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Immunoglobulin Light Chain and Systemic Light-Chain Amyloidosis
2007Light-chain amyloidosis (AL) is characterized by the clonal expansion of plasma B cells that secrete large amounts of monoclonal immunoglobulin light chains. The free light chains circulate in serum and form amyloid fibrils on vital organs such as the kidney, heart, and liver causing organ failure and eventually death.
Richard W. McLaughlin +5 more
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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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Nonchemotherapy Treatment of Immunoglobulin Light Chain Amyloidosis
Acta Haematologica, 2020Immunoglobulin light chain amyloidosis (AL amyloidosis) is a rare, life-threatening disease characterized by the deposition of misfolded proteins in vital organs such as the heart, the lungs, the kidneys, the peripheral nervous system, and the gastrointestinal tract. This causes a direct toxic effect, eventually leading to organ failure. The underlying
Suzanne Lentzsch, Layla Van Doren
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[14] In vitro immunoglobulin light chain fibrillogenesis
1999These techniques permit the production of bulk quantities of fibrils and provide methods for monitoring the kinetics of fibrillogenesis. Experiments performed in the fluorimeter require low protein concentrations, sampling is not necessary (with ThT in situ), and the measured fluorescence signal is indicative of fibril content and is not complicated by
Charles L. Murphy +2 more
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Shared epitopes of avian immunoglobulin light chains
Veterinary Immunology and Immunopathology, 2014Like all jawed vertebrates, birds (Aves) also produce antibodies i.e. immunoglobulins (Igs) as a defence mechanism against pathogens. Their Igs are composed of two identical heavy (H) and light (L) chains which are of lambda isotype. The L chain consists of variable (VL), joining (JL) and constant (CL) region.
Ivanka Cizelj +5 more
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Amyloid, 2001
The Congo red-binding fibrils of AL amyloidosis are the most common form of monoclonal immunoglobulin tissue deposition (MIDD). Nonetheless, the less structured deposits found in light chain deposition disease (LCDD) and the similar, but distinct, deposits of light and heavy chain deposition disease (LHCDD) and heavy chain deposition disease (HCDD) can
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The Congo red-binding fibrils of AL amyloidosis are the most common form of monoclonal immunoglobulin tissue deposition (MIDD). Nonetheless, the less structured deposits found in light chain deposition disease (LCDD) and the similar, but distinct, deposits of light and heavy chain deposition disease (LHCDD) and heavy chain deposition disease (HCDD) can
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Interaction between Glycosaminoglycans and Immunoglobulin Light Chains
Biochemistry, 1997Amyloidosis is a pathological process in which normally soluble proteins polymerize to form insoluble fibrils (amyloid). Amyloid formation is found in a number of diseases, including Alzheimer's disease, adult-onset diabetes, and light-chain-associated amyloidosis.
Elizabeth A. Myatt +3 more
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RL allotypes of light chains of rat immunoglobulins
Immunochemistry, 1971Abstract Allotypes of rat immunoglobulins have been detected by using the inhibition of immunoadsorption of iodinated rat immunoglobulin G on corresponding antibodies fixed on cellulose. The observed allotypic differences between the immunoglobulins of inbred rat strains—strain MSUB1 on the one hand and rat strains WAG and August on the other are due
O.V. Rokhlin +2 more
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Light chain ratios of serum immunoglobulins in disease
Clinical Biochemistry, 1991We have determined the individual kappa (kappa)/lambda (lambda) ratios of serum IgG, IgA, and IgM in normal subjects and patients with rheumatoid arthritis, systemic lupus erythematosus, hepatic cirrhosis and IgA nephropathy--40 in each group. Serum samples were first screened by agarose electrophoresis to exclude paraproteinaemia.
Nancy Leung +4 more
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Glycosylation of immunoglobulin light chains associated with amyloidosis
Amyloid, 2000AL amyloidosis is a fatal disease caused by deposition of immunoglobulin light chains in a fibrillarforin (AL) in various organs. By searching the Kabat database of immunoglobulin sequences using the KabatMan software, we have shown that there is a preponderance of the consensus glycosylation sequon (AsnXxxSer/Thr) in the framework regions of amyloid ...
Knut Sletten +8 more
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