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Carbamylation of the amino‐terminal residue (Gly1) of mouse serum amyloid A promotes amyloid formation in a cell culture model
Author(s) -
KluveBeckerman Barbara,
Liepnieks Juris J.,
Benson Merrill D.,
Lai Xianyin,
Qi Guihong,
Wang Mu
Publication year - 2016
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 - 10.1002/1873-3468.12472
Subject(s) - amyloidosis , amyloid (mycology) , serum amyloid a , fibril , aa amyloidosis , inflammation , chemistry , in vitro , amyloid disease , biochemistry , senile plaques , residue (chemistry) , protein subunit , amyloid fibril , biology , immunology , medicine , amyloid β , alzheimer's disease , disease , inorganic chemistry , familial mediterranean fever , gene
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.