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.
Export to BibTeX Export to EndNote
Paper type: Journal Article, Research Support, Non-U. S. Gov'T,
Impact factor: 3.035, 5-year impact factor: 2.945
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-56549094997&partnerID=40&md5=0c8758d42e3bb9a3e15bcb4f813332a3
Keywords: Apoa-I Zaragoza, Apoa-I Zavalla, High-Density Lipoprotein, Lecithin-Cholesterol Acyltransferase, Peptides, Reverse Cholesterol Transport, Apolipoprotein A1, Haptoglobin, High Density Lipoprotein Cholesterol, Phosphatidylcholine Sterol Acyltransferase, Amino Acid Substitution, Article, Binding Assay, Binding Site, Correlation Analysis, Enzyme Activity, Enzyme Regulation, Human, Point Mutation, Priority Journal, Protein Binding, Protein Protein Interaction, Protein Variant, Amino Acid Sequence, Competitive, Molecular Sequence Data, Phosphatidylcholine-Sterol O-Acyltransferase,
Affiliations:
*** IBB - CNR ***
Dipartimento delle Scienze Biologiche, Universita di Napoli Federico II, I-80134 Napoli, Italy.
Istituto di Biostrutture e Bioimmagini, Consiglio Nazionale Delle Ricerche, I-80134 Napoli, Italy
Dipartimento di Patologia Sistematica, Sezione di Dermatologia, Università di Napoli Federico II, I-80131 Napoli, Italy
Istituto Per Il Sistema Produzione Animale in Ambiente Mediterraneo, Consiglio Nazionale Delle Ricerche, I-80147 Napoli, Italy
Istituto di Genetica e Biofisica 'A. Buzzati Traverso', Consiglio Nazionale Delle Ricerche, I-80131 Napoli, Italy
References:
Alexander, E.T., Bhat, S., Thomas, M.J., Weinberg, R.B., Cook, V.R., Bharadwaj, M.S., Sorci-Thomas, M., Apolipoprotein A-I helix 6 negatively charged residues attenuate lecithin-cholesterol acyltransferase (LCAT) reactivity (2005) Biochemistry, 44, pp. 5409-541
Ansell, B.J., Navab, M., Hama, S., Kamranpour, N., Fonarow, G., Hough, G., Rahmani, S., Fogelman, A.M., Inflammatory/antiinflammatory properties of high-density lipoprotein distinguish patients from control subjects better than high-density lipoprotein cholesterol levels and are favorably affected by simvastatin treatment (2003) Circulation, 108, pp. 2751-2756
Ajees, A.A., Anantharamaiah, G.M., Mishra, V.K., Hussain, M.M., Murthy, H.M., Crystal structure of human apolipoprotein A-I: Insights into its protective effect against cardiovascular diseases (2006) Proc. Natl. Acad. Sci. USA, 103, pp. 2126-2131
Balestrieri, M., Cigliano, L., De Simone, M.L., Dale, B., Abrescia, P., Haptoglobin inhibits lecithin-cholesterol acyltransferase in human ovarian follicular fluid (2001) Mol. Reprod. Dev, 59, pp. 186-191
Borhani, D.W., Rogers, D.P., Engler, J.A., Brouillette, C.G., Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation (1997) Proc. Natl. Acad. Sci. USA, 94, pp. 12291-12296
Chan, W.D., White, P.D., (2000) Fmoc Solid Phase Peptide Synthesis, , New York, USA: Academic Press
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
Cigliano, L., Spagnuolo, M.S., Dale, B., Balestrieri, M., Abrescia, P., Estradiol esterification in the human preovulatory follicle (2001) Steroids, 66, pp. 889-896
Davidson, V.S., Thompson, T.B., The structure of apolipoprotein A-I in high density lipoproteins (2007) J. Biol. Chem, 282, pp. 22249-22253
Fielding, C., Fielding, P.E., Molecular physiology of reverse cholesterol transport (1995) J. Lipid Res, 36, pp. 211-228
