scholarly journals Current and New Perspectives on the Molecular and Cellular Mechanisms of Amyloid Formation and Toxicity in Light Chain Amyloidosis

10.5772/19477 ◽  
2011 ◽  
Author(s):  
Ara Celi ◽  
Marina Ramirez-Alvarado
Keyword(s):  
Light Chain ◽  
Amyloid Formation ◽  
Cellular Mechanisms ◽  
Light Chain Amyloidosis

scholarly journals Thermal Stability Threshold for Amyloid Formation in Light Chain Amyloidosis

2013 ◽  
Vol 14 (11) ◽  
pp. 22604-22617 ◽  
Author(s):  
Tanya Poshusta ◽  
Nagaaki Katoh ◽  
Morie Gertz ◽  
Angela Dispenzieri ◽  
Marina Ramirez-Alvarado
Keyword(s):  
Thermal Stability ◽  
Light Chain ◽  
Amyloid Formation ◽  
Stability Threshold ◽  
Light Chain Amyloidosis

Stability and aggregation propensity do not fully account for the association of various germline variable domain gene segments with light chain amyloidosis

2017 ◽  
Vol 398 (4) ◽  
pp. 477-489 ◽  
Author(s):  
Sergio A. Garay Sánchez ◽  
Francisco Javier Rodríguez Álvarez ◽  
Guadalupe Zavala-Padilla ◽  
Luz María Mejia-Cristobal ◽  
Armando Cruz-Rangel ◽  
...  
Keyword(s):  
Light Chain ◽  
Conformational Stability ◽  
Variable Domain ◽  
Amyloid Formation ◽  
Aggregation Propensity ◽  
Light Chain Amyloidosis ◽  
Formation Kinetics ◽  
Domain V ◽  
Kinetics Of

Abstract Variable domain (VL) gene segments exhibit variable tendencies to be associated with light chain amyloidosis (AL). While few of them are very frequent in AL and give rise to most of the amyloidogenic light chains compiled at the sequence databases, other are rarely found among the AL cases. To analyze to which extent these tendencies depend on folding stability and aggregation propensity of the germline VL protein, we characterized VL proteins encoded by four AL-associated germline gene segments and one not associated to AL. We found that the AL-associated germline rVL proteins differ widely in conformational stability and propensity to in vitro amyloid aggregation. While in vitro the amyloid formation kinetics of these proteins correlate well with their folding stabilities, the folding stability does not clearly correlate with their germline’s frequencies in AL. We conclude that the association of the VL genes segments to amyloidosis is not determined solely by the folding stability and aggregation propensity of the germline VL protein. Other factors, such as the frequencies of destabilizing mutations and susceptibility to proteolysis, must play a role in determining the light chain amyloidogenicity.

Prognostic stratification and treatment of cardiac light chain amyloidosis: A narrow path in the jungle

2014 ◽  
Vol 33 (2) ◽  
pp. 136-138 ◽  
Author(s):  
Luciano Potena ◽  
Candida Cristina Quarta ◽  
Francesco Grigioni ◽  
Claudio Rapezzi
Keyword(s):  
Light Chain ◽  
Light Chain Amyloidosis ◽  
Prognostic Stratification

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.

Severe intrahepatic cholestasis as the initial manifestation of light chain amyloidosis

2021 ◽  
Vol 44 (1) ◽  
pp. 29-31
Author(s):  
Diego Martínez-Acitores de la Mata ◽  
Silvia Bravo Meléndez ◽  
Candela Ceballos Bolaños ◽  
Irene Amat Villegas ◽  
María Carmen Mateos Rodriguez ◽  
...  
Keyword(s):  
Light Chain ◽  
Intrahepatic Cholestasis ◽  
Initial Manifestation ◽  
Light Chain Amyloidosis
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