Analysis of the haptoglobin binding region on the apolipoprotein A-I-derived P2a peptide (376 views)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2013 Apr; 19(4): 220-226.
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Paper type: Journal Article,
Impact factor: 1.862, 5-year impact factor: 1.715
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84875594325&partnerID=40&md5=fa7490af0f41d4e6b5c89a039660eab1
Keywords: Apoa-I, Haptoglobin, Helix Conformation, Lcat, Apolipoprotein 141 161, Apolipoprotein 144 164, Apolipoprotein 146 164, Cardiovascular Agent, High Density Lipoprotein, Phosphatidylcholine Sterol Acyltransferase, Protein P 2a, Synthetic Peptide, Unclassified Drug, Amino Acid Sequence, Amino Terminal Sequence, Article, Binding Affinity, Controlled Study, Drug Binding Site, Drug Design, Drug Protein Binding, Drug Structure, Enzyme Activity, Priority Journal, Protein Analysis, Protein Protein Interaction, Protein Structure, Amino Acid Substitution, Anti-Bacterial Agents, Apolipoprotein A-I, Cholesterol, Female, Humans, Phosphatidylcholine-Sterol O-Acyltransferase,
Affiliations:
*** IBB - CNR ***
Istituto per il Sistema Produzione Animale in Ambiente Mediterraneo, CNR, via Argine 1085, Napoli, Italy
Istituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 16, Napoli, Italy
Dipartimento delle Scienze Biologiche, Università di Napoli 'Federico II', Via Mezzocannone 8, Napoli, Italy
References:
Sorci-Thomas, M.G., Thomas, M.J., The effects of altered apolipoprotein A-I structure on plasma HDL concentration (2002) Trends Cardiovasc. Med., 12, pp. 121-12
Davidson, W.S., Thompson, T.B., The structure of apolipoprotein A-I in high density lipoproteins (2007) J. Biol. Chem., 282, pp. 22249-22253
Thomas, M.J., Bhat, S., Sorci-Thomas, M.G., Three-dimensional models of HDL apoA-I: implications for its assembly and function (2008) J. Lipid Res., 49, pp. 1875-1883
Wu, Z., Gogonea, V., Lee, X., Wagner, M.A., Li, X.M., Huang, Y., Undurti, A., Hazen, S.L., Double superhelix model of high density lipoprotein (2009) J. Biol. Chem., 284, pp. 36605-36619
Mei, X., Atkinson, D., Crystal structure of C-terminal truncated apolipoprotein A-I reveals the assembly of high density lipoprotein (HDL) by dimerization (2011) J. Biol. Chem., 286, pp. 38570-38582
Huang, R., Silva, R.A., Jerome, W.G., Kontush, A., Chapman, M.J., Curtiss, L.K., Hodges, T.J., Davidson, W.S., Apolipoprotein A-I structural organization in high-density lipoproteins isolated from human plasma (2011) Nat. Struct. Mol. Biol., 18, pp. 416-422
Sevugan Chetty, P., Mayne, L., Kan, Z.Y., Lund-Katz, S., Englander, S.W., Phillips, M.C., Apolipoprotein A-I helical structure and stability in discoidal high-density lipoprotein (HDL) particles by hydrogen exchange and mass spectrometry (2012) Proc. Natl. Acad. Sci. U.S.A., 109, pp. 11687-11692
Balestrieri, M., Cigliano, L., De Simone, M.L., Dale, B., Abrescia, P., Haptoglobin inhibits lecithin-cholesterol-acyltrasferase in human ovarian follicular fluid (2001) Mol. Reprod. Dev., 59, pp. 186-191
Spagnuolo, M.S., Cigliano, L., Abrescia, P., The binding of haptoglobin to apolipoprotein A-I: influence of hemoglobin and concanavalin A (2003) Biol. Chem., 384, pp. 1593-1596
Giblett, E.R., The haptoglobin system (1968) Ser. Haematol., 1, pp. 3-20
Nagel, R.L., Gibson, Q.H., The binding of Hemoglobin to Haptoglobin and its relation to subunit dissociation of Hemoglobin (1971) J. Biol. Chem., 246, pp. 69-73