Hovingh, G.K., Brownlie, A., Bisoendial, R.J., Dube, M.P., Levels, J.H., Petersen, W., Dullaart, R.P., de Groot, E., A novel apoA-I mutation (L178P) leads to endothelial dysfunction, increased arterial wall thickness, and premature coronary artery disease (2004) J. Am. Coll. Cardiol, 44, pp. 1429-1435
Huang, W., Sasaki, J., Matsunaga, A., Nanimatsu, H., Moriyama, K., Han, H., Kugi, M., Arakawa, K., A novel homozygous missense mutation in the apo A-I gene with apo A-I deficiency (1998) Arterioscler. Thromb. Vasc. Biol, 18, pp. 389-396
Langlois, M.R., Delanghe, J.R., Biological and clinical significance of haptoglobin polymorphism in humans (1996) Clin. Chem, 42, pp. 1589-1600
Lindholm, E.M., Bielicki, J.K., Curtiss, L.K., Rubin, E.M., Forte, T.M., Deletion of amino acids Glu146 to Arg160 in human apolipoprotein A-I (apoA-I Seattle) alters lecithin: Cholesterol acyltransferase activity and recruitment of cell phospholipid (1998) Biochemistry, 37, pp. 4863-4868
Miccoli, R., Bertolotto, A., Navalesi, R., Odoguardi, L., Boni, A., Wessling, J., Funke, H., Assmann, G., Compound heterozygosity for a structural apolipoprotein A-I variant, apo A-I(L141R) Pisa, and an apolipoprotein A-I null allele in patients with absence of HDL cholesterol, corneal opacifications, and coronary heart disease (1996) Circulation, 94, pp. 1622-1628
Miettinen, H.E., Gylling, H., Miettinen, T.A., Viikari, J., Paulin, L., Kontula, K., Apolipoprotein A-IFin. Dominantly inherited hypoalphalipoproteinemia due to a single base substitution in the apolipoprotein A-I gene (1997) Arterioscler. Thromb. Vasc. Biol, 17, pp. 83-90
Miller, M., Aiello, D., Pritchard, H., Friel, G., Zeller, K., Apolipoprotein A-IZavalla (Leu159 → Pro) HDL cholesterol deficiency in a kindred associated with premature coronary heart disease (1998) Arterioscler. Thromb. Vasc. Biol, 18, pp. 1242-1247
Palgunachari, M.N., Mishra, V.K., Lund-Katz, S., Phillips, M.C., Adeyeye, S.O., Alluri, S., Anantharamaiah, G.M., Segrest, J.P., Only the two end helixes of eight tandem amphipathic helical domains of human apo A-I have significant lipid affinity. Implications for HDL assembly (1996) Arterioscler. Thromb. Vasc. Biol, 16, pp. 328-338
Rader, D.J., High-density lipoproteins and atherosclerosis (2002) Am. J. Cardiol, 90, pp. 62i-70i
Recalde, D., Velez-Carrasco, W., Civeira, F., Cenarro, A., Gomez-Coronado, D., Ordovas, J.M., Pocovi, M., Enhanced fractional catabolic rate of apo A-I and apo A-II in heterozygous subjects for apo A-I Zaragoza (L144R) (2001) Atherosclerosis, 154, pp. 613-623
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. 11158-11168
Sorci-Thomas, M.G., Thomas, M.J., The effects of altered apolipoproteinA-I structure on plasma HDL concentration (2002) Trends Cardiovasc. Med, 12, pp. 121-128
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
Yamakawa-Kobayashi, K., Yanagi, H., Fukayama, H., Hirano, C., Shimakura, Y., Yamamoto, N., Arinami, T., Hamaguchi, H., Frequent occurrence of hypoalpha-lipoproteinemia due to mutant apolipoprotein A-I gene in the population: A population-based survey (1999) Hum. Mol. Genet, 8, pp. 331-336
Zannis, V.I., Chroni, A., Krieger, M., Role of apoA-I, ABCA1, LCAT, and SR-BI in the biogenesis of HDL (2006) J. Mol. Med, 84, pp. 276-294
Zannis, V.I., Koukos, G., Drosatos, K., Vezeridis, A., Zanni, E.E., Kypreos, K.E., Chroni, A., Discrete roles of apoAI and apoE in the biogenesis of HDL species: Lessons learned from gene transfer studies in different mouse models (2008) Ann. Med, 40 (SUPPL. 1), pp. 14-28
