scholarly journals Gastric perforation caused by secondary systemic amyloidosis

2021 ◽  
Author(s):  
Hiroto Yamamoto ◽  
Akihiko Yokota ◽  
Noriyuki Suzuki ◽  
Mitsuhiro Tachibana ◽  
Yutaka Tsutsumi
Keyword(s):  
Gastric Perforation ◽  
Systemic Amyloidosis ◽  
Watery Diarrhea ◽  
Femoral Prosthesis ◽  
Amyloid A ◽  
Prosthesis Replacement ◽  
Purulent Peritonitis

An 82-year-old man, suffering abscess secondary to femoral prosthesis replacement, complained of intractable watery diarrhea and melena. Autopsy disclosed 12 mm-sized perforation at the gastric prepylorus and purulent peritonitis. Amyloid A was deposited in systemic organs and tissues, including the site of gastric perforation. IgM was co-deposited in the glomeruli.

Methods to study the structure of misfolded protein states in systemic amyloidosis

2021 ◽  
Vol 49 (2) ◽  
pp. 977-985
Author(s):  
Marcus Fändrich ◽  
Matthias Schmidt
Keyword(s):  
Protein Misfolding ◽  
Amyloid Fibrils ◽  
Ex Vivo ◽  
Systemic Amyloidosis ◽  
Structural Basis ◽  
Amyloid A ◽  
Serum Amyloid A Protein ◽  
Proteolytic Stability

Systemic amyloidosis is defined as a protein misfolding disease in which the amyloid is not necessarily deposited within the same organ that produces the fibril precursor protein. There are different types of systemic amyloidosis, depending on the protein constructing the fibrils. This review will focus on recent advances made in the understanding of the structural basis of three major forms of systemic amyloidosis: systemic AA, AL and ATTR amyloidosis. The three diseases arise from the misfolding of serum amyloid A protein, immunoglobulin light chains or transthyretin. The presented advances in understanding were enabled by recent progress in the methodology available to study amyloid structures and protein misfolding, in particular concerning cryo-electron microscopy (cryo-EM) and nuclear magnetic resonance (NMR) spectroscopy. An important observation made with these techniques is that the structures of previously described in vitro formed amyloid fibrils did not correlate with the structures of amyloid fibrils extracted from diseased tissue, and that in vitro fibrils were typically more protease sensitive. It is thus possible that ex vivo fibrils were selected in vivo by their proteolytic stability.

Histopathology of Cutaneous Amyloid: A Comparative Study on 144 Cases of Localized Cutaneous Amyloidosis and 20 Cases of Systemic Amyloidosis

Amyloidosis ◽  
1986 ◽  
pp. 821-828 ◽  
Author(s):  
Yoshiko Okuzono ◽  
Toshikazu Gondoh ◽  
Hiroo Kawano ◽  
Takaaki Nagasawa ◽  
Fumiya Uchino
Keyword(s):  
Comparative Study ◽  
Systemic Amyloidosis ◽  
Amyloid A

Systemic Amyloid A Amyloidosis in Stejneger’s Beaked Whales (Mesoplodon stejnegeri)

2020 ◽  
Vol 57 (3) ◽  
pp. 437-444
Author(s):  
Shotaro Nakagun ◽  
Kenichi Watanabe ◽  
Yuko Tajima ◽  
Tadasu K. Yamada ◽  
Yoshiyasu Kobayashi
Keyword(s):  
Body Condition ◽  
Gel Electrophoresis ◽  
Systemic Amyloidosis ◽  
Population Status ◽  
Amyloid A ◽  
High Prevalence ◽  
High Incidence ◽  
Beaked Whales ◽  
Hematoxylin And Eosin ◽  
Population Numbers

Stejneger’s beaked whales ( Mesoplodon stejnegeri) are one of the lesser known species of mammals, with little information available on their population status or incidence of diseases. Recent pathologic investigations on stranded and bycaught wild cetaceans around Hokkaido, Japan, revealed an unusually high incidence of systemic amyloidosis in this species, warranting further investigation. The objective of this study was to further characterize the systemic amyloidosis of Stejneger’s beaked whales by retrospective histopathologic analyses of tissues from animals that stranded in Japan between 1994 and 2018. Various tissues from 35 individuals were examined histologically with hematoxylin and eosin, Congo red, and immunohistochemistry for amyloid A (AA), in which 12 (34%) were diagnosed with systemic amyloidosis. The organs with the highest severity of amyloid deposition were the stomach and intestine. The type of amyloid was confirmed as AA of approximately 9 kDa by 2-dimensional gel electrophoresis with extracted amyloid from the liver and subsequent Western blotting with an antiserum against AA peptide. There were no statistically significant associations between amyloidosis and sex, body condition of the whales, or the presence of chronic inflammation. The high prevalence of this disease might be of concern for overall population numbers, and continued pathologic monitoring of stranded animals is necessary throughout its distributional range.

