http://www.cnr.it/ontology/cnr/individuo/prodotto/ID205201
Analysis of the haptoglobin binding region on the apolipoprotein A-I-derived P2a peptide (Articolo in rivista)
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- Analysis of the haptoglobin binding region on the apolipoprotein A-I-derived P2a peptide (Articolo in rivista) (literal)
- Anno
- 2013-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1002/psc.2487 (literal)
- Alternative label
Spagnuolo MS, Di Stasi R, De Rosa L, Maresca B, Cigliano L, D'Andrea LD (2013)
Analysis of the haptoglobin binding region on the apolipoprotein A-I-derived P2a peptide
in Journal of peptide science (Online); John Wiley & Sons, Ltd., Chichester (Regno Unito)
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- Spagnuolo MS, Di Stasi R, De Rosa L, Maresca B, Cigliano L, D'Andrea LD (literal)
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- Scopus (literal)
- ISI Web of Science (WOS) (literal)
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- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Spagnuolo MS: Istituto per il Sistema Produzione Animale in Ambiente Mediterraneo, CNR
Di Stasi R, De Rosa L, D'Andrea LD: Istituto di Biostrutture e Bioimmagini, CNR
Maresca B, Cigliano L: Dipartimento delle Scienze Biologiche, Università di Napoli 'Federico II', (literal)
- Titolo
- Analysis of the haptoglobin binding region on the apolipoprotein A-I-derived P2a peptide (literal)
- Abstract
- Apolipoprotein A-I (ApoA-I) is the main protein component of the high density lipoproteins and it plays an important role in the reverse cholesterol transport. In particular, it stimulates cholesterol efflux from peripheral cells toward liver and activates the enzyme lecithin-cholesterol acyltransferase (LCAT). Haptoglobin (Hpt), a plasma ?(2) -glycoprotein belonging to the family of acute-phase proteins, binds to ApoA-I inhibiting the stimulation of the enzyme LCAT. Previously, we reported that a synthetic peptide, P2a, binds to and displaces Hpt from ApoA-I restoring the LCAT cholesterol esterification activity in the presence of Hpt. Here, we investigate the molecular determinants underlining the interaction between Hpt and P2a peptide. Analysis of truncated P2a analogs showed that P2a sequence can only be slight reduced in length at the N-terminal to preserve the ability of binding to Hpt. Binding assays showed that charged residues are not involved in Hpt recognition; actually, E146A and D157A substitutions increase the binding affinity to Hpt. Biological characterization of the corresponding P2a peptide analogs, Apo146 and Apo157, showed that the two peptides interfere with Hpt binding to HDL and are more effective than P2a peptide in rescue LCAT activity from Hpt inhibition. This result suggests novel hints to design peptides with anti-atherogenic activity. (literal)
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