Langlois, M.R., Delanghe, J.R., Biological and clinical significance of haptoglobin polymorphism in humans (1996) Clin. Chem., 42, pp. 1589-1600
Kristiansen, M., Graversen, J.H., Jacobsen, C., Sonne, O., Hoffman, H.J., Law, S.K., Moestrup, S.K., Identification of the haemoglobin scavenger receptor (2001) Nature, 409, pp. 198-201
Gutteridge, J.M.C., The antioxidant activity of haptoglobin towards haemoglobin-stimulated lipid peroxidation (1987) Biochim. Biophys. Acta, 917, pp. 219-223
Alayash, A.I., Redox biology of blood (2004) Antioxid. Redox Signal., 6, pp. 941-949
Salvatore, A., Cigliano, L., Bucci, E.M., Corpillo, D., Velasco, S., Carlucci, A., Pedone, C., Abrescia, P., Haptoglobin binding to apolipoprotein A-I prevents damage from hydroxyl radicals on its stimulatory activity of the enzyme lecithin-cholesterol acyl-transferase (2007) Biochemistry, 46, pp. 1158-1168
Cigliano, L., Pugliese, C.R., Spagnuolo, M.S., Palumbo, R., Abrescia, P., Haptoglobin binds the antiatherogenic protein apolipoprotein E - impairment of apolipoprotein E stimulation of both lecithin:cholesterol acyltransferase activity and cholesterol uptake by hepatocytes (2009) FEBS J., 276, pp. 6158-6171
Braeckman, L., De Bacquer, D., Delanghe, J., Claeys, L., De Backer, G., Associations between haptoglobin polymorphism, lipids, lipoproteins and inflammatory variables (1999) Atherosclerosis, 143, pp. 383-388
De Bacquer, D., De Backer, G., Langlois, M., Delanghe, J., Kesteloot, H., Kornitzer, M., Haptoglobin polymorphism as a risk factor for coronary heart disease mortality (2001) Atherosclerosis, 157, pp. 161-166
Matuszek, M.A., Aristoteli, L.P., Bannon, P.G., Hendel, P.N., Hughes, C.F., Jessup, W., Dean, R.T., Kritharides, L., Haptoglobin elutes from human atherosclerotic coronary arteries--a potential marker of arterial pathology (2003) Atherosclerosis, 168, pp. 389-396
Bucci, M., Cigliano, L., Vellecco, V., D'Andrea, L.D., Ziaco, B., Rossi, A., Sautebin, L., Cirino, G., Apolipoprotein A-I (ApoA-I) mimetic peptide P2a by restoring cholesterol esterification unmasks ApoA-I anti-inflammatory endogenous activity in vivo (2012) J. Pharmacol. Exp. Ther., 340, pp. 716-722
Bradford, M.M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding (1976) Anal. Biochem., 72, pp. 248-254
Cigliano, L., Spagnuolo, M.S., Abrescia, P., Quantitative variations of the isoforms in haptoglobin 1-2 and 2-2 individual phenotypes (2003) Arch. Biochem. Biophys., 416, pp. 227-237
Cigliano, L., D'Andrea, L.D., Maresca, B., Serino, M., Carlucci, A., Salvatore, A., Spagnuolo, M.S., Abrescia, P., Relevance of the amino acid conversions L144R (Zaragoza) and L159P (Zavalla) in the apolipoprotein A-I binding site for haptoglobin (2008) Biol. Chem., 389, pp. 1421-1426
Porta, A., Cassano, E., Balestrieri, M., Bianco, M., Picone, R., De Stefano, C., Abrescia, P., Haptoglobin transport into human ovarian follicles and its binding to apolipoprotein A-I (1999) Zygote, 7, pp. 67-77
Chen, C.-H., Albers, J.J., Characterization of proteoliposomes containing apoprotein A-I: a new substrate for the measurement of lecithin: cholesterol acyltransferase activity (1982) J. Lipid Res., 23, pp. 680-691
DeGrado, W.F., Summa, C.M., Pavone, V., Nastri, F., Lombardi, A., De novo design and structural characterization of proteins and metalloproteins (1999) Annu. Rev. Biochem., 68, pp. 779-819
Luo, P., Baldwin, R.L., Mechanism of helix induction by trifluoroethanol: a framework for extrapolating the helix-forming properties of peptides from trifluoroethanol/water mixtures back to water (1997) Biochemistry, 36, pp. 8413-8421
