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Codeposition of apo...
Codeposition of apolipoprotein A-IV and transthyretin in senile systemic (ATTR) amyloidosis
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Bergström, Joakim (author)
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Murphy, Charles (author)
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Eulitz, Manfred (author)
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Weiss, Deborah (author)
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- Westermark, Gunilla, 1958- (author)
- Linköpings universitet,Hälsouniversitetet,Cellbiologi
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Solomon, Alan (author)
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Westermark, Per (author)
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(creator_code:org_t)
- Elsevier BV, 2001
- 2001
- English.
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In: Biochemical and Biophysical Research Communications - BBRC. - : Elsevier BV. - 0006-291X .- 1090-2104. ; 285:4, s. 903-908
- Related links:
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
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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.
Keyword
- MEDICINE
- MEDICIN
Publication and Content Type
- ref (subject category)
- art (subject category)
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