A new apolipoprotein Al variant, Trp50Arg, causes hereditary amyloidosis
BOOTH, D.R.; TAN, S.Y.; BOOTH, S.E.; HSUAN, J.J.; TOTTY, N.F.; NGUYEN, O.; HUTTON, T.; VIGUSHIN, D.M.; TENNENT, G.A.; HUTCHINSON, W.L.; THOMSON, N.; SOUTAR, A.K.; HAWKINS, P.N.; PEPYS, M.B.; BOOTH D.R.; Immunological Medicine Unit, Department of Medicine, Royal Postgraduate Medical School, Hammersmith Hospital; TAN S.Y.; Immunological Medicine Unit, Department of Medicine, Royal Postgraduate Medical School, Hammersmith Hospital; BOOTH S.E.; Immunological Medicine Unit, Department of Medicine, Royal Postgraduate Medical School, Hammersmith Hospital; HSUAN J.J.; Ludwig Institute for Cancer Research, University College London School of Medicine; TOTTY N.F.; Ludwig Institute for Cancer Research, University College London School of Medicine; NGUYEN O.; Ludwig Institute for Cancer Research, University College London School of Medicine; HUTTON T.; Fisons VG BioTech, Altrincham; VIGUSHIN D.M.; Immunological Medicine Unit, Department of Medicine, Royal Postgraduate Medical School, Hammersmith Hospital; TENNENT G.A.; Immunological Medicine Unit, Department of Medicine, Royal Postgraduate Medical School, Hammersmith Hospital; HUTCHINSON W.L.; Immunological Medicine Unit, Department of Medicine, Royal Postgraduate Medical School, Hammersmith Hospital; THOMSON N.; Department of Medicine, Monash University; SOUTAR A.K.; MRC Lipoprotein Team, Department of Medicine, Royal Postgraduate Medical School, Hammersmith Hospital; HAWKINS P.N.; Immunological Medicine Unit, Department of Medicine, Royal Postgraduate Medical School, Hammersmith Hospital; PEPYS M.B.; Immunological Medicine Unit, Department of Medicine, Royal Postgraduate Medical School, Hammersmith Hospital
Журнал:
Quarterly Journal of Mechanics and Applied Mathematics
Дата:
1995
Аннотация:
A man with hereditary non-neuropathic systemic amyloidosis had amyloid fibril protein subunits consisting of N-terminal fragments (residues 1–86, 1–92 and 1–93) of a previously unknown variant of apolipoprotein Al, Trp50Arg, encoded by a thyminecytosine transition. This is the third reported amyloidogenic apoAl variant. All involve substitutions of single neutral amino acids by the cationic residue arginine, suggesting a common mechanism of amyloidogenesis. However, the phenotypic expression of these mutations varies both within and between the seven known families with hereditary apoAl amyloidosis. These findings should facilitate analysis of the molecular basis of fibrillogenesis and of factors that modulate amyloid deposition and its consequences in vivo.
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