Linkage of protection against amyloid fibril formation in the mouse to a single, autosomal dominant gene.

Gonnerman, Wayne A.; Elliott-Bryant, Rosemary; Carreras, Isabel; Sipe, Jean D.; Cathcart, Edgar S.

doi:10.1084/jem.181.6.2249

Cited by 19 publications

(16 citation statements)

References 20 publications

(19 reference statements)

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“…Recent studies have been designed to elucidate the mechanism of this resistance (Elliott-Bryant et al, 1996;Gonnerman et al, 1995Gonnerman et al, , 1996Liang et al, 1998). Results suggest that the CE/J mice, although they do not develop amyloidosis, have detectable AEF activity in the spleen .…”

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confidence: 99%

“…Furthermore, the SAA2.2 protein in CE/J mice was not degraded by peritoneal macrophages and SAA2.2 bound to the macrophages with a higher affinity than SAA1.1 or SAA2.1 (Elliot-Bryant et al, 1996;Liang et al, 1998). Amyloid immunity in the CE/J mouse was examined by crossing the CE/J mouse with the amyloidsusceptible CBA/J strain (Gonnerman et al, 1995). F2 generation animals expressed either the SAA1.1 and SAA2.1 isoforms, or the SAA2.2 isoform concomitantly with the SAA1.1 and SAA2.1 proteins.…”

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Expression of Mouse Apolipoprotein SAA1.1 in CE/J Mice: Isoform-Specific Effects on Amyloidogenesis

Zhu

Guo

et al. 2000

Laboratory Investigation

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Kentucky SUMMARY:Amyloid A (AA) amyloid deposition in mice is dependent upon isoform-specific effects of the serum amyloid A (SAA) protein. In type A mice, SAA1.1 and SAA2.1 are the major apolipoprotein-SAA isoforms found on high-density lipoproteins. During inflammation, both isoforms are increased 1000-fold, but only SAA1.1 is selectively deposited into amyloid fibrils. Previous studies showed that the CE/J mouse strain is resistant to amyloid induction. This resistance is not due to a deficiency in SAA synthesis, but is probably related to the unusual SAA isoform present. The CE/J mouse has a single acute-phase SAA protein (SAA2.2), which is a composite of the SAA1.1 and SAA2.1, with an amino terminus similar to the nonamyloidogenic SAA2.1. Recently, genetic experiments suggested that the SAA2.2 isoform might provide protection from amyloid deposition. To determine the amyloidogenic potential of the CE/J mouse, we generated SAA adenoviral vectors to express the various isoforms in vitro and in vivo. Purified recombinant SAA proteins demonstrated that SAA1.1 was fibrillogenic in vitro, whereas SAA2.2 was unable to form fibrils. Incubation of increasing concentrations of the nonamyloidogenic SAA2.2 protein with the amyloidogenic SAA1.1 did not inhibit the fibrillogenic nature of SAA1.1, or alter its ability to form extensive fibrils. Injection of the mouse SAA1.1 or SAA2.2 adenoviral vectors into mice resulted in isoform-specific expression of the SAA proteins. Amyloid induction after viral expression of the SAA1.1 protein resulted in the deposition of amyloid fibrils in the CE/J mouse, whereas SAA2.2 expression had no effect. Similar expression of the SAA2.2 protein in C57BL/6 mice did not alter amyloid deposition. These data demonstrate that the failure of the CE/J mouse to deposit amyloid is due to the structural inability of the SAA2.2 to form amyloid fibrils. This mouse provides a unique system to test the amyloidogenic potential of altered SAA proteins and to determine the important structural features of the protein. (Lab Invest 2000, 80:1797-1806.

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Expression of Mouse Apolipoprotein SAA1.1 in CE/J Mice: Isoform-Specific Effects on Amyloidogenesis

Zhu

Guo

et al. 2000

Laboratory Investigation

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“…Mice of the C57BL/6 and CBA/J strains are known to develop reactive AA amyloidosis within 15-21 days of casein treatment while mice of the A/J strain take more than 40 days to develop AA amyloidosis and are thus considered resistant to the development of amyloidosis. Genetic analysis has suggested that the relative resistance to the development of reactive AA amyloidosis seen in mice of the A/J strain is controlled by a single autosomal dominant gene [9][10][11].…”

Section: Introductionmentioning

confidence: 99%

Degradation of Amyloid A Precursor Protein SAA by Macrophage Cell Lines Obtained from Amyloid Resistant and Susceptible Strains of Mice

et al. 1997

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1997;45:354-360 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-g (IFN-g) 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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“…by repeated injections of casein, LPS, or silver nitrate) and should represent an amyloidogenic isotype. Amyloid resistant mouse strains were found to have a non-amyloidogenic acute phase SAA (Gonnerman et al, 1995;Liang et al, 1998). Rats were shown not to form acute phase SAA and AA-amyloid at all (Ren et al, 1999;Yu et al, 2000).…”

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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Linkage of protection against amyloid fibril formation in the mouse to a single, autosomal dominant gene.

Cited by 19 publications

References 20 publications

Expression of Mouse Apolipoprotein SAA1.1 in CE/J Mice: Isoform-Specific Effects on Amyloidogenesis

Expression of Mouse Apolipoprotein SAA1.1 in CE/J Mice: Isoform-Specific Effects on Amyloidogenesis

Degradation of Amyloid A Precursor Protein SAA by Macrophage Cell Lines Obtained from Amyloid Resistant and Susceptible Strains of Mice

Protein folding pathology in domestic animals

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