Enhanced detection of ATTR amyloid using a nanofibril-based assayShow others and affiliations
2021 (English)In: Amyloid: Journal of Protein Folding Disorders, ISSN 1350-6129, E-ISSN 1744-2818, Vol. 28, no 3, p. 158-167Article in journal (Refereed) Published
Abstract [en]
More than 30 proteins and peptides have been found to form amyloid fibrils in human diseases. Fibrils formed by transthyretin (TTR) are associated with ATTR amyloidosis, affecting many vital organs, including the heart and peripheral nervous system. Congo red staining is the gold standard method for detection of amyloid deposits in tissue. However, Congo red staining and amyloid typing methods such as immunofluorescence labelling are limited to relatively large deposits. Detection of small ATTR deposits present at an early stage of the disease could enable timely treatment and prevent severe tissue damage. In this study, we developed an enhanced ATTR amyloid detection method that uses functionalised protein nanofibrils. Using this method, we achieved sensitive detection of monomeric TTR in a microplate immunoassay and immunofluorescence labelling of ex vivo tissue from two patients containing ATTR aggregates. The system's utility was confirmed on sections from a patient with AA amyloidosis and liver sections from inflamed mouse. These results suggest that the detection system constitutes important new technology for highly sensitive detection of microscopic amounts of ATTR amyloid deposited in tissue.
Place, publisher, year, edition, pages
Taylor and Francis Ltd. , 2021. Vol. 28, no 3, p. 158-167
Keywords [en]
AA amyloid, ATTR amyloid, enhanced detection, functional protein nanofibril, immunoassay, amyloid A protein, monomer, nanofiber, protein aggregate, AA amyloidosis, animal tissue, Article, ATTR amyloidosis, ex vivo study, human, human tissue, immunofluorescence assay, liver tissue, mouse, nonhuman, protein determination
National Category
Biochemistry Molecular Biology
Identifiers
URN: urn:nbn:se:kth:diva-305492DOI: 10.1080/13506129.2021.1886072ISI: 000618006200001PubMedID: 33583280Scopus ID: 2-s2.0-85100839734OAI: oai:DiVA.org:kth-305492DiVA, id: diva2:1615434
Note
QC 20211130
2021-11-302021-11-302025-02-20Bibliographically approved