Localized Amyloidosis of the Uterine Cervix with Spheroid Type of Amyloid

Jf, Val-Bernal

doi:10.1097/00004347-199904000-00018

Cited by 6 publications

(6 citation statements)

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“…Herein, we presented the first case of lactoferrin amyloidosis of the bronchus exhibiting characteristic spheroid structure. Spheroid‐type (corpora amylacea‐like) amyloid deposition is rare and to date, only a few cases have been reported . Lactoferrin was initially discovered as “red protein” in milk, and is contained in the secretions of many kinds of exocrine glands, including bronchial glands .…”

Section: Discussionmentioning

confidence: 99%

A case of spheroid‐type localized lactoferrin amyloidosis in the bronchus

Ichimata

Aoyagi

Yoshinaga

et al. 2019

Pathology International

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We report a case of localized bronchial lactoferrin amyloidosis. A 47‐year‐old man presented with a complaint of persistent dry cough for two months. Chest computed‐tomography revealed a calcification shadow of the right main bronchus; hence, a biopsy was performed, showing layered spheroid‐type eosinophilic deposits in the bronchial wall. These deposits were positive for Congo red staining, exhibiting apple‐green birefringence under polarized light. In addition, an electron microscopic examination demonstrated that this layered structure was formed by very thin cord‐like amyloid deposits. By proteomics analysis using liquid chromatography–tandem mass spectrometry and immunohistochemistry, we confirmed that the deposited amyloid was composed of lactoferrin. While lactoferrin is known to be a precursor protein of localized corneal and seminal vesicle amyloidosis, localized lactoferrin amyloidosis of the bronchus has not been reported in the English literature. Our pathological findings suggested that localized lactoferrin amyloidosis may be caused by long‐term tissue damage, and the characteristic spheroid‐type appearance is thought to be associated with unique, thin cord‐like amyloid deposits.

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Section: Discussionmentioning

confidence: 99%

A case of spheroid‐type localized lactoferrin amyloidosis in the bronchus

Ichimata

Aoyagi

Yoshinaga

et al. 2019

Pathology International

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“…Cases of intracellular amyloid deposition have been reported in few organs including cardiomyocytes, plasma cells, as well as the histiocytes and β cells of the pancreas [12][13][14]. Spheroid type (corpora amylacea-like) amyloid deposition is reported in pituitary adenoma, squamous cell carcinoma of the uterine cervix, and amyloidoma of the bone, jejunum, and colon [15][16][17][18]. One case of spheroid type amyloid deposition from our group in association with colon adenocarcinoma is identified [2] (Figures 6 and 7).…”

Section: Atypical Amyloid Findingsmentioning

confidence: 99%

Pathologic Findings of Amyloidosis: Recent Advances

Kim¹,

Baek²,

Truong³

et al. 2019

Amyloid Diseases

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Amyloids are aggregations of misfolded protein, which creates fibrillary structures. Unlike normally folded proteins, misfolded fibrils are insoluble and deposited extracellularly or intracellularly. The pathologic mechanism is still unclear, but resultant toxic oligomers within the tissue are known to damage the tissue via aberrant protein interactions. This condition has been known as amyloidosis. Different kinds of amyloid protein may cause similar or different clinical signs and symptoms, largely depending on the target organ it is deposited. However, because treatments and prognoses of each type are different drastically, it is critical to distinguish them and determine the specific type of amyloidosis. The confirmation and typing of amyloid heavily depend on pathologic examination of tissue. The gold standard method for the former is a Congo red staining and birefringence under polarized microscopy. The conventional way for the latter is immunohistochemistry (IHC), where most of the amyloid types can be classified. However, electron microscopy, mass spectrometry, or other molecular methods are required for typing some amyloids that are difficult to identify through IHC. In this chapter, we will describe basic concepts of amyloidosis and pathologic findings of amyloid deposition, including atypical structural deposition. Furthermore, we will review methodologies for amyloid typing briefly.

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“…Amyloid also shows affinity for thioflavin T, and is immunohistochemically stained for amyloid P component. Recently, this definition has been questioned as a number of atypical structure depositions and presence of amyloid in intracellular areas have been reported in various systems, including our case. GI amyloidosis can be acquired or genetic, and usually results from chronic inflammatory disorders (AA amyloidosis), hematologic malignancy (AL amyloidosis), and end‐stage renal disease (beta‐2 amyloidosis) …”

Section: Discussionmentioning

confidence: 91%

“…Spheroid‐type (corpora amylacea‐like or Liesegang ring formation) amyloid has been reported in pituitary adenoma, especially prolactinoma, squamous cell carcinoma of the uterine cervix, and amyloidomas of bone and jejunum . In prolactin‐producing adenoma and squamous cell carcinoma, the deposits are formed by cytokeratin fibrils .…”

Section: Discussionmentioning

confidence: 99%

“…GI amyloidosis can be acquired or genetic, and usually results from chronic inflammatory disorders (AA amyloidosis), hematologic malignancy (AL amyloidosis), and end-stage renal disease (beta-2 amyloidosis). 9 Spheroid-type (corpora amylacea-like or Liesegang ring formation) amyloid has been reported in pituitary adenoma, especially prolactinoma, 6 squamous cell carcinoma of the uterine cervix, 7 and amyloidomas of bone and jejunum. 10 In prolactin-producing adenoma and squamous cell carcinoma, the deposits are formed by cytokeratin fibrils.…”

Section: Discussionmentioning

confidence: 99%

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Spheroid‐type of AL amyloid deposition associated with colonic adenocarcinoma: A case report with literature review

Kim

McCroskey

Piao

et al. 2017

Pathology International

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We report a colonic adenocarcinoma associated with diffuse submucosal deposition of a peculiar spheroid-type amyloid identified in the colon, terminal ileum, and appendix. A 65-year-old woman with past medical histories of hypertension, and chronic obstructive pulmonary disease, presented to the emergency room with cramping abdominal pain and nausea. A computed tomography (CT) scan of abdomen showed right colonic volvulus. Emergency right hemicolectomy was performed. The specimen showed colonic adenocarcinoma with focal submucosal invasion (pT1) arising from a villotubular adenoma. A diffuse submucosal spheroid-type amyloid deposition (resembling corpora amylacea-like structures with Liesegang ring formation) was identified in the colon, ileum, and appendix. Electron microscopy examination of this unusual spheroidal-type material further confirmed the presence of amyloid fibrils. Analysis by liquid chromatography-mass spectrometry detected AL (lambda) type amyloidosis in this specimen. Tests for monoclonal gammopathy were not performed because patient consent was not obtained. In tissue section evaluation, however, no plasma cell neoplasm was identified. Cases with isolated AL amyloid deposition in the gastrointestinal tract have been reported rarely, and there is no case report of colonic adenocarcinoma associated with primary amyloid deposition in the English literature.

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Localized Amyloidosis of the Uterine Cervix with Spheroid Type of Amyloid

Cited by 6 publications

References 0 publications

A case of spheroid‐type localized lactoferrin amyloidosis in the bronchus

A case of spheroid‐type localized lactoferrin amyloidosis in the bronchus

Pathologic Findings of Amyloidosis: Recent Advances

Spheroid‐type of AL amyloid deposition associated with colonic adenocarcinoma: A case report with literature review

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