HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in Web of Science Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Web of Science (1) Citing Articles via Google Scholar Google Scholar Articles by Torricelli, C Articles by Pacini, A Search for Related Content PubMed PubMed Citation Articles by Torricelli, C Articles by Pacini, A

Department of Physiology, University of Siena, via Aldo Moro, 53100 Siena, Italy
¹ Department of Molecular Biology, University of Siena, via Fiorentina 1, 53100 Siena, Italy
² Proteomics and Mass Spectrometry Laboratory, ISPAAM, National Research Council, via Argine 1085, 80147 Napoli, Italy

(Requests for offprints should be addressed to A Pacini, Department of Physiology, Via Aldo Moro-53100 Siena, Italy; Email: pacinia{at}unisi.it)

We have recently demonstrated that human -atrial natriuretic peptide (-hANP), an amyloidogenic peptide responsible for isolated atrial amyloidosis, binds to a dimeric form of apo A-I belonging to small high-density lipoproteins (HDL). This binding phenomenon is considered a protective mechanism since it inhibits or strongly reduces the ANP aggregation process. The observation that plasma exhibits at least four times greater amyloid inhibitory activity than HDL prompted us to determine whether small HDL are the only ANP plasma-binding factors. After incubation of whole plasma with labelled ANP, the macromolecular complexes were subjected to two-dimensional gel electrophoresis followed by autoradiography. The results presented here provide novel evidence of additional binding proteins, in addition to apo A-I dimer, able to bind ANP in vitro and to prevent its aggregation. The mass spectrometry analysis of the radioactive spots identified them as albumin, -1 antitrypsin, orosomucoid and apo A-IV-TTR complex. The putative impact of these findings in the amyloidogenic/antiamyloidogenic peptides network is discussed.