دورية أكاديمية
Clinical ApoA-IV amyloid is associated with fibrillogenic signal sequence
| العنوان: | Clinical ApoA-IV amyloid is associated with fibrillogenic signal sequence |
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| المؤلفون: | Canetti D., Nocerino P., Rendell N. B., Botcher N., Gilbertson J. A., Blanco A., Rowczenio D., Morelli A., Mangione P. P., Corazza A., Verona G., Giorgetti S., Marchese L., Westermark P., Hawkins P. N., Gillmore J. D., Bellotti V., Taylor G. W. |
| المساهمون: | Canetti, D., Nocerino, P., Rendell, N. B., Botcher, N., Gilbertson, J. A., Blanco, A., Rowczenio, D., Morelli, A., Mangione, P. P., Corazza, A., Verona, G., Giorgetti, S., Marchese, L., Westermark, P., Hawkins, P. N., Gillmore, J. D., Bellotti, V., Taylor, G. W. |
| سنة النشر: | 2021 |
| المجموعة: | IRIS UNIPV (Università degli studi di Pavia) |
| مصطلحات موضوعية: | amyloid proteomic, ApoA-IV amyloidosi, ApoA-IV sequence coverage, ApoA-IV signal-containing peptide, fibrillogenic ApoA-IV signal-containing peptide, targeted mass spectrometry in serum, Aged, Amyloidosi, Female, Human, Male, Plaque, Amyloid, Apolipoproteins A, Protein Sorting Signals |
| الوصف: | Apolipoprotein A-IV amyloidosis is an uncommon form of the disease normally resulting in renal and cardiac dysfunction. ApoA-IV amyloidosis was identified in 16 patients attending the National Amyloidosis Centre and in eight clinical samples received for histology review. Unexpectedly, proteomics identified the presence of ApoA-IV signal sequence residues (p.18-43 to p.20-43) in 16/24 trypsin-digested amyloid deposits but in only 1/266 non-ApoA-IV amyloid samples examined. These additional signal residues were also detected in the cardiac sample from the Swedish patient in which ApoA-IV amyloid was first described, and in plasma from a single cardiac ApoA-IV amyloidosis patient. The most common signal-containing peptide observed in ApoA-IV amyloid, p.20-43, and to a far lesser extent the N-terminal peptide, p.21-43, were fibrillogenic in vitro at physiological pH, generating Congo red-positive fibrils. The addition of a single signal-derived alanine residue to the N-terminus has resulted in markedly increased fibrillogenesis. If this effect translates to the mature circulating protein in vivo, then the presence of signal may result in preferential deposition as amyloid, perhaps acting as seed for the main circulating native form of the protein; it may also influence other ApoA-IV-associated pathologies. © 2021 The Authors. The Journal of Pathology published by John Wiley & Sons, Ltd. on behalf of The Pathological Society of Great Britain and Ireland. |
| نوع الوثيقة: | article in journal/newspaper |
| اللغة: | English |
| العلاقة: | info:eu-repo/semantics/altIdentifier/pmid/34331462; info:eu-repo/semantics/altIdentifier/wos/WOS:000689701500001; volume:255; issue:3; firstpage:311; lastpage:318; numberofpages:8; journal:JOURNAL OF PATHOLOGY; http://hdl.handle.net/11571/1450348Test; info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-85113448489 |
| DOI: | 10.1002/path.5770 |
| الإتاحة: | https://doi.org/10.1002/path.5770Test http://hdl.handle.net/11571/1450348Test |
| رقم الانضمام: | edsbas.82537420 |
| قاعدة البيانات: | BASE |
| DOI: | 10.1002/path.5770 |
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