Rohl, C.A., Chakrabartty, A., Baldwin, R.L., Helix propagation and N-cap propensities of the amino acids measured in alanine-based peptides in 40 volume percent trifluoroethanol (1996) Protein Sci., 5, pp. 2623-2637
Vuilleumier, S., Mutter, M., Synthetic peptide and template-assembled synthetic protein models of the hen egg white lysozyme 87-97 helix: importance of a protein-like framework for conformational stability in a short peptide sequence (1993) Biopolymers, 33, pp. 389-400
Sorci-Thomas, M. G., Thomas, M. J., The effects of altered apolipoprotein A-I structure on plasma HDL concentration (2002) Trends Cardiovasc. Med., 12, pp. 121-12
Davidson, W. S., Thompson, T. B., The structure of apolipoprotein A-I in high density lipoproteins (2007) J. Biol. Chem., 282, pp. 22249-22253
Thomas, M. J., Bhat, S., Sorci-Thomas, M. G., Three-dimensional models of HDL apoA-I: implications for its assembly and function (2008) J. Lipid Res., 49, pp. 1875-1883
Spagnuolo, M. S., Cigliano, L., Abrescia, P., The binding of haptoglobin to apolipoprotein A-I: influence of hemoglobin and concanavalin A (2003) Biol. Chem., 384, pp. 1593-1596
Giblett, E. R., The haptoglobin system (1968) Ser. Haematol., 1, pp. 3-20
Nagel, R. L., Gibson, Q. H., The binding of Hemoglobin to Haptoglobin and its relation to subunit dissociation of Hemoglobin (1971) J. Biol. Chem., 246, pp. 69-73
Langlois, M. R., Delanghe, J. R., Biological and clinical significance of haptoglobin polymorphism in humans (1996) Clin. Chem., 42, pp. 1589-1600
Gutteridge, J. M. C., The antioxidant activity of haptoglobin towards haemoglobin-stimulated lipid peroxidation (1987) Biochim. Biophys. Acta, 917, pp. 219-223
Alayash, A. I., Redox biology of blood (2004) Antioxid. Redox Signal., 6, pp. 941-949
Matuszek, M. A., Aristoteli, L. P., Bannon, P. G., Hendel, P. N., Hughes, C. F., Jessup, W., Dean, R. T., Kritharides, L., Haptoglobin elutes from human atherosclerotic coronary arteries--a potential marker of arterial pathology (2003) Atherosclerosis, 168, pp. 389-396
Bradford, M. M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding (1976) Anal. Biochem., 72, pp. 248-254
Chen, C. -H., Albers, J. J., Characterization of proteoliposomes containing apoprotein A-I: a new substrate for the measurement of lecithin: cholesterol acyltransferase activity (1982) J. Lipid Res., 23, pp. 680-691
DeGrado, W. F., Summa, C. M., Pavone, V., Nastri, F., Lombardi, A., De novo design and structural characterization of proteins and metalloproteins (1999) Annu. Rev. Biochem., 68, pp. 779-819
Rohl, C. A., Chakrabartty, A., Baldwin, R. L., Helix propagation and N-cap propensities of the amino acids measured in alanine-based peptides in 40 volume percent trifluoroethanol (1996) Protein Sci., 5, pp. 2623-2637
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2013 Apr; 19(4): 220-226.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 1.862, 5-year impact factor: 1.715
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84875594325&partnerID=40&md5=fa7490af0f41d4e6b5c89a039660eab1
