Kinetics of Glycosaminoglycan Deposition in Splenic AA Amyloidosis Induced in Mink

Wien, Tale Norbye; Sørby, Randi; Omtvedt, L. A.; Landsverk, Thor; Husby, Gunnar

doi:10.1111/j.0300-9475.2004.01520.x

Cited by 12 publications

(3 citation statements)

References 45 publications

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“…In our material there was no association between amyloidosis and chronic infections, and amyloidosis appeared to be a primary pathological process. However, this and previous studies have demonstrated both AA and AL amyloidosis in martens [ 29 , 30 , 122 , 125 ], suggesting that in martens amyloidosis cannot be attributed to a single cause. Genetics has been proposed to play a role in black footed ferrets [ 30 ] and stone martens [ 126 ], however, evidence of the transmissibility of the amyloid protein has been recently shown in laboratory animals [ 127 , 128 ].…”

Section: Discussioncontrasting

confidence: 70%

Causes of mortality and morbidity in free-ranging mustelids in Switzerland: necropsy data from over 50 years of general health surveillance

et al. 2018

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BackgroundAlthough mustelids occur worldwide and include a wide range of species, little is known about the diseases affecting them. Mustelids have regularly been submitted for post mortem investigation in the framework of the program for general wildlife health surveillance in Switzerland, which has been in place for nearly 60 years. We performed a retrospective analysis of the necropsy reports on mustelids submitted to the diagnostic service of the University of Bern. The aims of this study were to present an overview of the causes of mortality and morbidity observed in these carnivores, to assess differences among species, to assess changes in disease detection over the study period, and to describe the pathology of selected diseases.ResultsFive hundred and sixty-six reports from 1958 to 2015 were analyzed. Most animals were stone martens (Martes foina, 46%) and badgers (Meles meles, 44%); the remaining species were polecats (Mustela putorius, 4.7%), pine martens (Martes martes, 2%), stoats (Mustela erminea, 1.4%), weasels (Mustela nivalis, 0.8%) and otters (Lutra lutra, 0.3%). Infectious diseases (n = 262) were frequent and were mostly bacterial or viral; non-infectious conditions (n = 169) were less common and were mostly traumatic or due to metabolic disorders. The most frequent diagnoses included distemper (75% were badgers), amyloidosis (96% were martens), bacterial respiratory infections (all mustelids), biting lice (badgers only) and pulmonary and gastro-intestinal helminths (all species). Less frequent diseases included histoplasmosis (badgers only), aspergillosis, toxoplasmosis, hepatozoonosis, and sarcoptic mange. Lesions due to infection with distemper virus were primarily appreciated in the respiratory tract and central nervous system; they presented species-specific characteristics such as necrosis in the ependyma in badgers and absence of syncytia in stone martens. Amyloidosis in martens was multisystemic in most cases and included both AA and AL amyloidosis; the main macroscopic change was severe splenomegaly.ConclusionInfectious diseases were the most frequent causes of morbidity and mortality of mustelids, with marked species-specific differences. Lung and skin were the most commonly affected organs. Contagious diseases such as canine distemper, sarcoptic mange and rabies in mustelids showed a similar temporal pattern as in red foxes (Vulpes vulpes), suggesting pathogen spillovers from foxes to mustelids.

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Section: Discussioncontrasting

confidence: 70%

Causes of mortality and morbidity in free-ranging mustelids in Switzerland: necropsy data from over 50 years of general health surveillance

et al. 2018

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“…As deposition of the HSPG core protein agrin has previously been described only in relation to Aβ in AD [66,67,70] and in experimental AA amyloidosis [71], our findings indicate that this basement membrane‐associated HSPG may have a more generic role in the pathogenesis of cerebral and systemic amyloid diseases. It has been shown that under experimental conditions agrin is able to bind, probably through its HS GAG side chains, to the fibrillar, but not to the soluble form of Aβ and that it is also able to stabilize and protect Aβ fibrils from proteolytic degradation [70].…”

Section: Discussionsupporting

confidence: 59%

Molecular chaperons, amyloid and preamyloid lesions in the BRI2 gene‐related dementias: a morphological study

