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BSE-associated prion-amyloid cardiomyopathy in primates.

Krasemann S, Mearini G, Krämer E, Wagenführ K, Schulz-Schaeffer W, Neumann M, Bodemer W, Kaup FJ, Beekes M, Carrier L, Aguzzi A, Glatzel M - Emerging Infect. Dis. (2013)

Bottom Line: Prion amyloidosis occurred in the heart of 1 of 3 macaques intraperitoneally inoculated with bovine spongiform encephalopathy prions.This macaque had a remarkably long duration of disease and signs of cardiac distress.Variant Creutzfeldt-Jakob disease, caused by transmission of bovine spongiform encephalopathy to humans, may manifest with cardiac symptoms from prion-amyloid cardiomyopathy.

View Article: PubMed Central - PubMed

Affiliation: University Medical Center Hamburg-Eppendorf, Hamburg, Germany.

ABSTRACT
Prion amyloidosis occurred in the heart of 1 of 3 macaques intraperitoneally inoculated with bovine spongiform encephalopathy prions. This macaque had a remarkably long duration of disease and signs of cardiac distress. Variant Creutzfeldt-Jakob disease, caused by transmission of bovine spongiform encephalopathy to humans, may manifest with cardiac symptoms from prion-amyloid cardiomyopathy.

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Related in: MedlinePlus

PrPSc distribution and content in brain of bovine spongiform encephalopathy (BSE)–infected rhesus macaques. A) Paraffin-embedded tissue blot of striatum and cerebellum show a typical BSE-like deposition pattern of PrPSc with no differences between individual BSE-diseased monkeys at 49, 59, and 61 months postinoculation (mpi). Scale bars = 1 mm. B) Western blot analysis for PrPSc in brain of BSE-infected monkeys with incubation times of 49, 59, and 61 mpi. PrPSc-type is as expected for BSE prions, and no major differences in PrPSc load were detected. All samples were proteinase K–digested; loading amount was 0.5 and 0.1 mg fresh wet tissue for each sample
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Figure 1: PrPSc distribution and content in brain of bovine spongiform encephalopathy (BSE)–infected rhesus macaques. A) Paraffin-embedded tissue blot of striatum and cerebellum show a typical BSE-like deposition pattern of PrPSc with no differences between individual BSE-diseased monkeys at 49, 59, and 61 months postinoculation (mpi). Scale bars = 1 mm. B) Western blot analysis for PrPSc in brain of BSE-infected monkeys with incubation times of 49, 59, and 61 mpi. PrPSc-type is as expected for BSE prions, and no major differences in PrPSc load were detected. All samples were proteinase K–digested; loading amount was 0.5 and 0.1 mg fresh wet tissue for each sample

Mentions: In 2002, three rhesus macaques were inoculated with BSE intraperitoneally (10 mL of a 10% homogenate of brain from BSE-diseased cattle). As controls, 2 rhesus macaques received saline (10 mL) and 1 was untreated. All procedures involving rhesus macaques were performed at the Institute of Neuropathology, University Medical Center Hamburg-Eppendorf (Hamburg, Germany), in accordance with the German Animal Welfare Act and the Council Directive 86/609/EEC (Permit 33.42502/08–08.02 LAVES, Lower Saxony, Germany). Animals were observed for clinical signs of prion disease and, when signs of terminal prion disease became evident, were euthanized and underwent autopsy. In all 3 BSE-challenged macaques and none of the controls a progressive neurologic disease developed 49, 59, and 61 months postinoculation. Examination of brain by using hematoxylin and eosin staining showed typical neuropathologic features of vCJD (data not shown) and abundant deposits of PrPSc in the cortex, basal ganglia, and cerebellum in paraffin-embedded tissue blots performed as described by using 12F10 monclonal antiprion antibody (6) (Figure 1, panel A). The mobility of the unglycosylated PrPSc band and the glycoform ratio of proteinase K–digested PrPSc were similar to those in BSE when assessed by Western blot analysis by using monoclonal POM-1 antiprion antibody as described (7) (Figure 1, panel B).