Alexander, E. T., Bhat, S., Thomas, M. J., Weinberg, R. B., Cook, V. R., Bharadwaj, M. S., Sorci-Thomas, M., Apolipoprotein A-I helix 6 negatively charged residues attenuate lecithin-cholesterol acyltransferase (LCAT) reactivity (2005) Biochemistry, 44, pp. 5409-541
Ansell, B. J., Navab, M., Hama, S., Kamranpour, N., Fonarow, G., Hough, G., Rahmani, S., Fogelman, A. M., Inflammatory/antiinflammatory properties of high-density lipoprotein distinguish patients from control subjects better than high-density lipoprotein cholesterol levels and are favorably affected by simvastatin treatment (2003) Circulation, 108, pp. 2751-2756
Ajees, A. A., Anantharamaiah, G. M., Mishra, V. K., Hussain, M. M., Murthy, H. M., Crystal structure of human apolipoprotein A-I: Insights into its protective effect against cardiovascular diseases (2006) Proc. Natl. Acad. Sci. USA, 103, pp. 2126-2131
Borhani, D. W., Rogers, D. P., Engler, J. A., Brouillette, C. G., Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation (1997) Proc. Natl. Acad. Sci. USA, 94, pp. 12291-12296
Chan, W. D., White, P. D., (2000) Fmoc Solid Phase Peptide Synthesis, , New York, USA: Academic Press
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
Davidson, V. S., Thompson, T. B., The structure of apolipoprotein A-I in high density lipoproteins (2007) J. Biol. Chem, 282, pp. 22249-22253
Hovingh, G. K., Brownlie, A., Bisoendial, R. J., Dube, M. P., Levels, J. H., Petersen, W., Dullaart, R. P., de Groot, E., A novel apoA-I mutation (L178P) leads to endothelial dysfunction, increased arterial wall thickness, and premature coronary artery disease (2004) J. Am. Coll. Cardiol, 44, pp. 1429-1435
Langlois, M. R., Delanghe, J. R., Biological and clinical significance of haptoglobin polymorphism in humans (1996) Clin. Chem, 42, pp. 1589-1600
Lindholm, E. M., Bielicki, J. K., Curtiss, L. K., Rubin, E. M., Forte, T. M., Deletion of amino acids Glu146 to Arg160 in human apolipoprotein A-I (apoA-I Seattle) alters lecithin: Cholesterol acyltransferase activity and recruitment of cell phospholipid (1998) Biochemistry, 37, pp. 4863-4868
Miettinen, H. E., Gylling, H., Miettinen, T. A., Viikari, J., Paulin, L., Kontula, K., Apolipoprotein A-IFin. Dominantly inherited hypoalphalipoproteinemia due to a single base substitution in the apolipoprotein A-I gene (1997) Arterioscler. Thromb. Vasc. Biol, 17, pp. 83-90
Palgunachari, M. N., Mishra, V. K., Lund-Katz, S., Phillips, M. C., Adeyeye, S. O., Alluri, S., Anantharamaiah, G. M., Segrest, J. P., Only the two end helixes of eight tandem amphipathic helical domains of human apo A-I have significant lipid affinity. Implications for HDL assembly (1996) Arterioscler. Thromb. Vasc. Biol, 16, pp. 328-338
Rader, D. J., High-density lipoproteins and atherosclerosis (2002) Am. J. Cardiol, 90, pp. 62i-70i
Sorci-Thomas, M. G., Thomas, M. J., The effects of altered apolipoproteinA-I structure on plasma HDL concentration (2002) Trends Cardiovasc. Med, 12, pp. 121-128
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
Zannis, V. I., Chroni, A., Krieger, M., Role of apoA-I, ABCA1, LCAT, and SR-BI in the biogenesis of HDL (2006) J. Mol. Med, 84, pp. 276-294
Zannis, V. I., Koukos, G., Drosatos, K., Vezeridis, A., Zanni, E. E., Kypreos, K. E., Chroni, A., Discrete roles of apoAI and apoE in the biogenesis of HDL species: Lessons learned from gene transfer studies in different mouse models (2008) Ann. Med, 40 (SUPPL. 1), pp. 14-28
Biol Chem Biological Chemistry (ISSN: 1431-6730, 1437-4315), 2008 Nov; 389(11): 1421-1426.
