AL amyloidosis with a localized B cell neoplasia

Stuhlmann-Laeisz, Christiane; Schönland, Stefan; Hegenbart, Ute; Oschlies, Ilske; Baumgart, Julius-Valentin; Krüger, Sandra; Röcken, Christoph

doi:10.1007/s00428-019-02527-7

Cited by 17 publications

(25 citation statements)

References 42 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…29 to detect the clone in most cases, while more sophisticated approaches for clonality assessment, for example, in situ hybridization and molecular pathological analyses, are more effective. 5,11,13 Since these latter techniques were not systematically used in our study, it is possible that we identified only cases with more extended B-cell clones, while cases with more subtle infiltrations could have been missed for example, due to sampling errors (note the correlation with sample size) or technical issue…”

Section: Discussionmentioning

confidence: 99%

“…However, a larger study revealed that the infiltrate is currently best classified as "localized B-cell neoplasia of undermined significance" in the majority of cases. 13 Thus, like in sysAL, the amyloidogenic clone is usually small and has not the full characteristics of a well-defined malignant disease. 4 The B-cell clones in locAL might have other not yet known biologic characteristics that affect the outcome, as already observed in sysAL.…”

Section: Discussionmentioning

confidence: 99%

“…Moreover, few data are available on local cellular infiltrate and B-cell clone at amyloid deposition site and its role in natural history of locAL has not been studied so far. 13 We present the results of a comprehensive study conducted on a large series of 293 consecutive patients with verified locAL evaluated at the Heidelberg Amyloidosis Center. We coupled an extensive characterization of clinical features with detailed pathology data from tissue biopsy.…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Localized immunoglobulin light chain amyloidosis: Novel insights including prognostic factors for local progression

et al. 2020

Self Cite

View full text Add to dashboard Cite

In localized light chain amyloidosis (locAL), amyloidogenic light chains (aLC) are produced and deposited locally by a B‐cell clone. We present 293 patients with immunohistochemically confirmed locAL. Lung (nodular pulmonary) with 63 patients was the most involved organ. The aLC was λ in 217 cases (κ:λ ratio 1:3). A local B‐cell clone was identified in 30% of cases. Sixty‐one (21%) had a concomitant autoimmune disorder (cAD). A monoclonal component (MC) were present in 101 (34%) patients and were more frequent in subjects with cAD (51% vs 34%; P = .03). Cigarette smoking was more prevalent in lung locAL (54% vs 37%; P = .018). After a median follow‐up of 44 months, 16 patients died and 5‐ and 10‐years locAL progression‐free survival (PFS) were 62% and 44%. Interestingly, locAL‐PFS was shorter among patients with an identified clonal infiltrate at amyloid deposition site (40 vs 109 months; P = .02) and multinuclear giant cells and/or an inflammatory infiltrate resulted in longer locAL‐PFS in lung involvement (65 vs 42 months; P = .01). However, no differences in locAL PFS were observed in patients with cAD, a MC and involved organ site. Treatment was administered in 163 (54%) patients and was surgical in 135 (46%). Median locAL‐PFS after first treatment was 56 months. Responders had longer locAL‐PFS (78 vs 17 months; P < .001). Three patients with lung locAL and a MC were diagnosed as systemic AL amyloidosis at follow‐up. In summary, locAL pathogenesis seems to be heterogeneous and the clonal infiltrate leads local progression.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Localized immunoglobulin light chain amyloidosis: Novel insights including prognostic factors for local progression

et al. 2020

Self Cite

View full text Add to dashboard Cite

show abstract

“…In the preceding decades, we and others have collected ample evidence of the tissue-specific patterns from different types of amyloid deposits (Mahmood et al 2015;Freudenthaler et al 2016;Baumgart et al 2018;Stuhlmann-Laeisz et al 2019). Hence, we consider amyloidosis as a disease of cells and tissues, and amyloid itself as a "gemisch" (mixture) of constituents that show organ-, tissue-, and amyloid-type specific patterns.…”

Section: Introductionmentioning

confidence: 99%

The amyloid proteome: a systematic review and proposal of a protein classification system

Gottwald

Röcken

2021

Critical Reviews in Biochemistry and Molecular Biology

Self Cite

View full text Add to dashboard Cite

Amyloidosis is a disease caused by pathological fibril aggregation and deposition of proteins in different tissues and organs. Thirty-six fibril-forming proteins have been identified. So far, proteomic evaluation of amyloid focused on the detection and characterization of fibril proteins mainly for diagnostic purposes or to find novel fibril-forming proteins. However, amyloid deposits are a complex mixture of constituents that show organ-, tissue-, and amyloid-type specific patterns, that is the amyloid proteome. We carried out a comprehensive literature review on publications investigating amyloid via liquid chromatography coupled to tandem mass spectrometry, including but not limited to sample preparation by laser microdissection. Our review confirms the complexity and dynamics of the amyloid proteome, which can be divided into four functional categories: amyloid proteome-category 1 (APC1) includes exclusively fibrillary proteins found in the patient; APC2 includes potential fibril-forming proteins found in other types of amyloid; and APC3 and APC4 summarizes non-fibril proteins-some being amyloid signature proteins. Our categorization may help to systemically explore the nature and role of the amyloid proteome in the manifestation, progression, and clearance of disease. Further exploration of the amyloid proteome may form the basis for the development of novel diagnostic tools, thereby enabling the development of novel therapeutic targets.

show abstract

“…Only a few, small case series reported an association between marginal zone lymphoma (MZL) of mucosaassociated lymphoid tissue and localized AL amyloidosis, mainly with nodular pulmonary involvement. [17][18][19] Recently, German investigators published a series of 29 patients with AL amyloidosis and localized B-cell neoplasia, mostly with an MZL immunophenotype 20 ; only 5 patients had systemic lymphoma, and 2 were classified as systemic AL amyloidosis.…”

mentioning

confidence: 99%