scholarly journals Multiple pulmonary nodules mimicking metastasis in a case of systemic amyloidosis

2020 ◽  
pp. 34-43
Author(s):  
Warath Chantaksinopas ◽  
Papon Prettiwitayakul ◽  
Kaewkamol Srichai ◽  
Kanet Kanjanapradit
Keyword(s):  
Pulmonary Nodules ◽  
Systemic Amyloidosis ◽  
Transthoracic Needle Biopsy ◽  
Amyloid A ◽  
Thoracic Computed Tomography ◽  
Contrast Enhanced ◽  
Abnormal Accumulation ◽  
Systemic Process ◽  
Pulmonary Amyloidosis ◽  
Pulmonary Masses

Amyloidosis is a disorder resulting from the abnormal accumulation of amyloid, a fibrillary protein, in various tissues and organs. Pulmonary amyloidosis can be a part of a systemic process and can mimic other lung diseases which present with multiple pulmonary masses or nodules, such as metastasis. We reported a case of systemic amyloidosis, which is histopathologically confirmed from the nasal lesion, initially presented with multiple lung nodules mimicking pulmonary metastasis but had been stable for years. Pathological study of tissues obtained from three times of percutaneous transthoracic needle biopsy (PTNB) failed to show specific features. The findings on chest radiographs, contrast enhanced thoracic computed tomography (CT) and histology were reviewed and discussed.

scholarly journals Systemic Amyloidosis as a Rare Complication of IgG4 Related Disease: Case Report and Literature Review

2021 ◽  
Author(s):  
Leonardo Oliveira Mendonca ◽  
Henrikki Gomes Antila ◽  
Alex Isidoro Prado ◽  
Luiz Augusto Marcondes Fonseca ◽  
Miton de Arruda Martins ◽  
...  
Keyword(s):  
Rare Complication ◽  
Systemic Amyloidosis ◽  
Aa Amyloidosis ◽  
Amyloid A ◽  
Related Disease ◽  
Igg4 Related Disease ◽  
Inflammatory Conditions ◽  
Immune Mediated ◽  
Brazilian Patient ◽  
Disease Case

Abstract Immunoglobulin 4 Related Disease (IgG4-RD) is immune-mediated fibroinflammatory disease and despite recent advances the immunological process involved in the disease pathogenesis is still unclear. Serum amyloid A (SAA) the precursor protein in AA amyloidosis is induced by inflammatory mediators such as IL-1, IL-6 and TNF cytokines. The treatment of AA amyloidosis is directed by the theoretical cytokine involved in the underlying inflammatory condition. Many inflammatory conditions has already been associated to AA amyloidosis and secondary to IgG4-RD seems to be rare. Here we report the case of a Brazilian patient with IgG4-RD with a fatal evolution of systemic amyloidosis. We also revised the cases already reporte in the literature with IgG4-RD and systemic amyloidosis.

Systemic amyloidosis derived from EFEMP1 in a captive Tsushima leopard cat

2021 ◽  
pp. 030098582110486
Author(s):  
Shinya Miyazaki ◽  
Yuki Kobayashi ◽  
Fuyuki Kametani ◽  
Kyoko Kobayashi ◽  
Susumu Iwaide ◽  
...  
Keyword(s):  
Matrix Protein ◽  
Systemic Amyloidosis ◽  
Extracellular Matrix Protein ◽  
Amyloid A ◽  
Multiple Organs ◽  
Age Related ◽  
Amyloid Deposits ◽  
Amyloidogenic Region ◽  
Leopard Cat ◽  
Different Characteristics

In animals, most cases of systemic amyloidosis are of amyloid A type, and the other types of systemic amyloidoses are rare. This study analyzed systemic amyloidosis in a 15-year-old female Tsushima leopard cat. Amyloid deposits strongly positive for Congo red staining were observed in the arterial walls as well as the interstitium in multiple organs. Mass spectrometry–based proteomic analysis with laser microdissection of amyloid deposits identified epidermal growth factor–containing fibulin-like extracellular matrix protein 1 (EFEMP1) as a prime amyloidogenic protein candidate. Immunohistochemistry showed that the amyloid deposits were positive for the N-terminal region of EFEMP1. From these results, the present case was diagnosed as EFEMP1-derived amyloidosis. It is the first such case in an animal. EFEMP1-derived amyloidosis in humans has recently been reported as a systemic amyloidosis, and it is known as an age-related venous amyloidosis. The present case showed different characteristics from human EFEMP1-derived amyloidosis, including the amyloid deposition sites and the amyloidogenic region of the EFEMP1 protein, suggesting a different pathogenesis between Tsushima leopard cat and human EFEMP1-derived amyloidosis.