Export to BibTeX Export to EndNote
Paper type: Journal Article, Research Support, Non-U. S. Gov'T,
Impact factor: 3.035, 5-year impact factor: 2.945
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-56549094997&partnerID=40&md5=0c8758d42e3bb9a3e15bcb4f813332a3
Keywords: Apoa-I Zaragoza, Apoa-I Zavalla, High-Density Lipoprotein, Lecithin-Cholesterol Acyltransferase, Peptides, Reverse Cholesterol Transport, Apolipoprotein A1, Haptoglobin, High Density Lipoprotein Cholesterol, Phosphatidylcholine Sterol Acyltransferase, Amino Acid Substitution, Article, Binding Assay, Binding Site, Correlation Analysis, Enzyme Activity, Enzyme Regulation, Human, Point Mutation, Priority Journal, Protein Binding, Protein Protein Interaction, Protein Variant, Amino Acid Sequence, Competitive, Molecular Sequence Data, Phosphatidylcholine-Sterol O-Acyltransferase,
Affiliations:
*** IBB - CNR ***
Dipartimento delle Scienze Biologiche, Universita di Napoli Federico II, I-80134 Napoli, Italy.
Istituto di Biostrutture e Bioimmagini, Consiglio Nazionale Delle Ricerche, I-80134 Napoli, Italy
Dipartimento di Patologia Sistematica, Sezione di Dermatologia, Università di Napoli Federico II, I-80131 Napoli, Italy
Istituto Per Il Sistema Produzione Animale in Ambiente Mediterraneo, Consiglio Nazionale Delle Ricerche, I-80147 Napoli, Italy
Istituto di Genetica e Biofisica 'A. Buzzati Traverso', Consiglio Nazionale Delle Ricerche, I-80131 Napoli, Italy
References:
Alexander, E.T., Bhat, S., Thomas, M.J., Weinberg, R.B., Cook, V.R., Bharadwaj, M.S., Sorci-Thomas, M., Apolipoprotein A-I helix 6 negatively charged residues attenuate lecithin-cholesterol acyltransferase (LCAT) reactivity (2005) Biochemistry, 44, pp. 5409-541
Ansell, B.J., Navab, M., Hama, S., Kamranpour, N., Fonarow, G., Hough, G., Rahmani, S., Fogelman, A.M., Inflammatory/antiinflammatory properties of high-density lipoprotein distinguish patients from control subjects better than high-density lipoprotein cholesterol levels and are favorably affected by simvastatin treatment (2003) Circulation, 108, pp. 2751-2756
Ajees, A.A., Anantharamaiah, G.M., Mishra, V.K., Hussain, M.M., Murthy, H.M., Crystal structure of human apolipoprotein A-I: Insights into its protective effect against cardiovascular diseases (2006) Proc. Natl. Acad. Sci. USA, 103, pp. 2126-2131
Balestrieri, M., Cigliano, L., De Simone, M.L., Dale, B., Abrescia, P., Haptoglobin inhibits lecithin-cholesterol acyltransferase in human ovarian follicular fluid (2001) Mol. Reprod. Dev, 59, pp. 186-191
Borhani, D.W., Rogers, D.P., Engler, J.A., Brouillette, C.G., Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation (1997) Proc. Natl. Acad. Sci. USA, 94, pp. 12291-12296
Chan, W.D., White, P.D., (2000) Fmoc Solid Phase Peptide Synthesis, , New York, USA: Academic Press
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
Cigliano, L., Spagnuolo, M.S., Dale, B., Balestrieri, M., Abrescia, P., Estradiol esterification in the human preovulatory follicle (2001) Steroids, 66, pp. 889-896
Davidson, V.S., Thompson, T.B., The structure of apolipoprotein A-I in high density lipoproteins (2007) J. Biol. Chem, 282, pp. 22249-22253
Fielding, C., Fielding, P.E., Molecular physiology of reverse cholesterol transport (1995) J. Lipid Res, 36, pp. 211-228
