PuSH - Publikationsserver des Helmholtz Zentrums München: Codeposition of Apolipoprotein A-IV and Transthyretin in Senile Systemic (ATTR) Amyloidosis.

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Bergström, J.* ; Murphy, C.* ; Eulitz, M. ; Weiss, D.T.* ; Westermark, G.T.* ; Solomon, A.* ; Westermark, P.*

Codeposition of Apolipoprotein A-IV and Transthyretin in Senile Systemic (ATTR) Amyloidosis.

Biochem. Biophys. Res. Commun. 285, 903-908 (2001)

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Open Access Green möglich sobald Postprint bei der ZB eingereicht worden ist.

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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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