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Codeposition of apolipoprotein A-IV and transthyretin in senile systemic (ATTR) amyloidosis
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2001 (English)In: Biochemical and Biophysical Research Communications - BBRC, ISSN 0006-291X, E-ISSN 1090-2104, Vol. 285, no 4, 903-908 p.Article in journal (Refereed) Published
Abstract [en]

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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2001. Vol. 285, no 4, 903-908 p.
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Medical and Health Sciences
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URN: urn:nbn:se:liu:diva-25455DOI: 10.1006/bbrc.2001.5260Local ID: 9901OAI: oai:DiVA.org:liu-25455DiVA: diva2:245784
Available from: 2009-10-07 Created: 2009-10-07 Last updated: 2017-12-13

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Westermark, Gunilla

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