Hovingh, G.K., Brownlie, A., Bisoendial, R.J., Dube, M.P., Levels, J.H., Petersen, W., Dullaart, R.P., de Groot, E., A novel apoA-I mutation (L178P) leads to endothelial dysfunction, increased arterial wall thickness, and premature coronary artery disease (2004) J. Am. Coll. Cardiol, 44, pp. 1429-1435
Huang, W., Sasaki, J., Matsunaga, A., Nanimatsu, H., Moriyama, K., Han, H., Kugi, M., Arakawa, K., A novel homozygous missense mutation in the apo A-I gene with apo A-I deficiency (1998) Arterioscler. Thromb. Vasc. Biol, 18, pp. 389-396
Langlois, M.R., Delanghe, J.R., Biological and clinical significance of haptoglobin polymorphism in humans (1996) Clin. Chem, 42, pp. 1589-1600
Lindholm, E.M., Bielicki, J.K., Curtiss, L.K., Rubin, E.M., Forte, T.M., Deletion of amino acids Glu146 to Arg160 in human apolipoprotein A-I (apoA-I Seattle) alters lecithin: Cholesterol acyltransferase activity and recruitment of cell phospholipid (1998) Biochemistry, 37, pp. 4863-4868
Miccoli, R., Bertolotto, A., Navalesi, R., Odoguardi, L., Boni, A., Wessling, J., Funke, H., Assmann, G., Compound heterozygosity for a structural apolipoprotein A-I variant, apo A-I(L141R) Pisa, and an apolipoprotein A-I null allele in patients with absence of HDL cholesterol, corneal opacifications, and coronary heart disease (1996) Circulation, 94, pp. 1622-1628
Miettinen, H.E., Gylling, H., Miettinen, T.A., Viikari, J., Paulin, L., Kontula, K., Apolipoprotein A-IFin. Dominantly inherited hypoalphalipoproteinemia due to a single base substitution in the apolipoprotein A-I gene (1997) Arterioscler. Thromb. Vasc. Biol, 17, pp. 83-90
Miller, M., Aiello, D., Pritchard, H., Friel, G., Zeller, K., Apolipoprotein A-IZavalla (Leu159 → Pro) HDL cholesterol deficiency in a kindred associated with premature coronary heart disease (1998) Arterioscler. Thromb. Vasc. Biol, 18, pp. 1242-1247
Palgunachari, M.N., Mishra, V.K., Lund-Katz, S., Phillips, M.C., Adeyeye, S.O., Alluri, S., Anantharamaiah, G.M., Segrest, J.P., Only the two end helixes of eight tandem amphipathic helical domains of human apo A-I have significant lipid affinity. Implications for HDL assembly (1996) Arterioscler. Thromb. Vasc. Biol, 16, pp. 328-338
Rader, D.J., High-density lipoproteins and atherosclerosis (2002) Am. J. Cardiol, 90, pp. 62i-70i
Recalde, D., Velez-Carrasco, W., Civeira, F., Cenarro, A., Gomez-Coronado, D., Ordovas, J.M., Pocovi, M., Enhanced fractional catabolic rate of apo A-I and apo A-II in heterozygous subjects for apo A-I Zaragoza (L144R) (2001) Atherosclerosis, 154, pp. 613-623
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. 11158-11168
Sorci-Thomas, M.G., Thomas, M.J., The effects of altered apolipoproteinA-I structure on plasma HDL concentration (2002) Trends Cardiovasc. Med, 12, pp. 121-128
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
Yamakawa-Kobayashi, K., Yanagi, H., Fukayama, H., Hirano, C., Shimakura, Y., Yamamoto, N., Arinami, T., Hamaguchi, H., Frequent occurrence of hypoalpha-lipoproteinemia due to mutant apolipoprotein A-I gene in the population: A population-based survey (1999) Hum. Mol. Genet, 8, pp. 331-336
Zannis, V.I., Chroni, A., Krieger, M., Role of apoA-I, ABCA1, LCAT, and SR-BI in the biogenesis of HDL (2006) J. Mol. Med, 84, pp. 276-294
Zannis, V.I., Koukos, G., Drosatos, K., Vezeridis, A., Zanni, E.E., Kypreos, K.E., Chroni, A., Discrete roles of apoAI and apoE in the biogenesis of HDL species: Lessons learned from gene transfer studies in different mouse models (2008) Ann. Med, 40 (SUPPL. 1), pp. 14-28
