Codeposition of apolipoprotein A-IV and transthyretin in senile systemic (ATTR) amyloidosis

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.

Murphy, Charles (author)
Eulitz, Manfred (author)
Weiss, Deborah (author)
Westermark, Gunilla,1958-Linköpings universitet,Hälsouniversitetet,Cellbiologi(Swepub:liu)gunwe13 (author)
Solomon, Alan (author)
Westermark, Per (author)
Linköpings universitetHälsouniversitetet (creator_code:org_t)

In:Biochemical and Biophysical Research Communications - BBRC: Elsevier BV285:4, s. 903-9080006-291X1090-2104

By the author/editor: Bergström, Joaki ...; Murphy, Charles; Eulitz, Manfred; Weiss, Deborah; Westermark, Guni ...; Solomon, Alan; show more...; Westermark, Per; show less...

Kungliga biblioteket hanterar dina personuppgifter i enlighet med EU:s dataskyddsförordning (2018), GDPR. Läs mer om hur det funkar här.
Så här hanterar KB dina uppgifter vid användning av denna tjänst.