Keywords: Apoa-I, Haptoglobin, Helix Conformation, Lcat, Apolipoprotein 141 161, Apolipoprotein 144 164, Apolipoprotein 146 164, Cardiovascular Agent, High Density Lipoprotein, Phosphatidylcholine Sterol Acyltransferase, Protein P 2a, Synthetic Peptide, Unclassified Drug, Amino Acid Sequence, Amino Terminal Sequence, Article, Binding Affinity, Controlled Study, Drug Binding Site, Drug Design, Drug Protein Binding, Drug Structure, Enzyme Activity, Priority Journal, Protein Analysis, Protein Protein Interaction, Protein Structure, Amino Acid Substitution, Anti-Bacterial Agents, Apolipoprotein A-I, Cholesterol, Female, Humans, Phosphatidylcholine-Sterol O-Acyltransferase,
Affiliations:
*** IBB - CNR ***
Istituto per il Sistema Produzione Animale in Ambiente Mediterraneo, CNR, via Argine 1085, Napoli, Italy
Istituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 16, Napoli, Italy
Dipartimento delle Scienze Biologiche, Università di Napoli 'Federico II', Via Mezzocannone 8, Napoli, Italy
References:
Sorci-Thomas, M.G., Thomas, M.J., The effects of altered apolipoprotein A-I structure on plasma HDL concentration (2002) Trends Cardiovasc. Med., 12, pp. 121-12
Davidson, W.S., Thompson, T.B., The structure of apolipoprotein A-I in high density lipoproteins (2007) J. Biol. Chem., 282, pp. 22249-22253
Thomas, M.J., Bhat, S., Sorci-Thomas, M.G., Three-dimensional models of HDL apoA-I: implications for its assembly and function (2008) J. Lipid Res., 49, pp. 1875-1883
Wu, Z., Gogonea, V., Lee, X., Wagner, M.A., Li, X.M., Huang, Y., Undurti, A., Hazen, S.L., Double superhelix model of high density lipoprotein (2009) J. Biol. Chem., 284, pp. 36605-36619
Mei, X., Atkinson, D., Crystal structure of C-terminal truncated apolipoprotein A-I reveals the assembly of high density lipoprotein (HDL) by dimerization (2011) J. Biol. Chem., 286, pp. 38570-38582
Huang, R., Silva, R.A., Jerome, W.G., Kontush, A., Chapman, M.J., Curtiss, L.K., Hodges, T.J., Davidson, W.S., Apolipoprotein A-I structural organization in high-density lipoproteins isolated from human plasma (2011) Nat. Struct. Mol. Biol., 18, pp. 416-422
Sevugan Chetty, P., Mayne, L., Kan, Z.Y., Lund-Katz, S., Englander, S.W., Phillips, M.C., Apolipoprotein A-I helical structure and stability in discoidal high-density lipoprotein (HDL) particles by hydrogen exchange and mass spectrometry (2012) Proc. Natl. Acad. Sci. U.S.A., 109, pp. 11687-11692
Balestrieri, M., Cigliano, L., De Simone, M.L., Dale, B., Abrescia, P., Haptoglobin inhibits lecithin-cholesterol-acyltrasferase in human ovarian follicular fluid (2001) Mol. Reprod. Dev., 59, pp. 186-191
Spagnuolo, M.S., Cigliano, L., Abrescia, P., The binding of haptoglobin to apolipoprotein A-I: influence of hemoglobin and concanavalin A (2003) Biol. Chem., 384, pp. 1593-1596
Giblett, E.R., The haptoglobin system (1968) Ser. Haematol., 1, pp. 3-20
Nagel, R.L., Gibson, Q.H., The binding of Hemoglobin to Haptoglobin and its relation to subunit dissociation of Hemoglobin (1971) J. Biol. Chem., 246, pp. 69-73
Langlois, M.R., Delanghe, J.R., Biological and clinical significance of haptoglobin polymorphism in humans (1996) Clin. Chem., 42, pp. 1589-1600
Kristiansen, M., Graversen, J.H., Jacobsen, C., Sonne, O., Hoffman, H.J., Law, S.K., Moestrup, S.K., Identification of the haemoglobin scavenger receptor (2001) Nature, 409, pp. 198-201
Gutteridge, J.M.C., The antioxidant activity of haptoglobin towards haemoglobin-stimulated lipid peroxidation (1987) Biochim. Biophys. Acta, 917, pp. 219-223
Alayash, A.I., Redox biology of blood (2004) Antioxid. Redox Signal., 6, pp. 941-949
Salvatore, A., Cigliano, L., Bucci, E.M., Corpillo, D., Velasco, S., Carlucci, A., Pedone, C., Abrescia, P., Haptoglobin binding to apolipoprotein A-I prevents damage from hydroxyl radicals on its stimulatory activity of the enzyme lecithin-cholesterol acyl-transferase (2007) Biochemistry, 46, pp. 1158-1168