Alexander, E. T., Bhat, S., Thomas, M. J., Weinberg, R. B., Cook, V. R., Bharadwaj, M. S., Sorci-Thomas, M., Apolipoprotein A-I helix 6 negatively charged residues attenuate lecithin-cholesterol acyltransferase (LCAT) reactivity (2005) Biochemistry, 44, pp. 5409-541
Ansell, B. J., Navab, M., Hama, S., Kamranpour, N., Fonarow, G., Hough, G., Rahmani, S., Fogelman, A. M., Inflammatory/antiinflammatory properties of high-density lipoprotein distinguish patients from control subjects better than high-density lipoprotein cholesterol levels and are favorably affected by simvastatin treatment (2003) Circulation, 108, pp. 2751-2756
Ajees, A. A., Anantharamaiah, G. M., Mishra, V. K., Hussain, M. M., Murthy, H. M., Crystal structure of human apolipoprotein A-I: Insights into its protective effect against cardiovascular diseases (2006) Proc. Natl. Acad. Sci. USA, 103, pp. 2126-2131
Borhani, D. W., Rogers, D. P., Engler, J. A., Brouillette, C. G., Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation (1997) Proc. Natl. Acad. Sci. USA, 94, pp. 12291-12296
Chan, W. D., White, P. D., (2000) Fmoc Solid Phase Peptide Synthesis, , New York, USA: Academic Press
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
Davidson, V. S., Thompson, T. B., The structure of apolipoprotein A-I in high density lipoproteins (2007) J. Biol. Chem, 282, pp. 22249-22253
Hovingh, G. K., Brownlie, A., Bisoendial, R. J., Dube, M. P., Levels, J. H., Petersen, W., Dullaart, R. P., de Groot, E., A novel apoA-I mutation (L178P) leads to endothelial dysfunction, increased arterial wall thickness, and premature coronary artery disease (2004) J. Am. Coll. Cardiol, 44, pp. 1429-1435
Langlois, M. R., Delanghe, J. R., Biological and clinical significance of haptoglobin polymorphism in humans (1996) Clin. Chem, 42, pp. 1589-1600
Lindholm, E. M., Bielicki, J. K., Curtiss, L. K., Rubin, E. M., Forte, T. M., Deletion of amino acids Glu146 to Arg160 in human apolipoprotein A-I (apoA-I Seattle) alters lecithin: Cholesterol acyltransferase activity and recruitment of cell phospholipid (1998) Biochemistry, 37, pp. 4863-4868
Miettinen, H. E., Gylling, H., Miettinen, T. A., Viikari, J., Paulin, L., Kontula, K., Apolipoprotein A-IFin. Dominantly inherited hypoalphalipoproteinemia due to a single base substitution in the apolipoprotein A-I gene (1997) Arterioscler. Thromb. Vasc. Biol, 17, pp. 83-90
Palgunachari, M. N., Mishra, V. K., Lund-Katz, S., Phillips, M. C., Adeyeye, S. O., Alluri, S., Anantharamaiah, G. M., Segrest, J. P., Only the two end helixes of eight tandem amphipathic helical domains of human apo A-I have significant lipid affinity. Implications for HDL assembly (1996) Arterioscler. Thromb. Vasc. Biol, 16, pp. 328-338
Rader, D. J., High-density lipoproteins and atherosclerosis (2002) Am. J. Cardiol, 90, pp. 62i-70i
Sorci-Thomas, M. G., Thomas, M. J., The effects of altered apolipoproteinA-I structure on plasma HDL concentration (2002) Trends Cardiovasc. Med, 12, pp. 121-128
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
Zannis, V. I., Chroni, A., Krieger, M., Role of apoA-I, ABCA1, LCAT, and SR-BI in the biogenesis of HDL (2006) J. Mol. Med, 84, pp. 276-294
Zannis, V. I., Koukos, G., Drosatos, K., Vezeridis, A., Zanni, E. E., Kypreos, K. E., Chroni, A., Discrete roles of apoAI and apoE in the biogenesis of HDL species: Lessons learned from gene transfer studies in different mouse models (2008) Ann. Med, 40 (SUPPL. 1), pp. 14-28
