications

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“…Although AA amyloidogenesis was shown to be enhanced by oral administration of a splenic extract from an AA mouse, this material was reported not to contain AA protein (47). However, given the extremely potent effect of our AEF, we attribute this response to the presence of trace amounts of AA-fibrillar material in the preparation used.…”

Section: Discussionmentioning

confidence: 86%

Transmissibility of systemic amyloidosis by a prion-like mechanism

Lundmark

Westermark

Nyström

et al. 2002

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

249

213

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3T3-L1 adipocytes were incubated in serum-free media at 37°C with (dashed line) or without (solid line) 100 ng͞ml insulin for 8 h. Isoproterenol (10 M) was then added for the indicated time course at 37°C, and intracellular cAMP was determined by enzyme immunoassay, as described in Materials and Methods. Data are from a typical experiment done in triplicate wells Ϯ SEM and are representative of three separate experiments. (B) 3T3-L1 adipocytes were incubated in serum-free media for 8 h. Where indicated, 100 ng͞ml insulin was added for 15 min before isoproterenol treatment. Cells were then treated with 10 M isoproterenol for 5 min at 37°C, and intracellular cAMP was determined by enzyme immunoassay, as described in Materials and Methods. Data are from a typical experiment done in triplicate wells Ϯ SEM and are representative of three separate experiments.www.pnas.org͞cgi͞doi͞10.1073͞pnas.0630528100 After this, cells were treated with 10 M isoproterenol for 5 min at 37°C. Cells were then washed with PBS at 37°C and restimulated with a second 10 M dose of isoproterenol for an additional 5 min at 37°C; intracellular cAMP was determined by enzyme immunoassay. (B) 3T3-L1 adipocytes were incubated at 37°C in serum-free media for 8 h in the presence (dashed lines) or absence (solid lines) of 100 ng͞ml insulin. Forskolin was added for the final 5 min, and intracellular cAMP levels were determined by enzyme-linked immunoassay. Data are from typical experiments done in triplicate wells and are representative of three separate experiments.

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Section: Discussionmentioning

confidence: 86%

Transmissibility of systemic amyloidosis by a prion-like mechanism

Lundmark

Westermark

Nyström

et al. 2002

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

249

213

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“…Disturbingly, this socalled 'amyloid enhancing factor' (AEF) effect has more recently been reproduced following oral administration of an AEF preparation. 18 This raised the possibility that a transmissible agent present in diet may be a contributory factor in AA amyloid fibril formation, analogous to the situation in the prion diseases, where the bovine spongiform encephalopathy has been transmitted from cattle to man as new variant Creutzfeldt-Jakob disease. 19 Hormonal influences may also predispose to AA amyloidosis, it being notable that amyloid developed only in male members of the Indian MWS family, and in none of the six affected female members.…”

Section: Discussionmentioning

confidence: 99%

Allelic variants in genes associated with hereditary periodic fever syndromes as susceptibility factors for reactive systemic AA amyloidosis

et al. 2004

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We investigated the hypothesis that low-penetrance mutations in genes (TNFRSF1A, MEFV and NALP3/CIAS1) associated with hereditary periodic fever syndromes (HPFs) might be risk factors for AA amyloidosis among patients with chronic inflammatory disorders, including rheumatoid arthritis (RA), juvenile idiopathic arthritis (JIA), Crohn's disease, undiagnosed recurrent fevers and HPFs themselves. Four of 67 patients with RA plus amyloidosis had MEFV variants compared with none of 34 RA patients without amyloid (P value ¼ 0.03). The E148Q variant of MEFV was present in two of the three patients with TNF receptor-associated periodic syndrome (TRAPS) complicated by amyloid in two separate multiplex TRAPS families containing 5 and 16 affected members respectively, and the single patient with Muckle-Wells syndrome who had amyloidosis was homozygous for this variant. The R92Q variant of TNFRSF1A was present in two of 61 JIA patients with amyloidosis, and none of 31 nonamyloidotic JIA patients. No HPF gene mutations were found in 130 healthy control subjects. Although allelic variants in HPFs genes are not major susceptibility factors for AA amyloidosis in chronic inflammatory disease, low-penetrance variants of MEFV and TNFRSF1A may have clinically significant proinflammatory effects.

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“…Injection of AApoAII amyloid fibrils dramatically accelerates progression of amyloidosis in young R1.P1-Apoa2 c mice [13]. The AEF preparation was also effective in promoting amyloid formation when administered orally [14,15]. These phenomena indicated that amyloid disease may be transmissible by oral ingestion of amyloid fibrils or amyloid-like pathologic agents.…”

Section: Introductionmentioning

confidence: 99%

Acceleration of murine AA amyloid deposition by bovine amyloid fibrils and tissue homogenates

Cui

Kawano

Hoshii

et al. 2008

Amyloid

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Acceleration of amyloid deposition by administration of amyloid fibrils and transmissibility of disease have been reported for several types of amyloidosis. Reactive amyloidosis (AA) occurs in a wide variety of domestic animal species and is characterized by amyloid deposition mainly in spleen, liver, and kidneys. Because the visceral organs of domestic animals have traditionally been used in Asian cuisines, it is important to examine whether dietary ingestion of the organs themselves (rather than purified amyloid fibrils) accelerates AA amyloid deposition. Herein, we show that murine AA amyloidosis develops rapidly after intraperitoneal or oral administration of purified amyloid fibrils or homogenates of amyloid-laden bovine liver. The amyloidosis development in mice was dependent on the concentration of amyloid fibrils or amyloidotic liver homogenates. We found that experimental murine AA amyloidosis was accelerated by dietary ingestion of both purified amyloid fibrils and tissue homogenates that contain amyloid fibrils. We also investigated livers of beef cattle and food chickens to examine whether they contain amyloid-enhancing factor activity. By microscopic examination of hematoxylin and eosin- and Congo red-stained sections, no amyloid deposition was detected in these livers, and no effective activity for experimental induction of AA amyloidosis in mice was detected in homogenates of these livers.

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Amyloid Enhancing Factor and Dietary Transmission in Accelerated Amyloid A Amyloidosis

Cited by 25 publications

References 24 publications

Transmissibility of systemic amyloidosis by a prion-like mechanism

Transmissibility of systemic amyloidosis by a prion-like mechanism

Allelic variants in genes associated with hereditary periodic fever syndromes as susceptibility factors for reactive systemic AA amyloidosis

Acceleration of murine AA amyloid deposition by bovine amyloid fibrils and tissue homogenates

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