Cigliano, L., Pugliese, C.R., Spagnuolo, M.S., Palumbo, R., Abrescia, P., Haptoglobin binds the antiatherogenic protein apolipoprotein E - impairment of apolipoprotein E stimulation of both lecithin:cholesterol acyltransferase activity and cholesterol uptake by hepatocytes (2009) FEBS J., 276, pp. 6158-6171
Braeckman, L., De Bacquer, D., Delanghe, J., Claeys, L., De Backer, G., Associations between haptoglobin polymorphism, lipids, lipoproteins and inflammatory variables (1999) Atherosclerosis, 143, pp. 383-388
De Bacquer, D., De Backer, G., Langlois, M., Delanghe, J., Kesteloot, H., Kornitzer, M., Haptoglobin polymorphism as a risk factor for coronary heart disease mortality (2001) Atherosclerosis, 157, pp. 161-166
Matuszek, M.A., Aristoteli, L.P., Bannon, P.G., Hendel, P.N., Hughes, C.F., Jessup, W., Dean, R.T., Kritharides, L., Haptoglobin elutes from human atherosclerotic coronary arteries--a potential marker of arterial pathology (2003) Atherosclerosis, 168, pp. 389-396
Bucci, M., Cigliano, L., Vellecco, V., D'Andrea, L.D., Ziaco, B., Rossi, A., Sautebin, L., Cirino, G., Apolipoprotein A-I (ApoA-I) mimetic peptide P2a by restoring cholesterol esterification unmasks ApoA-I anti-inflammatory endogenous activity in vivo (2012) J. Pharmacol. Exp. Ther., 340, pp. 716-722
Bradford, M.M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding (1976) Anal. Biochem., 72, pp. 248-254
Cigliano, L., Spagnuolo, M.S., Abrescia, P., Quantitative variations of the isoforms in haptoglobin 1-2 and 2-2 individual phenotypes (2003) Arch. Biochem. Biophys., 416, pp. 227-237
Cigliano, L., D'Andrea, L.D., Maresca, B., Serino, M., Carlucci, A., Salvatore, A., Spagnuolo, M.S., Abrescia, P., Relevance of the amino acid conversions L144R (Zaragoza) and L159P (Zavalla) in the apolipoprotein A-I binding site for haptoglobin (2008) Biol. Chem., 389, pp. 1421-1426
Porta, A., Cassano, E., Balestrieri, M., Bianco, M., Picone, R., De Stefano, C., Abrescia, P., Haptoglobin transport into human ovarian follicles and its binding to apolipoprotein A-I (1999) Zygote, 7, pp. 67-77
Chen, C.-H., Albers, J.J., Characterization of proteoliposomes containing apoprotein A-I: a new substrate for the measurement of lecithin: cholesterol acyltransferase activity (1982) J. Lipid Res., 23, pp. 680-691
DeGrado, W.F., Summa, C.M., Pavone, V., Nastri, F., Lombardi, A., De novo design and structural characterization of proteins and metalloproteins (1999) Annu. Rev. Biochem., 68, pp. 779-819
Luo, P., Baldwin, R.L., Mechanism of helix induction by trifluoroethanol: a framework for extrapolating the helix-forming properties of peptides from trifluoroethanol/water mixtures back to water (1997) Biochemistry, 36, pp. 8413-8421
Rohl, C.A., Chakrabartty, A., Baldwin, R.L., Helix propagation and N-cap propensities of the amino acids measured in alanine-based peptides in 40 volume percent trifluoroethanol (1996) Protein Sci., 5, pp. 2623-2637
Vuilleumier, S., Mutter, M., Synthetic peptide and template-assembled synthetic protein models of the hen egg white lysozyme 87-97 helix: importance of a protein-like framework for conformational stability in a short peptide sequence (1993) Biopolymers, 33, pp. 389-400
Sorci-Thomas, M. G., Thomas, M. J., The effects of altered apolipoprotein A-I structure on plasma HDL concentration (2002) Trends Cardiovasc. Med., 12, pp. 121-12
