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Innere Medizin (Heidelberg, Germany), 2023
Light chain amyloidosis (AL) is a rare protein deposition disease. It is caused by a clonal plasma cell or B‑cell disease in the bone marrow. With the exception of the central nervous system, all organs can be affected by amyloid deposits. Cardiac involvement is the most frequent organ manifestation that leads to significantly increased mortality when ...
Ute, Hegenbart +2 more
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Light chain amyloidosis (AL) is a rare protein deposition disease. It is caused by a clonal plasma cell or B‑cell disease in the bone marrow. With the exception of the central nervous system, all organs can be affected by amyloid deposits. Cardiac involvement is the most frequent organ manifestation that leads to significantly increased mortality when ...
Ute, Hegenbart +2 more
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Amyloidosis and Light Chain Plasmocytoma
Tumori Journal, 1976Nine cases of light chain plasmocytomas, 6 type λ and 3 type k, have been studied in reference to amyloid presence and localisation. Bone marrow plasmocytosis, light chains in serum and/or in the urine, and osteolytic lesions were demonstrated in all the patients.
G, Tosato, E, Fagiolo
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Coagulation Abnormalities in Light Chain Amyloidosis
Mayo Clinic Proceedings, 2021To assess the prevalence of coagulation abnormalities in patients with systemic light chain (AL) amyloidosis and their association with disease-related characteristics, disease progression, and survival.This is a retrospective study of patients with AL amyloidosis seen at Mayo Clinic, Rochester, Minnesota, from January 1, 2006, to December 31, 2015. We
Nadine Abdallah +16 more
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Macroglossia in Light-Chain Amyloidosis
New England Journal of Medicine, 2018Macroglossia in Light-Chain Amyloidosis A 78-year-old man presented with enlargement and stiffening of the tongue. Biopsy confirmed that this finding of macroglossia was due to light-chain amyloidosis.
João Melo Alves, Natália Marto
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Immunoglobulin Light Chain Systemic Amyloidosis
2016Immunoglobulin light chain amyloidosis (AL) is a rare, complex disease caused by misfolded free light chains produced by a usually small, indolent plasma cell clone. Effective treatments exist that can alter the natural history, provided that they are started before irreversible organ damage has occurred.
Angela, Dispenzieri, Giampaolo, Merlini
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2016
Light-chain (AL) amyloidosis is the most common cause of acquired systemic amyloidosis. It is a highly heterogeneous disease with a wide spectrum of clinical presentation. Prognosis of AL amyloidosis depends on organ, particularly cardiac, involvement.
Amara S. Hussain, Anita D’Souza
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Light-chain (AL) amyloidosis is the most common cause of acquired systemic amyloidosis. It is a highly heterogeneous disease with a wide spectrum of clinical presentation. Prognosis of AL amyloidosis depends on organ, particularly cardiac, involvement.
Amara S. Hussain, Anita D’Souza
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Systemic Immunoglobulin Light-Chain Amyloidosis
Clinical Lymphoma and Myeloma, 2006Amyloidosis is a rare disease in which amyloid fibrils compromise organ function and lead to death. Systemic immunoglobulin light-chain amyloidosis, usually caused by free light chains (FLCs) made by clonal plasma cells, is the most frequent type. Hereditary and senile systemic amyloidosis are less frequent types.
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Managing Systemic Light-Chain Amyloidosis
Journal of the National Comprehensive Cancer Network, 2007Amyloidosis is a rare disease in which a specific protein is deposited as aggregated interstitial fibrils that can compromise organ function and lead to death. Immunoglobulin (Ig) light-chain amyloidosis (AL), caused by the monoclonal gammopathy of a plasma cell dyscrasia, is the most common type.
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Treatment of immunoglobulin light chain amyloidosis
Current Hematologic Malignancy Reports, 2009No therapy is uniformly effective in the management of immunoglobulin light chain amyloidosis (AL amyloidosis). Despite the common generalization, therapy is highly effective. Options available to patients with AL amyloidosis include high-dose therapy, but this is applicable to only about one fourth of patients.
Morie A, Gertz, Steven R, Zeldenrust
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Equine light-chain-associated amyloidosis
Amyloid, 1996We have previously immunologically typed amyloid protein extracted from a horse with malignant histiolymtphocytic lymphosarcoma as immunoglobulin (Ig)-derived amylaid. In the present paper, the Ig character of the horse amyloid is confirmed by the amino acid sequence of the constituent protein.
Theodoor A. Niewold +4 more
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