Comparison of amyloid fibril formation by two closely related immunoglobulin light chain variable domains

Autor:	Marina Ramirez-Alvarado, Douglas J. Martin
Rok vydání:	2010
Předmět:	Amyloid Chemistry Circular Dichroism Amyloidosis Blotting Western medicine.disease Fibril Immunoglobulin light chain Phenotype Article In vitro Germline Cell biology Microscopy Electron Transmission Biochemistry Internal Medicine medicine AL amyloidosis Humans Immunoglobulin Light Chains
Zdroj:	Amyloid. 17:129-136
ISSN:	1744-2818 1350-6129
DOI:	10.3109/13506129.2010.530081
Popis:	Light chain amyloidosis (AL amyloidosis) is a haematological disorder in which a clonal population of B cells expands and secretes enormous amounts of the immunoglobulin light chain protein. These light chains misfold and aggregate into amyloid fibrils, leading to organ dysfunction and death. We have studied the in vitro fibril formation kinetics of two patient-derived immunoglobulin light chain variable domain proteins, designated AL-09 and AL-103, in response to changes in solution conditions. Both proteins are members of the κI O18:O8 germline and therefore are highly similar in sequence, but they presented with different clinical phenotypes. We find that AL-09 forms fibrils more readily and more rapidly than AL-103 in vitro, mirroring the clinical phenotypes of the patients and suggesting a possible connection between the fibril kinetics of the disease protein and the disease progression.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5fa96c74434f92d73213330a8e749c92 https://doi.org/10.3109/13506129.2010.530081 Zobrazit plný text záznamu Plný text ve formátu PDF Plný text ve formátu HTML
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