Davidson, W. S., Thompson, T. B., The structure of apolipoprotein A-I in high density lipoproteins (2007) J. Biol. Chem., 282, pp. 22249-22253
Thomas, M. J., Bhat, S., Sorci-Thomas, M. G., Three-dimensional models of HDL apoA-I: implications for its assembly and function (2008) J. Lipid Res., 49, pp. 1875-1883
Spagnuolo, M. S., Cigliano, L., Abrescia, P., The binding of haptoglobin to apolipoprotein A-I: influence of hemoglobin and concanavalin A (2003) Biol. Chem., 384, pp. 1593-1596
Giblett, E. R., The haptoglobin system (1968) Ser. Haematol., 1, pp. 3-20
Nagel, R. L., Gibson, Q. H., The binding of Hemoglobin to Haptoglobin and its relation to subunit dissociation of Hemoglobin (1971) J. Biol. Chem., 246, pp. 69-73
Langlois, M. R., Delanghe, J. R., Biological and clinical significance of haptoglobin polymorphism in humans (1996) Clin. Chem., 42, pp. 1589-1600
Gutteridge, J. M. C., The antioxidant activity of haptoglobin towards haemoglobin-stimulated lipid peroxidation (1987) Biochim. Biophys. Acta, 917, pp. 219-223
Alayash, A. I., Redox biology of blood (2004) Antioxid. Redox Signal., 6, pp. 941-949
Matuszek, M. A., Aristoteli, L. P., Bannon, P. G., Hendel, P. N., Hughes, C. F., Jessup, W., Dean, R. T., Kritharides, L., Haptoglobin elutes from human atherosclerotic coronary arteries--a potential marker of arterial pathology (2003) Atherosclerosis, 168, pp. 389-396
Bradford, M. M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding (1976) Anal. Biochem., 72, pp. 248-254
Chen, C. -H., Albers, J. J., Characterization of proteoliposomes containing apoprotein A-I: a new substrate for the measurement of lecithin: cholesterol acyltransferase activity (1982) J. Lipid Res., 23, pp. 680-691
DeGrado, W. F., Summa, C. M., Pavone, V., Nastri, F., Lombardi, A., De novo design and structural characterization of proteins and metalloproteins (1999) Annu. Rev. Biochem., 68, pp. 779-819
Rohl, C. A., Chakrabartty, A., Baldwin, R. L., Helix propagation and N-cap propensities of the amino acids measured in alanine-based peptides in 40 volume percent trifluoroethanol (1996) Protein Sci., 5, pp. 2623-2637
Analysis of the haptoglobin binding region on the apolipoprotein A-I-derived P2a peptide
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. Copyright (c) 2013 European Peptide Society and John Wiley & Sons, Ltd.
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. Copyright (c) 2013 European Peptide Society and John Wiley & Sons, Ltd.
Analysis of the haptoglobin binding region on the apolipoprotein A-I-derived P2a peptide
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Analysis of the haptoglobin binding region on the apolipoprotein A-I-derived P2a peptide
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Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2005 Jan 14; 280(2): 1193-1198.
Impact Factor: 5.854
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Oliva R, Falcigno L, D'Auria G, Dettin M, Scarinci C, Pasquato A, Di Bello C, Paolillo L
* Structural investigation of the HIV-1 envelope glycoprotein gp160 cleavage site, 2: relevance of an N-terminal helix (360 views)
Chembiochem (ISSN: 1439-4227, 1439-7633, 1439-7633electronic), 2003 Aug 4; 4(8): 727-733.
Impact Factor: 2.92
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* Structure and biological activity of a conformational constrained apolipoprotein A-I-derived helical peptide targeting the protein haptoglobin (401 views)
Rsc Adv (ISSN: 2046-2069), 2014; 4(93): 51353-51361.
