1. An N-terminal pro-atrial natriuretic peptide (NT-proANP) 'aggregation-prone' segment involved in isolated atrial amyloidosis.
- Author
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Louros NN, Iconomidou VA, Tsiolaki PL, Chrysina ED, Baltatzis GE, Patsouris ES, and Hamodrakas SJ
- Subjects
- Amino Acid Sequence, Amyloid chemistry, Amyloid metabolism, Amyloid ultrastructure, Atrial Natriuretic Factor chemistry, Atrial Natriuretic Factor genetics, Congo Red chemistry, Heart Atria metabolism, Heart Atria pathology, Humans, Microscopy, Electron, Molecular Sequence Data, Peptide Fragments chemistry, Peptide Fragments genetics, Protein Precursors chemistry, Protein Precursors genetics, Spectroscopy, Fourier Transform Infrared, X-Ray Diffraction methods, Amyloidosis metabolism, Atrial Natriuretic Factor metabolism, Peptide Fragments metabolism, Protein Precursors metabolism
- Abstract
Isolated atrial amyloidosis (IAA) is a common localized form of amyloid deposition within the atria of the aging heart. The main constituents of amyloid fibrils are atrial natriuretic peptide (ANP) and the N-terminal part of its precursor form (NT-proANP). An 'aggregation-prone' heptapeptide ((114)KLRALLT(120)) was located within the NT-proANP sequence. This peptide self-assembles into amyloid-like fibrils in vitro, as electron microscopy, X-ray fiber diffraction, ATR FT-IR spectroscopy and Congo red staining studies reveal. Consequently, remedies/drugs designed to inhibit the aggregation tendency of this 'aggregation-prone' segment of NT-proANP may assist in prevention/treatment of IAA, congestive heart failure (CHF) or atrial fibrillation (AF)., (Copyright © 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.)
- Published
- 2014
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