title: Carbamylation of the amino-terminal residue (Gly1) of mouse serum amyloid A promotes amyloid formation in a cell culture model.
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.
authors: Department of Pathology and Laboratory Medicine, Indiana University School of Medicine, Indianapolis, IN, USA.
authors: Barbara
authors: B
authors: Kluve-Beckerman
authors: Department of Pathology and Laboratory Medicine, Indiana University School of Medicine, Indianapolis, IN, USA.
authors: Juris J
authors: JJ
authors: Liepnieks
authors: Department of Pathology and Laboratory Medicine, Indiana University School of Medicine, Indianapolis, IN, USA.|Roudebush VA Medical Center, Indianapolis, IN, USA.
authors: Merrill D
authors: MD
authors: Benson
authors: Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, IN, USA.
authors: Xianyin
authors: X
authors: Lai
authors: Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, IN, USA.
authors: Guihong
authors: G
authors: Qi
authors: Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, IN, USA.
authors: Mu
authors: M
authors: Wang
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002478:Cells, Cultured; D005998:Glycine / Q000378:metabolism*; D006801:Humans; D051379:Mice; D010447:Peptide Hydrolases / Q000378:metabolism; D055503:Protein Multimerization; D011499:Protein Processing, Post-Translational; D017433:Protein Structure, Secondary; D059748:Proteolysis; D000685:Serum Amyloid A Protein / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D000685:Serum Amyloid A Protein; D010447:Peptide Hydrolases; D005998:Glycine
keywords: amyloidosis; carbamylation; inflammation; post-translational modification; serum amyloid A; urea