BSE-associated prion-amyloid cardiomyopathy in primates.

Krasemann S, Mearini G, Krämer E, Wagenführ K, Schulz-Schaeffer W, Neumann M, Bodemer W, Kaup FJ, Beekes M, Carrier L, Aguzzi A, Glatzel M - Emerging Infect. Dis. (2013)

PrPSc distribution and content in brain of bovine spongiform encephalopathy (BSE)–infected rhesus macaques. A) Paraffin-embedded tissue blot of striatum and cerebellum show a typical BSE-like deposition pattern of PrPSc with no differences between individual BSE-diseased monkeys at 49, 59, and 61 months postinoculation (mpi). Scale bars = 1 mm. B) Western blot analysis for PrPSc in brain of BSE-infected monkeys with incubation times of 49, 59, and 61 mpi. PrPSc-type is as expected for BSE prions, and no major differences in PrPSc load were detected. All samples were proteinase K–digested; loading amount was 0.5 and 0.1 mg fresh wet tissue for each sample
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC3713817&req=5

Figure 1: PrPSc distribution and content in brain of bovine spongiform encephalopathy (BSE)–infected rhesus macaques. A) Paraffin-embedded tissue blot of striatum and cerebellum show a typical BSE-like deposition pattern of PrPSc with no differences between individual BSE-diseased monkeys at 49, 59, and 61 months postinoculation (mpi). Scale bars = 1 mm. B) Western blot analysis for PrPSc in brain of BSE-infected monkeys with incubation times of 49, 59, and 61 mpi. PrPSc-type is as expected for BSE prions, and no major differences in PrPSc load were detected. All samples were proteinase K–digested; loading amount was 0.5 and 0.1 mg fresh wet tissue for each sample
Mentions: In 2002, three rhesus macaques were inoculated with BSE intraperitoneally (10 mL of a 10% homogenate of brain from BSE-diseased cattle). As controls, 2 rhesus macaques received saline (10 mL) and 1 was untreated. All procedures involving rhesus macaques were performed at the Institute of Neuropathology, University Medical Center Hamburg-Eppendorf (Hamburg, Germany), in accordance with the German Animal Welfare Act and the Council Directive 86/609/EEC (Permit 33.42502/08–08.02 LAVES, Lower Saxony, Germany). Animals were observed for clinical signs of prion disease and, when signs of terminal prion disease became evident, were euthanized and underwent autopsy. In all 3 BSE-challenged macaques and none of the controls a progressive neurologic disease developed 49, 59, and 61 months postinoculation. Examination of brain by using hematoxylin and eosin staining showed typical neuropathologic features of vCJD (data not shown) and abundant deposits of PrPSc in the cortex, basal ganglia, and cerebellum in paraffin-embedded tissue blots performed as described by using 12F10 monclonal antiprion antibody (6) (Figure 1, panel A). The mobility of the unglycosylated PrPSc band and the glycoform ratio of proteinase K–digested PrPSc were similar to those in BSE when assessed by Western blot analysis by using monoclonal POM-1 antiprion antibody as described (7) (Figure 1, panel B).

Bottom Line: Prion amyloidosis occurred in the heart of 1 of 3 macaques intraperitoneally inoculated with bovine spongiform encephalopathy prions.This macaque had a remarkably long duration of disease and signs of cardiac distress.Variant Creutzfeldt-Jakob disease, caused by transmission of bovine spongiform encephalopathy to humans, may manifest with cardiac symptoms from prion-amyloid cardiomyopathy.

View Article: PubMed Central - PubMed

Affiliation: University Medical Center Hamburg-Eppendorf, Hamburg, Germany.

ABSTRACT
Prion amyloidosis occurred in the heart of 1 of 3 macaques intraperitoneally inoculated with bovine spongiform encephalopathy prions. This macaque had a remarkably long duration of disease and signs of cardiac distress. Variant Creutzfeldt-Jakob disease, caused by transmission of bovine spongiform encephalopathy to humans, may manifest with cardiac symptoms from prion-amyloid cardiomyopathy.

Show MeSH
Related in: MedlinePlus