Differential effects on light chain amyloid formation depend on mutations and type of glycosaminoglycans

Luis M. Blancas-Mejía, Jared Hammernik, Marta Marin-Argany, Marina Ramirez-Alvarado

Research output: Contribution to journalArticlepeer-review

25 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)4953-4965
Number of pages13
JournalJournal of Biological Chemistry
Volume290
Issue number8
DOIs
StatePublished - Feb 20 2015

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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