Variant apolipoprotein AI as a major constituent of a human hereditary amyloid

William C. Nichols, Francis E. Dwulet, Juris Liepnieks, Merrill Benson

Research output: Contribution to journalArticle

171 Citations (Scopus)

Abstract

Amyloid fibrils were isolated from spleen and liver of a patient who died with Familial Amyloidotic Polyneuropathy Type III (Iowa). The major protein constituent of the fibrils was found to be the amino terminal portion (residues 1-83) of apolipoprotein AI with an arginine for glycine substitution at position 26. This is the first report of an apolipoprotein as a major amyloid constituent in a form of autosomal dominant hereditary amyloidosis in humans.

Original languageEnglish
Pages (from-to)762-768
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume156
Issue number2
DOIs
StatePublished - Oct 31 1988

Fingerprint

Apolipoprotein A-I
Amyloid
Familial Amyloidosis
Polyneuropathies
Apolipoproteins
Liver
Glycine
Arginine
Substitution reactions
Spleen
Proteins

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Variant apolipoprotein AI as a major constituent of a human hereditary amyloid. / Nichols, William C.; Dwulet, Francis E.; Liepnieks, Juris; Benson, Merrill.

In: Biochemical and Biophysical Research Communications, Vol. 156, No. 2, 31.10.1988, p. 762-768.

Research output: Contribution to journalArticle

Nichols, William C. ; Dwulet, Francis E. ; Liepnieks, Juris ; Benson, Merrill. / Variant apolipoprotein AI as a major constituent of a human hereditary amyloid. In: Biochemical and Biophysical Research Communications. 1988 ; Vol. 156, No. 2. pp. 762-768.
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