Impact Factor: 3.84
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Bucci M, Cigliano L, Vellecco V, D'Andrea LD, Ziaco B, Rossi A, Sautebin L, Carlucci A, Abrescia P, Pedone C, Ianaro A, Cirino G
* Apolipoprotein A-I (ApoA-I) mimetic peptide P2a by restoring cholesterol esterification unmasks ApoA-I anti-inflammatory endogenous activity in vivo (461 views)
J Pharmacol Exp Ther (ISSN: 1521-0103, 0022-3565), 2012 Mar; 340(3): 716-722.
Impact Factor: 3.891
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Cigliano L, Pugliese CR, Spagnuolo MS, Palumbo R, Abrescia P
* Haptoglobin binds the antiatherogenic protein apolipoprotein e - Impairment of apolipoprotein e stimulation of both lecithin: Cholesterol acyltransferase activity and cholesterol uptake by hepatocytes (398 views)
Febs J (ISSN: 1742-464x), 2009 Nov; 276(21): 6158-6171.
Impact Factor: 3.042
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Cigliano L, Pugliese CR, Spagnuolo MS, Palumbo R, Abrescia P
* Haptoglobin Binds The Anti-Atherogenic Protein Apolipoprotein E: Impairment Of The Apolipoprotein E Stimulation On Both The Enzyme Lecithin-Cholesterol Acyl-Transferase Activity And The Cholesterol Uptake By Hepatocytes (274 views)
Febs J, 2009; 276: 6158-6171.
Impact Factor: 3.986
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Cigliano L, D'Andrea LD, Maresca B, Serino M, Carlucci A, Salvatore A, Spagnuolo MS, Scigliuolo G, Pedone C, Abrescia P
* Relevance of the amino acid conversions L144R (Zaragoza) and L159P (Zavalla) in the apolipoprotein A-I binding site for haptoglobin (393 views)
Biol Chem Biological Chemistry (ISSN: 1431-6730, 1437-4315), 2008 Nov; 389(11): 1421-1426.
Impact Factor: 3.035
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Cigliano L, Maresca B, Salvatore A, Nino M, Monfrecola G, Ayala F, Carlucci A, Pugliese RC, Pedone C, Abrescia P
* Haptoglobin from psoriatic patients exhibits decreased activity in binding haemoglobin and inhibiting lecithin-cholesterol acyltransferase activity (417 views)
Journal Of The European Academy Of Dermatology And Venereology (ISSN: 1468-3083, 0926-9959), 2008 Apr; 22(4): 417-425.
Impact Factor: 2.276
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Salvatore A, Cigliano L, Bucci EM, Corpillo D, Velasco S, Carlucci A, Pedone C, Abrescia P
* Haptoglobin binding to apolipoprotein A-I prevents damage from hydroxyl radicals on its stimulatory activity of the enzyme lecithin-cholesterol acyl-transferase (495 views)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2007 Oct 2; 46(39): 11158-11168.
Impact Factor: 3.368
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Spagnuolo MS, Cigliano L, D'Andrea LD, Pedone C, Abrescia P
* Assignment of the binding site for haptoglobin on apolipoprotein A-I (496 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2005 Jan 14; 280(2): 1193-1198.
Impact Factor: 5.854
View Export to BibTeX Export to EndNote
Oliva R, Falcigno L, D'Auria G, Dettin M, Scarinci C, Pasquato A, Di Bello C, Paolillo L
* Structural investigation of the HIV-1 envelope glycoprotein gp160 cleavage site, 2: relevance of an N-terminal helix (360 views)
Chembiochem (ISSN: 1439-4227, 1439-7633, 1439-7633electronic), 2003 Aug 4; 4(8): 727-733.
Impact Factor: 2.92
View Export to BibTeX Export to EndNote
9 Records (9 excluding Abstracts).
Total impact factor: 32.212 (32.212 excluding Abstracts).
Total 5 year impact factor: 31.915 (31.915 excluding Abstracts).
Total impact factor: 32.212 (32.212 excluding Abstracts).
Total 5 year impact factor: 31.915 (31.915 excluding Abstracts).
376 views. Last view on Saturday 14 January 2023, 17:14:05
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