Coexistence of beta2 microglobulin and lambda light chain in amyloid fibrils of dialysis-unrelated plasma cell dyscrasia-associated systemic amyloidosis

Fujimoto, Norihiro; Wada, Naoko; Akiyama, Minoru; Tajima, S.; Ishibashi, Akira; Miyakawa, Shunpei

doi:10.1046/j.1365-2133.2002.04940.x

Cited by 6 publications

(2 citation statements)

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“…Haptoglobin as a Potential Molecular Chaperone for ␤2m; Role in Preventing Amyloid Fibril Formation, Acquired Cytotoxicity, and Resistance to Intracellular Degradation-Amyloid deposits of ␤2m occur in pathological conditions, such as dialysis-related amyloidosis, primary localized cutaneous nodular amyloidosis, and plasma cell-associated systemic amyloidosis (49,50). ␤2m is the major constituent protein of the amyloid fibrils in dialysis-related amyloidosis, whose major clinical FIGURE 11.…”

Section: Discussionmentioning

confidence: 99%

The Extracellular Chaperone Haptoglobin Prevents Serum Fatty Acid-promoted Amyloid Fibril Formation of β2-Microglobulin, Resistance to Lysosomal Degradation, and Cytotoxicity

Sultan¹,

Raman

Rao

et al. 2013

Journal of Biological Chemistry

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Background:The role of chaperones in extracellular space is important. Haptoglobin, an extracellular chaperone, is investigated in the context of ␤ 2 -microglobulin amyloidosis. Results: Haptoglobin interacts with prefibrillar species, facilitates intracellular degradation, and prevents formation of cytotoxic ␤2m fibrils. It exhibits pH-dependent chaperone activity. Conclusions: Haptoglobin is an extracellular chaperone for ␤ 2 -microglobulin under normal and inflammation-induced acidosis conditions. Significance: Haptoglobin has promising therapeutic implications in extracellular protein deposition diseases.

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Section: Discussionmentioning

confidence: 99%

The Extracellular Chaperone Haptoglobin Prevents Serum Fatty Acid-promoted Amyloid Fibril Formation of β2-Microglobulin, Resistance to Lysosomal Degradation, and Cytotoxicity

Sultan¹,

Raman

Rao

et al. 2013

Journal of Biological Chemistry

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“…Both of those patients had plasma cell dyscrasias. 6,7 Our patient did not have a plasma cell dyscrasia, but did carry a longstanding diagnosis of Sjogren's syndrome, which has been associated with nodular pulmonary amyloidosis in a handful of case reports. 8 In fact, Sjogren's syndrome is more commonly associated with primary localized cutaneous nodular amyloidosis and interestingly, some authors have described beta-2 microglobulin as the major component of primary localized cutaneous nodular amyloidosis, 9 whereas others have demonstrated both lambda and kappa light chains.…”

Section: Discussionmentioning

confidence: 93%

Nodular pulmonary amyloidosis with an unusual protein composition diagnosed by fine‐needle aspiration biopsy: A case report

Yang

Blutreich

Das

2009

Diagnostic Cytopathology

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Nodular pulmonary amyloidosis is rare, but a number of individual cases have been reported in the literature. Radiologically, pulmonary amyloid nodules often mimic cancer and hence require biopsy to obtain a specimen for definitive diagnosis. We describe a case of isolated nodular pulmonary amyloidosis with an unusual amyloid composition that given the patient's clinical history has not been described in the literature to the best of our knowledge, making this case unique. A 58-year-old woman with a history of mixed connective tissue disease was found to have multiple lung nodules on chest computed tomography (CT) that were radiologically suspicious for cancer. A CT-guided percutaneous fine-needle aspiration (FNA) biopsy of one of the nodules was performed. A diagnosis of amyloid was rendered using special stains and polarized light microscopic examination. Immunohistochemical stains revealed that the amyloid comprised beta-2 microglobulin as well as both kappa and lambda light chains. Further work up showed no evidence of systemic amyloidosis. We were successful in rendering an accurate diagnosis of a pulmonary amyloidoma on material procured by CT-guided FNA thus avoiding more invasive procedures. In addition, immunohistochemical staining revealed an unexpected and highly unusual protein composition of the amyloid.

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Cutaneous deposits

Weedon

2010

Weedon's Skin Pathology

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Coexistence of beta2 microglobulin and lambda light chain in amyloid fibrils of dialysis-unrelated plasma cell dyscrasia-associated systemic amyloidosis

Abstract: These results indicate that beta2 microglobulin is a component of amyloid fibrils in PASA.

Cited by 6 publications

References 22 publications

The Extracellular Chaperone Haptoglobin Prevents Serum Fatty Acid-promoted Amyloid Fibril Formation of β2-Microglobulin, Resistance to Lysosomal Degradation, and Cytotoxicity

The Extracellular Chaperone Haptoglobin Prevents Serum Fatty Acid-promoted Amyloid Fibril Formation of β2-Microglobulin, Resistance to Lysosomal Degradation, and Cytotoxicity

Nodular pulmonary amyloidosis with an unusual protein composition diagnosed by fine‐needle aspiration biopsy: A case report

Cutaneous deposits

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