Tissue Distribution, Biochemical Properties, and Transmission of Mouse Type A AApoAII Amyloid Fibrils

Korenaga, Tatsumi; Fu, Xiaoying; Xing, Yanming; Matsusita, T.; Kuramoto, Kazunao; Syumiya, Seigo; Hara, Kazuhiro; Naiki, Hironobu; Ueno, Masaki; Ishihara, Tokuhiro; Hosokawa, Masanori; Mori, Masayuki; Higuchi, Kenichi

doi:10.1016/s0002-9440(10)63718-2

Cited by 37 publications

(22 citation statements)

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“…We have previously showed that the degree of senile apoA-II amyloid deposition in mouse strains varied with the apoA-II allele such that Apoa2 c 4Apoa2 a 4Apoa2 b . 13,14 Elucidation of the mechanism by which amyloidogenic apoA-IIs (Apoa2 c and Apoa2 a ) induce a low concentration of HDL should shed light on the pathogenesis of amyloidosis (Figure 3). We have previously demonstrated that the mRNA level, synthesis rate, plasma clearance rates and translational efficiencies of apoA-II were similar in SAMP1 (Apoa2 c ) and SAMR1 (Apoa2 b ) mice.…”

Section: Discussionmentioning

confidence: 99%

“…Injection of AApoAII fibrils also induced amyloidosis in less-amyloidogenic mouse strains with Apoa2 a or Apoa2 b alleles. 13,14 Injection of various kinds of amyloid fibrils into R1.P1-Apoa2 c mice also induced amyloidosis. 15 These results demonstrated that a common amyloid fibril structure could serve as a seed for amyloid fibril formation (cross-seeding) in vivo.…”

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Amyloidosis in transgenic mice expressing murine amyloidogenic apolipoprotein A-II (Apoa2)

Yao

et al. 2007

Laboratory Investigation

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In mice, apolipoprotein A-II (apoA-II) self-associates to form amyloid fibrils (AApoAII) in an age-associated manner. We postulated that the two most important factors in apoA-II amyloidosis are the Apoa2 c allele, which codes for the amyloidogenic protein APOA2C (Gln5, Ala38) and transmission of amyloid fibrils. To characterize further the contribution of the Apoa2 c allele to amyloidogenesis and improve detection of amyloidogenic materials, we established transgenic mice that overexpress APOA2C protein under the cytomegalovirus (CMV) immediate early gene (CMV-IE) enhancer/ chicken b promoter. Compared to transgene negative (Tg À/À ) mice that express apoA-II protein mainly in the liver, mice homozygous (Tg þ / þ ) and heterozygous (Tg þ /À ) for the transgene express a high level of apoA-II protein in many tissues. They also have higher plasma concentrations of apoA-II, higher ratios of ApoA-II/apolipoprotein A-I (ApoA-I) and higher concentrations of high-density lipoprotein (HDL) cholesterol. Following injection of AApoAII fibrils into Tg þ / þ mice, amyloid deposition was observed in the testis, liver, kidney, heart, lungs, spleen, tongue, stomach and intestine but not in the brain. In Tg þ / þ mice, but not in Tg À/À mice, amyloid deposition was induced by injection of less than 10 À8 mg AApoAII fibrils. Furthermore, deposition in Tg þ / þ mice occurred more rapidly and to a greater extent than in Tg À/À mice. These studies indicate that increased levels of APOA2C protein lead to earlier and greater amyloid deposition and enhanced sensitivity to the transmission of amyloid fibrils in transgenic mice. This transgenic mouse model should prove valuable for studies of amyloidosis.

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Section: Discussionmentioning

confidence: 99%

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confidence: 96%

Amyloidosis in transgenic mice expressing murine amyloidogenic apolipoprotein A-II (Apoa2)

Yao

et al. 2007

Laboratory Investigation

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“…In addition to foie gras, meat derived from sheep (16) and seemingly healthy cattle (17) may represent other dietary sources of this material. Further, the fact that chemically heterologous fibrils can serve as AEF, as demonstrated in experimental models of AA (18)(19)(20) and AApoAII amyloidosis (21)(22)(23), suggests that it may be hazardous for individuals who are prone to develop other types of amyloid-associated disorders, e.g., Alzheimer's disease or type II diabetes, to consume such products.…”

