Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P43026 (lipopolysaccharide)
 62,215 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Reactive AA amyloidosis can be induced in mice in a model of sustained inflammation following daily casein subcutaneous injections. However, the development of AA amyloidosis is known to vary in different strains of mice. The C57BL/6 strain is susceptible to the development of amyloidosis while the A/J strain is resistant. The degradation of purified serum amyloid A (SAA) protein by human monocytes as well as by mouse macrophages has been shown. The resistance/susceptibility of different mouse strains to the development of systemic amyloidosis may therefore be related to a difference in the ability of macrophages to degrade SAA. The authors have used bone marrow-derived macrophage cell lines obtained from susceptible C57BL/6 (ANA-1) and resistant A/J (A/J 10) mouse strains to compare their ability to degrade HDL-SAA in vitro. Cells were incubated with HDL-SAA for up to 72 h and the culture medium was analysed by SDS-PAGE to determine the rate of SAA degradation by the macrophages. The A/J 10 cells (resistant) were found to initiate a constant HDL-SAA degradation promptly whereas ANA-1 cells (susceptible) showed an intermittent block in the degradation of the precursor. Activation of macrophages by lipopolysaccharide (LPS) or interferon-gamma (IFN-gamma) hampered the precursor degradation suggesting that the activation process may favour extracellular accumulation of the precursor leading to a partial degradation and fibril formation.
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PMID:Degradation of amyloid A precursor protein SAA by macrophage cell lines obtained from amyloid resistant and susceptible strains of mice. 910 21

Studies of amyloid enhancing factor (AEF)-induced amyloidosis are commonly performed in mice. In mink, earlier studies of amyloid A (AA) amyloidosis showed that the predeposition phase was highly variable. Thus, the aim of the study was to establish an AEF-induced AA amyloidosis model in mink to facilitate studies of early amyloid deposition in a species with prominent ellipsoids, anatomical structures lacking in mice but present in most other mammals. AEF was extracted from mink spleens containing AA. Mink received one intravenous injection of AEF and repeated subcutaneous injections of lipopolysaccharide (LPS) as an inflammatory stimulus. On day 4, small amounts of amyloid were detected in the marginal zone in the spleen. On day 7, considerable amyloid deposition was detected in the ellipsoids and marginal zones in the spleen and in the space of Disse in the liver. By immunohistochemistry, the deposits were identified as AA amyloid. Immunolabeling was also detected in lymphoid follicles and the red pulp of some animals. Control animals receiving only AEF were negative. Control animals receiving only LPS were negative except for one of three animals which had small amounts of amyloid in the spleen. The mink AEF model is a suitable tool to study the development of AA amyloidosis in a species with a spleen containing both well-developed ellipsoids and marginal zone.
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PMID:Rapid induction of experimental AA amyloidosis in mink by intravenous injection of amyloid enhancing factor. 1826 18

The authors describe a spontaneous case of amyloid A (AA) amyloidosis in an adult female Japanese quail ( Coturnix japonica). The bird developed AA amyloidosis secondary to chronic peritonitis caused by a Gram-negative bacillus infection. Mild amyloid deposition was also identified in the intestinal tract of apparently healthy adult individuals, suggesting that quail may develop intestinal amyloidosis with age. Based on these observations, it was hypothesized that quail can develop AA amyloidosis following inflammatory stimulation with lipopolysaccharide (LPS). Therefore, adult quail were repeatedly injected with LPS and the development of AA amyloidosis was confirmed. The amyloid deposition in this model increased when quail amyloid was intravenously injected as an amyloid-enhancing factor. The experiments were repeated with young quail, but amyloid deposits were not observed following LPS injections. However, AA amyloidosis did develop when quail amyloid was injected in addition to LPS. These results indicated that adult quail develop AA amyloidosis after inflammatory stimulation with LPS. Furthermore, quail AA amyloidosis was shown to have transmissibility regardless of age. Interestingly, the authors found that administration of chicken amyloid fibrils also induced AA amyloidosis in young quail. This is the first report of cross-species transmission of avian AA amyloidosis.
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PMID:Spontaneous, Experimentally Induced, and Transmissible AA Amyloidosis in Japanese Quail ( Coturnix japonica). 2881 32

In poultry and zoo birds, mass outbreaks of amyloid A (AA) amyloidosis are often reported, and horizontal transmission is considered as one of the causes. However, oral transmission of avian AA amyloidosis in nature has been unclear. In order to clarify the horizontal transmission of avian AA amyloidosis, basic research using an appropriate oral transmission model is necessary. In this study, we developed an oral transmission model of AA amyloidosis using quails, and assessed the oral transmission efficiency of AA amyloidosis in quails and mice. Young quails, adult quails, and young mice received inflammatory stimulation with lipopolysaccharide; simultaneously, homogeneous amyloid fibrils were orally or intravenously administered. By histological examination, induction of amyloidosis by oral or intravenous administration of amyloid was confirmed in all species. Furthermore, both quail and murine AA amyloidosis were orally transmitted in a dose-dependent manner. These results support the possibility of horizontal transmission of avian AA amyloidosis in nature. This model will be able to contribute to the elucidation of spontaneous horizontal transmission of avian AA amyloidosis in the future. RESEARCH HIGHLIGHTS Quail AA amyloidosis was orally transmitted in a dose-dependent manner. Oral transmission was less efficient than intravenous transmission. In-cage horizontal transmission did not occur during 4-week cohabitation. Amyloid deposition in tissues of quail was grossly visible.
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PMID:Experimental model of oral transmissible AA amyloidosis in quails. 3119 79