scholarly journals Salts enhance both protein stability and amyloid formation of an immunoglobulin light chain

2008 ◽  
Vol 135 (1-3) ◽  
pp. 25-31 ◽  
Author(s):  
Laura A. Sikkink ◽  
Marina Ramirez-Alvarado
Keyword(s):  
Protein Stability ◽  
Light Chain ◽  
Amyloid Formation ◽  
Immunoglobulin Light Chain

scholarly journals Heat-induced native dimerization prevents amyloid formation by variable domain from immunoglobulin light-chain REI

FEBS Journal ◽  
2017 ◽  
Vol 284 (18) ◽  
pp. 3114-3127 ◽  
Author(s):  
Marina Nawata ◽  
Hirotaka Tsutsumi ◽  
Yuta Kobayashi ◽  
Satoru Unzai ◽  
Shouhei Mine ◽  
...  
Keyword(s):  
Light Chain ◽  
Variable Domain ◽  
Amyloid Formation ◽  
Immunoglobulin Light Chain

Probing the role of λ6 immunoglobulin light chain dimerization in amyloid formation

2016 ◽  
Vol 1864 (4) ◽  
pp. 409-418 ◽  
Author(s):  
Mathieu Laporte Wolwertz ◽  
Phuong Trang Nguyen ◽  
Noé Quittot ◽  
Steve Bourgault
Keyword(s):  
Light Chain ◽  
Amyloid Formation ◽  
Immunoglobulin Light Chain

scholarly journals The effects of sodium sulfate, glycosaminoglycans, and Congo red on the structure, stability, and amyloid formation of an immunoglobulin light-chain protein

2006 ◽  
Vol 15 (7) ◽  
pp. 1710-1722 ◽  
Author(s):  
Richard W. Mclaughlin ◽  
Janelle K. De Stigter ◽  
Laura A. Sikkink ◽  
Elizabeth M. Baden ◽  
Marina Ramirez-Alvarado
Keyword(s):  
Light Chain ◽  
Congo Red ◽  
Sodium Sulfate ◽  
Structure Stability ◽  
Amyloid Formation ◽  
Immunoglobulin Light Chain

scholarly journals Inhibition by small-molecule ligands of formation of amyloid fibrils of an immunoglobulin light chain variable domain

eLife ◽  
2015 ◽  
Vol 4 ◽  
Author(s):  
Boris Brumshtein ◽  
Shannon R Esswein ◽  
Lukasz Salwinski ◽  
Martin L Phillips ◽  
Alan T Ly ◽  
...  
Keyword(s):  
Small Molecule ◽  
Light Chain ◽  
Amyloid Fibrils ◽  
Variable Domain ◽  
Light Chains ◽  
Amyloid Formation ◽  
Immunoglobulin Light Chains ◽  
Immunoglobulin Light Chain ◽  
Small Molecule Ligands ◽  
Irreversible Aggregation

Overproduction of immunoglobulin light chains leads to systemic amyloidosis, a lethal disease characterized by the formation of amyloid fibrils in patients' tissues. Excess light chains are in equilibrium between dimers and less stable monomers which can undergo irreversible aggregation to the amyloid state. The dimers therefore must disassociate into monomers prior to forming amyloid fibrils. Here we identify ligands that inhibit amyloid formation by stabilizing the Mcg light chain variable domain dimer and shifting the equilibrium away from the amyloid-prone monomer.

scholarly journals A Unique Case of Combined Nodular and Tracheobronchial Amyloidosis

2021 ◽  
Vol 2021 (2) ◽  
Author(s):  
Feihong Ding ◽  
Yun Li ◽  
Shailesh Balasubramanian ◽  
Subha Ghosh ◽  
Jason N Valent ◽  
...  
Keyword(s):  
Light Chain ◽  
Systemic Disease ◽  
Amyloid Deposition ◽  
Misfolded Proteins ◽  
Immunoglobulin Light Chain ◽  
Anatomic Site ◽  
Unique Case ◽  
Pulmonary Amyloidosis ◽  
Immunoglobulin Light Chain Amyloidosis ◽  
Tracheobronchial Amyloidosis

ABSTRACT Amyloidosis is a heterogeneous group of diseases characterized by the extracellular deposition of misfolded proteins that can affect either systemically or locally confined to one system. Pulmonary amyloidosis is rare and can be classified into three forms according to the anatomic site of involvement: nodular pulmonary amyloidosis, tracheobronchial amyloidosis and diffuse alveolar-septal amyloidosis. The former two usually represent localized amyloid disease and the latter represents systemic disease. Typically lung parenchymal and tracheobronchial amyloidosis do not present together in localized forms of pulmonary amyloidosis. Here we report a unique case of localized pulmonary immunoglobulin light-chain amyloidosis, manifested as both parenchymal nodules and tracheobronchial amyloid deposition.

