Localized laryngeal amyloidosis: Partial characterization of an amyloid fibril protein al

Westermark, Per; Sletten, Knut; Pitkänen, P; Natvig, J. B.; Lindholm, Carl‐Eric

doi:10.1016/0161-5890(82)90210-3

Cited by 36 publications

(19 citation statements)

References 18 publications

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“…Antisera to BJ-VAG [5][6][7][8][9][10][11][12][13][14], BJ-VAG [38][39][40][41][42][43][44][45][46][47] and BJ-VAG [191][192][193][194][195][196][197][198][199][200][201][202] were used for immunoblotting of SDS-PAGE of amyloid fibrils VAG and of fibrils from a kI-amyloid (case 366) used as a reference. SDS-PAGE of dissolved fibril material revealed a major protein corresponding to 14 kDa for VAG and about 12 kDa for 366 (Fig.…”

Section: Electrophoresis and Immunoblottingmentioning

confidence: 99%

“…A very faint labelling of a band corresponding to about 14 kDa can also be seen. Antiserum to BJ-VAG [5][6][7][8][9][10][11][12][13][14] labels the upper two bands of amyloid fibrils VAG strongly, while the bands at 14 kDa and lower are close to negative (Fig. 2, lane 6).…”

Section: Electrophoresis and Immunoblottingmentioning

confidence: 99%

“…Immunoglobulin light chains can also give rise to an uncommon form of localized, often tumour-like, amyloid form described for many different tissues including skin [6], breast [7], brain [8], respiratory tract [9,10] and urinary bladder [11]. In this form of AL-amyloidosis, the monoclonal protein is most likely produced at the site of deposition by a clone of plasma cells, present locally in the tissue [10].…”

Section: Introductionmentioning

confidence: 99%

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Constant Region of a κ III Immunoglobulin Light Chain as a Major AL‐Amyloid Protein

et al. 1998

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Engvig JP, Olsen KE, Gislefoss RE, Sletten K, Wahlström O, Westermark P. Constant Region of a k III Immunoglobulin Light Chain as a Major AL-Amyloid Protein. Scand J Immunol 1998;48:92-98 AL-amyloidoses are generally described as a group of disorders in which N-terminal fragments of monoclonal immunoglobulin light chains are transferred into amyloid fibrils. We have, by amino acid sequence analyses and immunological methods, characterized the Bence-Jones protein and the corresponding AL protein as a k III immunoglobulin light chain from material of a patient with systemic AL-amyloidosis presenting as a local inguinal tumour. The two proteins showed some unique features. The major part of the AL amyloid fibril protein consisted of C-terminal fragments of the Bence-Jones protein. Furthermore, both the Bence-Jones protein and the AL protein were glycosylated, with possibly a glycosylation in the constant part of the light chain.

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Section: Electrophoresis and Immunoblottingmentioning

confidence: 99%

Section: Electrophoresis and Immunoblottingmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Constant Region of a κ III Immunoglobulin Light Chain as a Major AL‐Amyloid Protein

et al. 1998

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“…[35][36][37][38][39][40][41] Of note, localized AL amyloidosis is not unique to the lungs and the tracheobronchial tree (see below). It can also occur at other sites including the larynx, 42 urinary bladder, 43 and colon. 44 In the past, nodular pulmonary amyloidosis and primary pulmonary lymphoma with amyloid production were thought to be 2 fundamentally different processes.…”

Section: Pathologymentioning

confidence: 99%

Amyloidosis of the Lung

Khoór¹,

Colby²

2017

Archives of Pathology &Amp; Laboratory Medicine

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Context.—Amyloidosis is a heterogeneous group of diseases characterized by the deposition of congophilic amyloid fibrils in the extracellular matrix of tissues and organs. To date, 31 fibril proteins have been identified in humans, and it is now recommended that amyloidoses be named after these fibril proteins. Based on this classification scheme, the most common forms of amyloidosis include systemic AL (formerly primary), systemic AA (formerly secondary), systemic wild-type ATTR (formerly age-related or senile systemic), and systemic hereditary ATTR amyloidosis (formerly familial amyloid polyneuropathy). Three different clinicopathologic forms of amyloidosis can be seen in the lungs: diffuse alveolar-septal amyloidosis, nodular pulmonary amyloidosis, and tracheobronchial amyloidosis. Objective.—To clarify the relationship between the fibril protein–based amyloidosis classification system and the clinicopathologic forms of pulmonary amyloidosis and to provide a useful guide for diagnosing these entities for the practicing pathologist. Data Sources.—This is a narrative review based on PubMed searches and the authors' own experiences. Conclusions.—Diffuse alveolar-septal amyloidosis is usually caused by systemic AL amyloidosis, whereas nodular pulmonary amyloidosis and tracheobronchial amyloidosis usually represent localized AL amyloidosis. However, these generalized scenarios cannot always be applied to individual cases. Because the treatment options for amyloidosis are dependent on the fibril protein–based classifications and whether the process is systemic or localized, the workup of new clinically relevant cases should include amyloid subtyping (preferably with mass spectrometry–based proteomic analysis) and further clinical investigation.

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“…In most cases immunohistochemical techniques have been applied and suggestions of immunoglobulin light chain origin of the amyloid material have been deduced from the positive-staining reaction of the amyloid substance and/or the surrounding plasma cells. In 12 cases of PLA, amino acid sequence analysis of extracted amyloid fibrils has been performed giving evidence of immunoglobulin origin, light chain type in 11 cases and heavy chain type in 1 case (Table 1) [1][2][3][4][5][6][7][8][9][10][11][12]. There has been no suggestion of any other protein constituents.…”

Section: Introductionmentioning

confidence: 99%

Primary localized amyloidosis of the eyelid: two cases of immunoglobulin light chain-derived proteins, subtype λV respectively λVI

Olsen

Sandgren

Sletten

et al. 1996

Clinical and Experimental Immunology

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Primary localized amyloidosis has been described in many different organs in the body. Studies by immunohistochemical techniques have suggested an immunoglobulin light chain origin of the amyloid material. Only in a limited number of cases has the amyloid protein been characterized by amino acid sequence analysis as subtypes of immunoglobulin light chain or heavy chain. In this report, two cases of primary localized amyloidosis of the eyelid are presented. The amyloid substance has been extracted and a major fibril protein subjected to amino acid sequence analysis. Both amyloid proteins were part of the variable region of immunoglobulin light chains, subtype λV and subtype λVI, respectively. While λVI has been shown to be a common subtype in systemic immunoglobulin light chain‐amyloidosis, it has never been demonstrated in localized amyloid. Very few λV immunoglobulin light chains have been characterized and the subgroup has never been found in amyloid before.

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Localized laryngeal amyloidosis: Partial characterization of an amyloid fibril protein al

Cited by 36 publications

References 18 publications

Constant Region of a κ III Immunoglobulin Light Chain as a Major AL‐Amyloid Protein

Constant Region of a κ III Immunoglobulin Light Chain as a Major AL‐Amyloid Protein

Amyloidosis of the Lung

Primary localized amyloidosis of the eyelid: two cases of immunoglobulin light chain-derived proteins, subtype λV respectively λVI

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