Antibody recognition of amyloidogenic transthyretin variants in serum of patients with familial amyloidotic polyneuropathy View Full Text


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Article Info

DATE

2000-12-12

AUTHORS

Joana Almeida Palha, Paulo Moreira, Anders Olofsson, Erik Lundgren, Maria João Saraiva

ABSTRACT

Familial amyloidotic polyneuropathy (FAP) is a late-onset inherited disease characterized by the deposition of amyloid fibrils. FAP is associated with mutations on the transthyretin (TTR) gene. A monoclonal antibody, MAb 39-44, reacting with high molecular weight aggregates of TTR but not with tetrameric TTR has recently been generated and characterized. This antibody recognizes a cryptic epitope that is expressed in isolated recombinant amyloidogenic mutants and in ex vivo amyloid. In the present work we show that this amyloid-specific antibody specifically recognizes in a direct enzyme-linked immunoassay (ELISA) plasma TTR from carriers of various mutations associated with FAP, both in asymptomatic individuals and in patients. In contrast, it does not react with plasma TTR from healthy individuals or that from carriers of nonpathogenic mutations. Using the ELISA developed in this study we identified three different TTR mutations in Portuguese patients with neuropathy of unknown cause, later shown to have amyloid tissue deposition. This antibody recognizes conformations that express cryptic epitopes shared by amyloidogenic TTR variants associated with FAP, not present among nonpathogenic TTR molecules. This antibody will contribute to further identify and characterize intermediates of the amyloidogenic cascade. In addition, it will also be useful for screening amyloidogenic TTR mutations in patients with neuropathy of unknown cause, prior to precise molecular diagnosis using protein and/or DNA analysis. More... »

PAGES

703-707

Journal

TITLE

Journal of Molecular Medicine

ISSUE

12

VOLUME

78

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1007/s001090000163

    DOI

    http://dx.doi.org/10.1007/s001090000163

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1044408435

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/11434723


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