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The amyloid fibrils of the constant domain of immunoglobulin light chain
Author(s) -
Yamamoto Kaori,
Yagi Hisashi,
Lee Young-Ho,
Kardos József,
Hagihara Yoshihisa,
Naiki Hironobu,
Goto Yuji
Publication year - 2010
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2010.06.019
Subject(s) - immunoglobulin light chain , fibril , amyloidosis , thioflavin , beta 2 microglobulin , chemistry , amyloid (mycology) , amyloid fibril , antibody , biophysics , immunoglobulin g , al amyloidosis , congo red , crystallography , biochemistry , immunology , pathology , biology , alzheimer's disease , amyloid β , medicine , adsorption , disease , organic chemistry , inorganic chemistry
Light chain‐associated (AL) amyloidosis is characterized by dominant fibril deposition of the variable domain (VL) of an immunoglobulin light chain, and thus its constant domain (CL) has been considered not to be amyloidogenic. We examined the in vitro fibril formation of the isolated CL in comparison with β 2 ‐microglobulin (β2‐m), an immunoglobulin domain‐like amyloidogenic protein responsible for dialysis‐related amyloidosis. Two methods useful for β2‐m at neutral pH also induced amyloid fibrils of CL, which were monitored by thioflavin‐T binding and electron microscopy (EM). These results suggest that CL plays an important role, more than previously assumed, in the development of AL‐amyloidosis.