Two distinct mechanisms of neuropathy in immunoglobulin light chain (AL) amyloidosis

2021 ◽  
pp. 117305
Author(s):  
Haruki Koike ◽  
Naohiro Mouri ◽  
Yuki Fukami ◽  
Masahiro Iijima ◽  
Koji Matsuo ◽  
...  
Keyword(s):  
Light Chain ◽  
Al Amyloidosis ◽  
Immunoglobulin Light Chain

scholarly journals Variance analysis of immunoglobulin alleles in natural populations of rabbit (Oryctolagus cuniculus): the extensive interallelic divergence at the b locus could be the outcome of overdominance-type selection.

Genetics ◽  
1993 ◽  
Vol 135 (1) ◽  
pp. 171-187 ◽  
Author(s):  
W van der Loo
Keyword(s):  
Heavy Chain ◽  
Light Chain ◽  
Gene Diversity ◽  
Natural Populations ◽  
Constant Region ◽  
Immunoglobulin Light Chain ◽  
Evolutionary Patterns ◽  
B Locus ◽  
Type Selection ◽  
Predominant Allele

Abstract Population genetic data are presented which should contribute to evaluation of the hypothesis that the extraordinary evolutionary patterns observed at the b locus of the rabbit immunoglobulin light chain constant region can be the outcome of overdominance-type selection. The analysis of allele correlations in natural populations revealed an excess of heterozygotes of about 10% at the b locus while heterozygote excess was not observed at loci determining the immunoglobulin heavy chain. Data from the published literature, where homozygote advantage was suggested, were reevaluated and found in agreement with data here presented. Gene diversity was evenly distributed among populations and showed similarities with patterns reported for histocompatibility loci. Analysis of genotypic disequilibria revealed strong digenic associations between the leading alleles of heavy and light chain constant region loci in conjunction with trigenic disequilibria corresponding to a preferential association of b locus heterozygosity with the predominant allele of the heavy chain e locus. It is argued that this may indicate compensatory or nonadditive aspects of a putative heterozygosity enhancing mechanism, implying that effects at the light chain might be more pronounced in populations fixed for the heavy chain polymorphism.

scholarly journals Genetic pathogenesis of immunoglobulin light chain amyloidosis: basic characteristics and clinical applications

2021 ◽  
Vol 10 (1) ◽  
Author(s):  
Linchun Xu ◽  
Yongzhong Su
Keyword(s):  
Plasma Cell ◽  
Light Chain ◽  
Amyloid Fibril ◽  
Treatment Modalities ◽  
Driver Gene ◽  
Immunoglobulin Light Chain ◽  
Disease Evolution ◽  
Genetic Aberrations ◽  
Light Chain Amyloidosis ◽  
Immunoglobulin Light Chain Amyloidosis

AbstractImmunoglobulin light chain amyloidosis (AL) is an indolent plasma cell disorder characterized by free immunoglobulin light chain (FLC) misfolding and amyloid fibril deposition. The cytogenetic pattern of AL shows profound similarity with that of other plasma cell disorders but harbors distinct features. AL can be classified into two primary subtypes: non-hyperdiploidy and hyperdiploidy. Non-hyperdiploidy usually involves immunoglobulin heavy chain translocations, and t(11;14) is the hallmark of this disease. T(11;14) is associated with low plasma cell count but high FLC level and displays distinct response outcomes to different treatment modalities. Hyperdiploidy is associated with plasmacytosis and subclone formation, and it generally confers a neutral or inferior prognostic outcome. Other chromosome abnormalities and driver gene mutations are considered as secondary cytogenetic aberrations that occur during disease evolution. These genetic aberrations contribute to the proliferation of plasma cells, which secrete excess FLC for amyloid deposition. Other genetic factors, such as specific usage of immunoglobulin light chain germline genes and light chain somatic mutations, also play an essential role in amyloid fibril deposition in AL. This paper will propose a framework of AL classification based on genetic aberrations and discuss the amyloid formation of AL from a genetic aspect.

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