Chemical typing of porcine systemic amyloid as AA-amyloid

Niewold, Theodoor; Murphy, Charles L.; Toussaint, Mathilda J. M.; Solomon, Alan; Gruys, E.

doi:10.1080/13506120500231806

Cited by 9 publications

(12 citation statements)

References 13 publications

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“…Niewold et al found a unique sequence of SAA that was highly similar to that of the N -terminus of SAA2. 4 This sequence was present in AA deposits in the tissue of a pig and might, therefore, play a role in the pathogenesis. However, this is the only published example.…”

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confidence: 93%

“…There are only 3 published cases of porcine AA amyloidosis. 4,8,14 In pigs, bacterial diseases occur frequently, and circulating SAA concentrations increase during the infection. 13 Further, circulating SAA concentrations increase in pigs experimentally infected with Actinobacillus pleuropneumoniae and Staphylococcus aureus , 1 although there are no reports of concurrent AA amyloidosis.…”

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confidence: 99%

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Identification of a Unique Amyloid Sequence in AA Amyloidosis of a Pig Associated With Streptococcus Suis Infection

et al. 2016

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Here we report a pig with amyloid A (AA) amyloidosis associated with Streptococcus suis infection and identification of a unique amyloid sequence in the amyloid deposits in the tissue. Tissues from the 180-day-old underdeveloped pig contained foci of necrosis and suppurative inflammation associated with S. suis infection. Congo red stain, immunohistochemistry, and electron microscopy revealed intense AA deposition in the spleen and renal glomeruli. Mass spectrometric analysis of amyloid material extracted from the spleen showed serum AA 2 (SAA2) peptide as well as a unique peptide sequence previously reported in a pig with AA amyloidosis. The common detection of the unique amyloid sequence in the current and past cases of AA amyloidosis in pigs suggests that this amyloid sequence might play a key role in the development of porcine AA amyloidosis. An in vitro fibrillation assay demonstrated that the unique AA peptide formed typically rigid, long amyloid fibrils (10 nm wide) and the N-terminus peptide of SAA2 formed zigzagged, short fibers (7 nm wide). Moreover, the SAA2 peptide formed long, rigid amyloid fibrils in the presence of sonicated amyloid fibrils formed by the unique AA peptide. These findings indicate that the N-terminus of SAA2 as well as the AA peptide mediate the development of AA amyloidosis in pigs via cross-seeding polymerization.

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confidence: 93%

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confidence: 99%

Identification of a Unique Amyloid Sequence in AA Amyloidosis of a Pig Associated With Streptococcus Suis Infection

et al. 2016

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“…44 Pigs rarely develop amyloidosis, and there are only a few porcine cases reported so far. 45 –49 Those cases were identified as a consequence of reactive systemic amyloidosis, and underlying conditions were in association with bacterial infection, leukosis, and hyperimmunization. 45 –47,49 Most cases of amyloidosis in animals are of the reactive systemic type, and common sites of amyloid distribution are the kidney, liver, spleen, thyroid gland, adrenal gland, and small muscular arteries and arterioles in many organs.…”

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confidence: 99%

Spontaneous Age-Related Histopathological Changes in Microminipigs

Kangawa

Nishimura²,

Nishimura³

et al. 2019

Toxicol Pathol

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Microminipigs have become an attractive animal model for toxicology and pharmacology studies and for human disease models, owing to their manageable size. Although there are numerous reports of spontaneous age-related lesions in mice, rats, dogs, and monkeys, those in minipigs are scarce. In the present study, spontaneous age-related histopathological changes were investigated using 37 microminipigs (20 males and 17 females) that were 6 months to 10 years of age. Abnormal deposits of materials were evident in several animals from 6 years of age, and these deposits included amyloid in the renal medulla, thyroid gland, and adrenal gland, hyaline droplets in glomeruli, and fibrillar inclusions in neurons. Arterial sclerosing changes (intimal thickening, intimal proliferation, and medial mineralization) and proliferative lesions (hyperplasia of hepatocytes, follicular cells, Leydig cells, and uterine endometrial glands) were present at 4 years of age and beyond. Renal adenoma, uterine leiomyoma, and Leydig cell tumor were observed in several microminipigs. Moreover, glomerulosclerosis, renal interstitial fibrosis, thymic involution, and adrenocortical cell vacuolation were common in aging microminipigs. Since knowledge of age-related changes is helpful for pathologists, the basic information obtained in this study will be a useful reference for all future toxicity evaluations in microminipigs.

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“…cattle and birds) but is exceptionally rare in pigs. 42 suggesting that APrP should it reside in pig fat would be traceable using newly developed screening methods. 37 FIGURE 5.…”

Section: Use Of Materials Derived From Pig In View Of Porcine Prp Amymentioning

confidence: 99%

Porcine prion protein amyloid

Hammarström¹,

Nyström

2015

Prion

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ABSTRACT. Mammalian prions are composed of misfolded aggregated prion protein (PrP) with amyloid-like features. Prions are zoonotic disease agents that infect a wide variety of mammalian species including humans. Mammals and by-products thereof which are frequently encountered in daily life are most important for human health. It is established that bovine prions (BSE) can infect humans while there is no such evidence for any other prion susceptible species in the human food chain (sheep, goat, elk, deer) and largely prion resistant species (pig) or susceptible and resistant pets (cat and dogs, respectively). PrPs from these species have been characterized using biochemistry, biophysics and neurobiology. Recently we studied PrPs from several mammals in vitro and found evidence for generic amyloidogenicity as well as cross-seeding fibril formation activity of all PrPs on the human PrP sequence regardless if the original species was resistant or susceptible to prion disease. Porcine PrP amyloidogenicity was among the studied. Experimentally inoculated pigs as well as transgenic mouse lines overexpressing porcine PrP have, in the past, been used to investigate the possibility of prion transmission in pigs. The pig is a species with extraordinarily wide use within human daily life with over a billion pigs harvested for human consumption each year. Here we discuss the possibility that the largely prion disease resistant pig can be a clinically silent carrier of replicating prions.

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Chemical typing of porcine systemic amyloid as AA-amyloid

Cited by 9 publications

References 13 publications

Identification of a Unique Amyloid Sequence in AA Amyloidosis of a Pig Associated With Streptococcus Suis Infection

Identification of a Unique Amyloid Sequence in AA Amyloidosis of a Pig Associated With Streptococcus Suis Infection

Spontaneous Age-Related Histopathological Changes in Microminipigs

Porcine prion protein amyloid

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