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An N-terminal pro-Atrial Natriuretic Peptide (NT-proANP) 'Aggregation-Prone' Segment Involved in Isolated Atrial Amyloidosis.
MedLine Citation:
PMID:  24220659     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
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).
Authors:
Nikolaos N Louros; Vassiliki A Iconomidou; Paraskevi L Tsiolaki; Evangelia D Chrysina; Georgios E Baltatzis; Efstratios S Patsouris; Stavros J Hamodrakas
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2013-11-9
Journal Detail:
Title:  FEBS letters     Volume:  -     ISSN:  1873-3468     ISO Abbreviation:  FEBS Lett.     Publication Date:  2013 Nov 
Date Detail:
Created Date:  2013-11-13     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0155157     Medline TA:  FEBS Lett     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
Copyright © 2013. Published by Elsevier B.V.
Affiliation:
Department of Cell Biology and Biophysics, Faculty of Biology, University of Athens, Panepistimiopolis, Athens 157 01, Greece.
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