Section: (9)mentioning

confidence: 99%

Amyloidogenic potential of foie gras

Solomon

Richey

Murphy

et al. 2007

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

117

103

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The human cerebral and systemic amyloidoses and prionassociated spongiform encephalopathies are acquired or inherited protein folding disorders in which normally soluble proteins or peptides are converted into fibrillar aggregates. This is a nucleation-dependent process that can be initiated or accelerated by fibril seeds formed from homologous or heterologous amyloidogenic precursors that serve as an amyloid enhancing factor (AEF) and has pathogenic significance in that disease may be transmitted by oral ingestion or parenteral administration of these conformationally altered components. Except for infected brain tissue, specific dietary sources of AEF have not been identified. Here we report that commercially available duck-or goose-derived foie gras contains birefringent congophilic fibrillar material composed of serum amyloid A-related protein that acted as a potent AEF in a transgenic murine model of secondary (amyloid A protein) amyloidosis. When such mice were injected with or fed amyloid extracted from foie gras, the animals developed extensive systemic pathological deposits. These experimental data provide evidence that an amyloid-containing food product hastened the development of amyloid protein A amyloidosis in a susceptible population. On this basis, we posit that this and perhaps other forms of amyloidosis may be transmissible, akin to the infectious nature of prion-related illnesses.amyloid protein A amyloidosis ͉ amyloid-enhancing factor ͉ protein aggregation ͉ rheumatoid arthritis ͉ transmissibility A myloid protein A amyloidosis (AA) occurs in patients with rheumatoid arthritis and other chronic inflammatory diseases and results from a sustained elevation of the apolipoprotein serum amyloid A (SAA) protein produced by hepatocytes under regulation by interleukin (IL)-1, IL-6, and tumor necrosis factor (1). This acute-phase reactant is cleaved into an Ϸ76-residue N-terminal fragment deposited as amyloid predominately in the kidneys, liver, and spleen. The disorder also can be induced experimentally in susceptible strains of mice by inflammatory stimuli that result in an Ͼ1,000-fold increase in SAA concentration (2). Further, the lag phase of this process is greatly decreased by injecting or feeding animals extracts of amyloidladen spleens of affected mice (2-5).To determine whether amyloid-containing food products exhibit amyloid enhancing factor (AEF) activity, we used a more robust in vivo murine model of AA amyloidosis involving mice carrying the human IL-6 (hIL-6) gene under control of either the murine metallothionein-1 (MT-1) (MT-1/hIL-6) or histocompatibility H2-L d (H2/hIL-6) promoter (6). Typically, AA amyloid develops in these animals at Ϸ5 mo of age and is initially located predominately in the perifollicular regions of the spleen. Over the next 2-3 mo, the deposits spread rapidly into the liver parenchyma, renal glomerular and intertubular regions, cardiac muscle, tongue, and gastrointestinal tract and lead to death at Ϸ8-9 mo. However, by injection into 8-wk-old transgenic mice of a ...

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“…The active component in these different preparations, named amyloid-enhancing factor (AEF), is known to serve as a seed for fibril formation (14). In addition to murine AA amyloidosis, murine apolipoprotein A-II amyloidosis also is transmittable (15,16), pointing to a general mechanism in the pathogenesis of systemic amyloidosis. Characterization of AEF, derived from animals with AA amyloidosis, demonstrated that it contained small AA-fibril fragments, and it was proposed that its amyloidenhancing activity was related to these fragments (17).…”

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Protein fibrils in nature can enhance amyloid protein A amyloidosis in mice: Cross-seeding as a disease mechanism

Lundmark

Westermark²,

Olsén³

et al. 2005

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

276

202

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Secondary, or amyloid protein A (AA), amyloidosis is a complication of chronic inflammatory diseases, both infectious and noninfectious. AA constitutes the insoluble fibrils, which are deposited in different organs, and is a major N-terminal part of the acute phase protein serum AA. It is not known why only some patients with chronic inflammation develop AA amyloidosis. Nucleation is a widely accepted mechanism in amyloidogenesis. Preformed amyloid-like fibrils act as nuclei in amyloid fibril formation in vitro, and AA amyloid fibrils and synthetic amyloid-like fibrils also may serve as seed for fibril formation in vivo. In addition to amyloid fibrils, there is a variety of similar nonmammalian protein fibrils with ␤-pleated structure in nature. We studied three such naturally occurring protein fibrils: silk from Bombyx mori, Sup35 from Saccharomyces cerevisiae, and curli from Escherichia coli. Our results show that these protein fibrils exert amyloid-accelerating properties in the murine experimental AA amyloidosis, suggesting that such environment factors may be important risk factors in amyloidogenesis.amyloid ͉ seeding ͉ protein misfolding ͉ aggregation ͉ prion

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Tissue Distribution, Biochemical Properties, and Transmission of Mouse Type A AApoAII Amyloid Fibrils

Cited by 37 publications

References 50 publications

Amyloidosis in transgenic mice expressing murine amyloidogenic apolipoprotein A-II (Apoa2)

Amyloidosis in transgenic mice expressing murine amyloidogenic apolipoprotein A-II (Apoa2)

Amyloidogenic potential of foie gras

Protein fibrils in nature can enhance amyloid protein A amyloidosis in mice: Cross-seeding as a disease mechanism

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