Relevance of the amino acid conversions L144R (Zaragoza) and L159P (Zavalla) in the apolipoprotein A-I binding site for haptoglobin
The high-density lipoprotein apolipoprotein A-I (ApoA-I) stimulates the enzyme lecithin-cholesterol acyltransferase (LCAT) in the reverse cholesterol transport pathway. Two ApoA-I variants, Zaragoza (L144R) and Zavalla (L159P), are associated with low levels of HDL-cholesterol but normal LCAT activity. Haptoglobin interacts with ApoA-I, impairing LCAT stimulation. Synthetic peptides matching the haptoglobin-binding site of native or variant ApoA-I (native, P2a; variants, Zav-pep and Zar-pep) bound haptoglobin with different activity: Zar-pep>P2a>Zav-pep. They also differently rescued LCAT in vitro activity in the presence of haptoglobin (P2a=Zar-pep>Zav-pep). Therefore, both amino acid conversions affect haptoglobin binding and LCAT regulation. We highlight the role of haptoglobin in LCAT regulation in subjects with ApoA-I variants. © 2008 by Walter de Gruyter.
The high-density lipoprotein apolipoprotein A-I (ApoA-I) stimulates the enzyme lecithin-cholesterol acyltransferase (LCAT) in the reverse cholesterol transport pathway. Two ApoA-I variants, Zaragoza (L144R) and Zavalla (L159P), are associated with low levels of HDL-cholesterol but normal LCAT activity. Haptoglobin interacts with ApoA-I, impairing LCAT stimulation. Synthetic peptides matching the haptoglobin-binding site of native or variant ApoA-I (native, P2a; variants, Zav-pep and Zar-pep) bound haptoglobin with different activity: Zar-pep>P2a>Zav-pep. They also differently rescued LCAT in vitro activity in the presence of haptoglobin (P2a=Zar-pep>Zav-pep). Therefore, both amino acid conversions affect haptoglobin binding and LCAT regulation. We highlight the role of haptoglobin in LCAT regulation in subjects with ApoA-I variants. © 2008 by Walter de Gruyter.
Relevance of the amino acid conversions L144R (Zaragoza) and L159P (Zavalla) in the apolipoprotein A-I binding site for haptoglobin
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Relevance of the amino acid conversions L144R (Zaragoza) and L159P (Zavalla) in the apolipoprotein A-I binding site for haptoglobin
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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 (396 views)
Febs J (ISSN: 1742-464x), 2009 Nov; 276(21): 6158-6171.
Impact Factor: 3.042
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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 (401 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
View Export to BibTeX Export to EndNote
* Haptoglobin binds the antiatherogenic protein apolipoprotein e - Impairment of apolipoprotein e stimulation of both lecithin: Cholesterol acyltransferase activity and cholesterol uptake by hepatocytes (396 views)
Febs J (ISSN: 1742-464x), 2009 Nov; 276(21): 6158-6171.
Impact Factor: 3.042
View Export to BibTeX Export to EndNote
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 (401 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
View Export to BibTeX Export to EndNote
2 Records (2 excluding Abstracts).
Total impact factor: 5.318 (5.318 excluding Abstracts).
Total 5 year impact factor: 5.333 (5.333 excluding Abstracts).
Total impact factor: 5.318 (5.318 excluding Abstracts).
Total 5 year impact factor: 5.333 (5.333 excluding Abstracts).
393 views. Last view on Saturday 14 January 2023, 19:19:25
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