TY - JOUR
T1 - Differential effects on light chain amyloid formation depend on mutations and type of glycosaminoglycans
AU - Blancas-Mejía, Luis M.
AU - Hammernik, Jared
AU - Marin-Argany, Marta
AU - Ramirez-Alvarado, Marina
N1 - Publisher Copyright:
© 2015 by The American Society for Biochemistry and Molecular Biology, Inc.
PY - 2015/2/20
Y1 - 2015/2/20
N2 - Background: Extracellular amyloid deposits involve glycosaminoglycans (GAGs). Results: Fibrillation of AL proteins was accelerated by heparan sulfate and inhibited by chondroitin sulfate A. Conclusion: Endogenous GAGs can modulate amyloid formation, and their effect is determined by the amyloidogenic properties of AL proteins studied. Significance: Biologically relevant molecules like GAGs play a major role in the amyloidogenicity of AL proteins.
AB - Background: Extracellular amyloid deposits involve glycosaminoglycans (GAGs). Results: Fibrillation of AL proteins was accelerated by heparan sulfate and inhibited by chondroitin sulfate A. Conclusion: Endogenous GAGs can modulate amyloid formation, and their effect is determined by the amyloidogenic properties of AL proteins studied. Significance: Biologically relevant molecules like GAGs play a major role in the amyloidogenicity of AL proteins.
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U2 - 10.1074/jbc.M114.615401
DO - 10.1074/jbc.M114.615401
M3 - Article
C2 - 25538238
AN - SCOPUS:84929105231
SN - 0021-9258
VL - 290
SP - 4953
EP - 4965
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 8
ER -