scholarly journals Colocalization of Apolipoprotein AI in Various Kinds of Systemic Amyloidosis

2005 ◽  
Vol 53 (2) ◽  
pp. 237-242 ◽  
Author(s):  
Naohiro Sakata ◽  
Yoshinobu Hoshii ◽  
Tomomi Nakamura ◽  
Makiko Kiyama ◽  
Hirofumi Arai ◽  
...  
Keyword(s):  
Transgenic Mice ◽  
Amyloid Fibrils ◽  
Senile Plaques ◽  
Systemic Amyloidosis ◽  
High Density Lipoproteins ◽  
Apolipoprotein Ai ◽  
Aa Amyloidosis ◽  
Amyloid A ◽  
Amyloid Deposits ◽  
A Minor

Apolipoprotein AI (apoAI), a major component of high-density lipoproteins, is one of the major amyloid fibril proteins and a minor constituent of the senile plaques observed in Alzheimer's disease. We examined colocalization of apoAI in various kinds of systemic amyloidosis in this study. Forty-three of 48 formalin-fixed paraffin-embedded heart specimens with various forms of systemic amyloidosis reacted immunohistochemically with anti-human apoAI antibody. ApoAI was also detected in water-extracted amyloid material by immunoblotting. In addition, we observed colocalization of apoAI and murine amyloid A (AA) amyloidosis in human apoAI transgenic mice. This is the first report of colocalization of apoAI with amyloid deposits in various forms of human systemic amyloidosis and murine AA amyloidosis in human apoAI transgenic mice. ApoAI may not always be a major component of amyloid fibrils, even when it is present in systemic amyloid deposits.

scholarly journals Lacrimal Gland Amyloidosis in an Elderly Patient

2020 ◽  
Vol 11 (1) ◽  
pp. 100-105
Author(s):  
Toshiya Nagai ◽  
Tatsuya Yunoki ◽  
Atsushi Hayashi
Keyword(s):  
Elderly Patient ◽  
Rare Disease ◽  
Lacrimal Gland ◽  
Light Chain ◽  
Systemic Amyloidosis ◽  
Amyloid A ◽  
Senile Systemic Amyloidosis ◽  
Localized Amyloidosis ◽  
Secretory Gland

Localized amyloidosis of the lacrimal gland is a rare disease. We report a case of transthyretin-positive localized amyloidosis of the lacrimal gland in a 74-year-old man with left lacrimal gland swelling. Biopsy of the left lacrimal gland showed extensive deposition of nonstructural eosinophilic material in the secretory gland and ducts, which stained positive with direct fast scarlet. Immunostaining was negative for amyloid A and positive for both globulin light chain (kappa, lambda) and transthyretin. It is necessary to consider the possibility of senile systemic amyloidosis, even if localized amyloidosis of the lacrimal gland is suspected.

α1-Antitrypsin and Reactive Systemic Amyloidosis

1983 ◽  
Vol 64 (4) ◽  
pp. 453-454 ◽  
Author(s):  
C. P. J. Maury ◽  
A.M. Teppo ◽  
B. Fröseth ◽  
O. Wegelius
Keyword(s):  
Rheumatoid Arthritis ◽  
Biological Activity ◽  
Protease Inhibitor ◽  
Inhibitory Activity ◽  
Systemic Amyloidosis ◽  
Amyloid A ◽  
Control Subjects ◽  
Patient Groups ◽  
The Difference

1. Serum contains amyloid A-degrading activity. This activity is markedly reduced in patients with rheumatoid arthritis (RA) complicated by amyloidosis. α1-Antitrypsin inhibits the degradative activity. To test the hypothesis that the activity of this enzyme is regulated by α1-antitrypsin, we determined the concentrations, elastase-inhibitory activity and phenotypes of α1-antitrypsin in 24 RA patients with and in 26 RA patients without amyloidosis. 2. α1-Antitrypsin concentrations and biological activity were significantly increased in both patient groups compared with control subjects, but there was no difference between the two patient groups. 3. All patients who had developed amyloidosis were of the normal protease inhibitor (Pi) MM-phenotype. 4. We conclude that the difference in the amyloid A-degrading activity between RA patients with or without amyloidosis cannot be accounted for by differences in concentration, activity or Pi type of α1-antitrypsin.

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