A new apolipoprotein Al variant, Trp50Arg, causes hereditary amyloidosis

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 amyloid...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:QJM : An International Journal of Medicine 1995-10, Vol.88 (10), p.695-702
Hauptverfasser: 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.
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
Beschreibung
Zusammenfassung: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.
ISSN:0033-5614
1460-2725
1460-2393
1464-3855
1460-2393
DOI:10.1093/oxfordjournals.qjmed.a068993