An N-terminal pro-atrial natriuretic peptide (NT-proANP) 'aggregation-prone' segment involved in isolated atrial amyloidosis.
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).
Department of Cell Biology and Biophysics, Faculty of Biology, University of Athens, Panepistimiopolis, Athens 157 01, Greece.
Nikolaos N
NN
Louros
Department of Cell Biology and Biophysics, Faculty of Biology, University of Athens, Panepistimiopolis, Athens 157 01, Greece.
Vassiliki A
VA
Iconomidou
Department of Cell Biology and Biophysics, Faculty of Biology, University of Athens, Panepistimiopolis, Athens 157 01, Greece.
Paraskevi L
PL
Tsiolaki
Institute of Biology, Medicinal Chemistry and Biotechnology, National Hellenic Research Foundation, 48 Vassileos Constantinou Avenue, Athens 116 35, Greece.
Evangelia D
ED
Chrysina
1st Department of Pathology, Medical School, University of Athens, 75 Mikras Assias, Goudi 115 27, Greece.
Georgios E
GE
Baltatzis
1st Department of Pathology, Medical School, University of Athens, 75 Mikras Assias, Goudi 115 27, Greece.
Efstratios S
ES
Patsouris
Department of Cell Biology and Biophysics, Faculty of Biology, University of Athens, Panepistimiopolis, Athens 157 01, Greece. Electronic address: shamodr@biol.uoa.gr.
Stavros J
SJ
Hamodrakas
D000595:Amino Acid Sequence; D000682:Amyloid / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure; D000686:Amyloidosis / Q000378:metabolism*; D009320:Atrial Natriuretic Factor / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D003224:Congo Red / Q000737:chemistry; D006325:Heart Atria / Q000378:metabolism / Q000473:pathology; D006801:Humans; D008854:Microscopy, Electron; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D011498:Protein Precursors / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D017550:Spectroscopy, Fourier Transform Infrared; D014961:X-Ray Diffraction / Q000379:methods
D000682:Amyloid; D010446:Peptide Fragments; D011498:Protein Precursors; D003224:Congo Red; D009320:Atrial Natriuretic Factor
AF; ANP; ATR FT-IR spectroscopy; Amyloid fibril; BNP; CHF; Cardiac amyloidose; IAA; Isolated atrial amyloidosis (IAA); N-terminal pro-atrial natriuretic peptide; N-terminal pro-atrial natriuretic peptide (NT-proANP); NT-proANP; Natriuretic peptide; SSA; TTR; atrial fibrosis; atrial natriuretic peptide; attenuated total reflectance Fourier-transform spectroscopy; brain natriuretic peptide; cGMP; congestive heart failure; cyclic guanosine monophosphate; isolated atrial amyloidosis; senile systemic amyloidosis; transthyretin