Plasmacytoma of the tonsil with AL amyloidosis: evidence of post-fibrillogenic proteolysis of the fibril protein

Röcken, Christoph; Hegenbarth, V.; Schmitz, Marc; Stix, Barbara; Schade, G.; Mohnert, A.; Roessner, Albert

doi:10.1007/s004280050456

Cited by 22 publications

(13 citation statements)

References 40 publications

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“…An increased number of mast cells has also been described [17,111]. Heterotopic ossifications and calcifications may be present occasionally [98].…”

Section: Histologymentioning

confidence: 94%

“…Systemic AL amyloidosis is a serious disease: patients with cardiac involvement survive 4-6 months, patients without cardiac involvement at the time of diagnosis have a median survival of 30 months [35]. If neither immunohistochemistry nor clinical history is informative, then preparation of the fibril protein and biochemical identification should be applied [54,72,98].…”

Section: Al Amyloidosismentioning

confidence: 99%

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Amyloid in surgical pathology

Röcken

Sletten

2003

Virchows Archiv

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Amyloid is defined as a proteinaceous tissue deposit that shows a typical green birefringence in polarized light after staining with Congo red, the presence of non-branching linear fibrils of indefinite length with a mean diameter of 10 nm, and a distinct X-ray diffraction pattern consistent with Pauling's model of a cross beta-fibril. Amyloid may deposit locally or may present as a systemic disease. The origin of amyloid is diverse: 25 different fibril proteins have been described so far. The precursor proteins differ from each other in their primary structures and functions. The only common denominator is the propensity to form anti-parallel cross beta-fibrils under certain circumstances. Early diagnosis of amyloid is still a major challenge in surgical pathology. Histological proof can be obtained using Congo-red staining and polarization microscopy. However, small deposits may be difficult to discern, and sensitivity can be improved using fluorescence microscopy. Classification of amyloid is mandatory, since amyloid is treatable and different treatment regimens are applied to different amyloid diseases. This review focuses on the epidemiology, clinical features, pathology and diagnosis of amyloid in surgical pathology.

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“…An increased number of mast cells has also been described [17,111]. Heterotopic ossifications and calcifications may be present occasionally [98].…”

Section: Histologymentioning

confidence: 94%

Section: Al Amyloidosismentioning

confidence: 99%

Amyloid in surgical pathology

Röcken

Sletten

2003

Virchows Archiv

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“…The extracted protein was resolved by SDS polyacrylamide gel electrophoresis, as described elsewhere (Röcken et al, 2000). Proteins were visualized by Coomassie blue staining or blotted onto PVDF or NC membranes.…”

Section: Immunohistochemistrymentioning

confidence: 99%

ALys amyloidosis caused by compound heterozygosity in Exon 2 (Thr70Asn) and Exon 4 (Trp112Arg) of the lysozyme gene

et al. 2005

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Hereditary amyloidoses are caused by germline mutations, which increase the propensity of a protein to form cross-beta aggregates and deposit as amyloid. Hereditary amyloidoses are particularly interesting as they help to understand how changes in the primary structure of an otherwise non-amyloidogenic protein contribute to amyloidogenesis. Here we report on a novel form of systemic ALys amyloidosis, caused by compound heterozygosity in exon 2 (p.T70N) and exon 4 (p.W112R) of the lysozyme gene (LYZ), with both mutations being present on the same allele. This type of hereditary ALys amyloidosis is characterized by extended amyloid deposits in the upper gastrointestinal tract, entire colon, and kidney, leading to gastrointestinal bleeding. Both mutations are probably effective in disease manifestation. The novel mutation at position 112 in the mature protein is located within the alpha-helical domain of the protein and therefore outside the cluster of residues that has so far been implicated in ALys amyloidosis. Taken together with the p.T70N mutation, this results in a lysozyme species where the correct folding of various protein domains is probably impaired and increases the propensity of amyloid fibril formation. Interestingly, this form of ALys amyloidosis is also characterized by the occurrence of proteolytic fragments of lysozyme in the amyloid deposits.

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“…Involvement of the tonsil is unusual [7,8] with only a few cases having been reported. Incidence is more in men (75%) [9].…”

Section: Introductionmentioning

confidence: 99%

Tonsillar Non-secreting Plasmacytoma in a Woman

Kouroupi¹,

Sivridis²,

Arelaki³

et al. 2018

JCR

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Background: Plasmacytomas are characterized by excessive proliferation of neoplastic plasma cells in the bone marrow. Extra-medullary plasmacytoma are by and large, encountered in the head and neck region and only rarely occur in the tonsils. Case Report: We report here a asymptomatic solitary non-secreting plasmacytoma of the right tonsil in a middle-aged woman. The diagnosis of a plasmacytoma was reached after surgical excision. Conclusion: Tonsil is a rare sight of plasmacytoma origin with no specific symptoms, thus recommendation of WHO 2015 for such tumors must be taken under consideration.

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Plasmacytoma of the tonsil with AL amyloidosis: evidence of post-fibrillogenic proteolysis of the fibril protein

Cited by 22 publications

References 40 publications

Amyloid in surgical pathology

Amyloid in surgical pathology

ALys amyloidosis caused by compound heterozygosity in Exon 2 (Thr70Asn) and Exon 4 (Trp112Arg) of the lysozyme gene

Tonsillar Non-secreting Plasmacytoma in a Woman

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