Carbamylation of the amino-terminal residue (Gly1) of mouse serum amyloid A promotes amyloid formation in a cell culture model

Barbara Kluve-Beckerman, Juris J. Liepnieks, Merrill Benson, Xianyin Lai, Guihong Qi, Mu Wang

Research output: Contribution to journalLetter

4 Scopus citations

Abstract

Amyloid A (AA) amyloidosis is a fatal protein deposition disease afflicting a small percentage of patients with chronic inflammation. Factors other than inflammation that determine development of AA amyloidosis remain largely unknown. The subunit protein comprising AA amyloid fibrils is derived from serum amyloid A (SAA), specifically its amino-terminal portion. In this in vitro study, carbamylation of residues in this region (primarily Gly1 but also Lys24) was shown to markedly increase amyloid-forming propensity as judged by extensive accumulation of amyloid in cell cultures. Contrastingly, no amyloid deposition occurred in cultures given SAA having a noncarbamylated amino terminus. Carbamylation, known to occur during uremia or inflammation, merits investigation as a potential determinant of AA amyloid fibril formation.

Original languageEnglish (US)
Pages (from-to)4296-4307
Number of pages12
JournalFEBS Letters
Volume590
Issue number23
DOIs
StatePublished - Dec 1 2016

Keywords

  • amyloidosis
  • carbamylation
  • inflammation
  • post-translational modification
  • serum amyloid A
  • urea

ASJC Scopus subject areas

  • Structural Biology
  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Fingerprint Dive into the research topics of 'Carbamylation of the amino-terminal residue (Gly1) of mouse serum amyloid A promotes amyloid formation in a cell culture model'. Together they form a unique fingerprint.

  • Cite this