Results 301 to 310 of about 248,637 (315)

Immunoglobulin Light Chain Systemic Amyloidosis

2016
Immunoglobulin 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
openaire   +3 more sources

[14] In vitro immunoglobulin light chain fibrillogenesis

1999
These 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, Alan Solomon, Jonathan S. Wall   +2 more
openaire   +2 more sources

Shared epitopes of avian immunoglobulin light chains

Veterinary Immunology and Immunopathology, 2014
Like 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, Mateja Benčina, Peter Dovč, Rebeka Lucijana Berčič, Dušan Benčina, Mojca Narat   +5 more
openaire   +3 more sources

Abnormal immunoglobulin synthesis in monoclonal immunoglobulin light chain and light and heavy chain deposition disease

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
openaire   +3 more sources

RL allotypes of light chains of rat immunoglobulins

Immunochemistry, 1971
Abstract 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, T.I. Vengerova, R.S. Nezlin   +2 more
openaire   +3 more sources

Interaction between Glycosaminoglycans and Immunoglobulin Light Chains

Biochemistry, 1997
Amyloidosis 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, Peter Lykos, Fred J. Stevens, Xiaoli Jiang   +3 more
openaire   +3 more sources

Light chain ratios of serum immunoglobulins in disease

Clinical Biochemistry, 1991
We 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, Christopher W.K. Lam, S. H. Chui, K. N. Lai, Edmund K. Li   +4 more
openaire   +3 more sources

Glycosylation of immunoglobulin light chains associated with amyloidosis

Amyloid, 2000
AL 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, Gunnar Husby, David Bailey, David V. Renouf, L. A. Omtvedt, Svein Haavik, Nikolay A. Paramonov, Elizabeth F. Hounsell, Michael J. Davies   +8 more
openaire   +3 more sources

Junctional diversity in Xenopus immunoglobulin light chains

Molecular Immunology, 1999
Xenopus cDNA sequences encoding the homolog of mammalian kappa (kappa) light (L) chains were isolated from isogenic tadpole and adult individuals to investigate whether there existed stage-specific immunoglobulin L chain expression and somatic diversification.
Youngran Ji, Ellen Hsu, Soléenne Desravines   +2 more
openaire   +3 more sources

Immunoglobulin transport in the absence of light chains

Trends in Biochemical Sciences, 2010
In their recent TIBS article [1], Feige and colleagues place a strong emphasis on the role of the first immunoglobulin (Ig) constant domain, CH1, in preventing transport of the Ig heavy chain (HC) to the cell surface when Ig light chains are absent.
openaire   +2 more sources