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  • Title: Codeposition of apolipoprotein A-IV and transthyretin in senile systemic (ATTR) amyloidosis.
    Author: Bergström J, Murphy C, Eulitz M, Weiss DT, Westermark GT, Solomon A, Westermark P.
    Journal: Biochem Biophys Res Commun; 2001 Jul 27; 285(4):903-8. PubMed ID: 11467836.
    Abstract:
    Protein material was extracted from amyloid-rich sections of formalin-fixed and paraffin-embedded heart tissue from an individual with senile systemic amyloidosis, known to contain wild-type transthyretin as major amyloid fibril protein. Amino acid sequence analysis of tryptic peptides of this material revealed in addition to transthyretin sequences, also amino acid sequence corresponding to an N-terminal fragment of apolipoprotein A-IV. In immunohistochemistry, an antiserum to a synthetic apolipoprotein A-IV peptide labeled amyloid specifically. This peptide formed spontaneously amyloid-like fibrils in vitro and enhanced fibril formation from wild-type transthyretin. We conclude that several apolipoproteins, including apolipoprotein A-IV, may be important minor amyloid constituents, promoting fibril formation.
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