Lashley

Holton

Verbeek

et al. 2006

Neuropathology Appl Neurobio

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Molecular chaperons or amyloid-associated proteins (AAPs) are deposited in vascular and parenchymal amyloid lesions in Alzheimer's disease (AD) and other amyloidoses. AAPs, such as apolipoprotein E (ApoE) or apolipoprotein J (ApoJ) have been strongly implicated in the pathogenesis of AD in vitro and in vivo. Furthermore the possession of the ApoE in4 allele is a well-studied risk factor for AD. In view of the similarities between AD and both familial British dementia (FBD) and familial Danish dementia (FDD), we investigated the presence of AAPs in these two diseases to understand better their role in the general process of amyloidogenesis. Immunohistochemistry for ApoE, ApoJ, serum amyloid P (SAP), alpha-1-antichymotrypsin, cystatin C, heparan sulphate proteoglycans, such as agrin, perlecan, syndecans, glypican-1 and for heparan sulphate glycosaminoglycan (HS GAG) side chains was carried out together with immunohistochemical preparations specific to the amyloid subunits. Significant or extensive staining for ApoE, ApoJ, agrin, glypican-1 and HS GAG side chains was found in both amyloid (fibrillar) and preamyloid (nonfibrillar) deposits in FBD and FDD. The remaining AAPs, including SAP, were predominantly found in amyloid lesions. Only very weak staining was present in a small proportion of the amyloid lesions using perlecan immunohistochemistry. These findings suggest that the deposition patterns of AAPs in FBD and FDD are mostly similar to those in AD. The presence of AAPs in the preamyloid lesions supports the notion that chaperon molecules may play a role in the early steps of fibrillogenesis.

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“…Although HS is the most abundant GAG present in AA deposits and has been the most widely investigated in SAA studies, various GAGs, in particular CS, have been identified in the amyloid deposits of afflicted individuals and in experimental models of the disease [55-57]. Interestingly, in a study of mice lacking serum amyloid P (SAP), a major component of the amyloid deposits found in AA amyloidosis, the amyloid deposits contained significant amounts of CS in the form of spherical particles [55].…”

Section: Discussionmentioning

confidence: 99%

Divergent effect of glycosaminoglycans on the in vitro aggregation of serum amyloid A

et al. 2014

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Serum amyloid A (SAA) is an apolipoprotein involved in poorly understood roles in inflammation. Upon trauma, hepatic expression of SAA rises 1000 times the basal levels. In the case of inflammatory diseases like rheumatoid arthritis, there is a risk for deposition of SAA fibrils in various organs leading to Amyloid A (AA) amyloidosis. Although the amyloid deposits in AA amyloidosis accumulate with the glycosaminoglycan (GAG) heparan sulfate, the role GAGs play in the function and pathology of SAA is an enigma. It has been shown that GAG sulfation is a contributing factor in protein fibrillation and for co-aggregating with a plethora of amyloidogenic proteins. Herein, the effects of heparin, heparan sulfate, hyaluronic acid, chondroitin sulfate A, and heparosan on the oligomerization and aggregation properties of pathogenic mouse SAA1.1 were investigated. Delipidated SAA was used to better understand the interactions between SAA and GAGs without the complicating involvement of lipids. The results revealed—to varying degrees—that all GAGs accelerated SAA1.1 aggregation, but had variable effects on its fibrillation. Heparan sulfate, hyaluronic acid, and heparosan did not affect much the fibrillation of SAA1.1. In contrast, chondroitin sulfate A blocked SAA fibril formation and facilitated the formation of spherical aggregates of various sizes. Interestingly, heparin caused formation of spherical SAA1.1 aggregates of various sizes, vast amounts of thin protofibrils, and few long fibrils of various heights. These results suggest that GAGs may have an intrinsic and divergent influence on the aggregation and fibrillation of HDL-free SAA1.1 in vivo, with functional and pathological implications.

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Kinetics of Glycosaminoglycan Deposition in Splenic AA Amyloidosis Induced in Mink

Cited by 12 publications

References 45 publications

Causes of mortality and morbidity in free-ranging mustelids in Switzerland: necropsy data from over 50 years of general health surveillance

Causes of mortality and morbidity in free-ranging mustelids in Switzerland: necropsy data from over 50 years of general health surveillance

Molecular chaperons, amyloid and preamyloid lesions in the BRI2 gene‐related dementias: a morphological study

Divergent effect of glycosaminoglycans on the in vitro aggregation of serum amyloid A

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