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

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.

2020 ◽  
Vol 21 (1) ◽  
pp. 34-43
Author(s):  
Warath Chantaksinopas ◽  
Papon Prettiwitayakul ◽  
Kaewkamol Srichai ◽  
Kanet Kanjanapradit

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.


2021 ◽  
Vol 91 (1) ◽  
Author(s):  
Xiaofang Gao ◽  
Peng Yan

Primary pulmonary lymphoma (PPL) is a rare neoplasm. We report a case of 45-year-old men who was admitted to hospital for multiple nodules and masses in both lungs. The contrast enhanced chest CT scans revealed multiple nodules and masses of varying sizes in right upper and middle lobes and both lower lobes. CT-guided percutaneous transthoracic needle biopsy was performed. The diagnosis of PPL was confirmed by histopathological examination and Immunohistochemical staining. PPL should be included in the differential diagnoses in symptomless patients with multiple pulmonary nodules and masses.


2018 ◽  
Vol 18 (3) ◽  
pp. 393
Author(s):  
Rashid S. Al-Umairi ◽  
Fatma Al-Lawati ◽  
Fadhila M. Al-Busaidi

Amyloidosis is a disorder characterised by the extracellular deposition of amyloid, a fibrillary protein, in various organs such as the lungs. Pulmonary nodular amyloidosis can mimic other lung conditions that present with pulmonary nodules, such as metastasis, sarcoidosis and hyalinising granuloma. We report a 60-year-old man who presented to the Royal Hospital, Muscat, Oman, in 2017 with a history of shortness of breath upon exertion, orthopnoea and bilateral lower limb swelling. A chest X-ray showed bilateral nodular opacities. Enhanced chest computed tomography revealed bilateral pulmonary nodules with a predominantly perilymphatic and subpleural distribution, giving the impression of a neoplastic nodule. A histopathological examination of biopsied lung tissue confirmed a diagnosis of nodular pulmonary amyloidosis.Keywords: Multiple Pulmonary Nodules; Amyloidosis; Computed Tomography; Case Report; Oman.


2007 ◽  
Vol 64 (3) ◽  
pp. 397-400 ◽  
Author(s):  
Aya Kino ◽  
Masaya Takahashi ◽  
Simon K. Ashiku ◽  
Malcolm M. Decamp ◽  
Robert E. Lenkinski ◽  
...  

2021 ◽  
Vol 49 (2) ◽  
pp. 977-985
Author(s):  
Marcus Fändrich ◽  
Matthias Schmidt

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.


Radiographics ◽  
1996 ◽  
Vol 16 (5) ◽  
pp. 1073-1084 ◽  
Author(s):  
D F Yankelevitz ◽  
S D Davis ◽  
D A Chiarella ◽  
C I Henschke

Amyloidosis ◽  
1986 ◽  
pp. 821-828 ◽  
Author(s):  
Yoshiko Okuzono ◽  
Toshikazu Gondoh ◽  
Hiroo Kawano ◽  
Takaaki Nagasawa ◽  
Fumiya Uchino

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