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Paolo Ascenzi - One of the best experts on this subject based on the ideXlab platform.
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Molecular phylogenetic analyses of Albuminoids reveal the molecular evolution of allosteric properties.
IUBMB life, 2013Co-Authors: Paolo Ascenzi, Gabriella Fanali, Loris Leboffe, Alessandra Di Masi, Tiziana Alberio, Mauro FasanoAbstract:Serum albumin, α-fetoprotein, afamin (also named α-albumin and vitamin E binding protein), and vitamin D binding protein are members of the Albuminoid superfamily. Albuminoids are plasma proteins characterized by a marked ability for ligand binding and transport. Here, a focused phylogenetic analysis of sequence evolution by maximum likelihood of fatty acid binding sites FA1–FA7 of mammalian Albuminoids reveals that the FA1, FA2, and FA3+FA4 sites in serum albumins have evolved from the most recent common ancestor through an intermediate that has originated the α-fetoprotein and afamin clades. The same topology has been observed for the whole protein sequences, for the sequences of all the fatty acid binding sites (FA1–FA7) taken together, and for the allosteric core corresponding to residues 1–303 of human serum albumin. The quantitative divergence analysis indicates that the ligand binding cleft corresponding to the FA2 site could be the main determinant of allosteric properties of serum albumins only. In fact, this binding cleft is structurally not effective in vitamin D binding proteins, whereas key residues that serve to allocate the allosteric effectors are not present in afamins and α-fetoproteins. © 2013 IUBMB Life, 65(6):544–549, 2013
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Heme binding to Albuminoid proteins is the result of recent evolution.
IUBMB life, 2007Co-Authors: Mauro Fasano, Gabriella Fanali, Loris Leboffe, Paolo AscenziAbstract:We hypothesize that the structure of the heme binding site of paralogous Albuminoids alpha-fetoprotein and serum albumin has evolved from the ancestor vitamin D binding protein through the 'phylogenetic intermediate' afamin, the most recently discovered Albuminoid. Heme binding to plasma proteins should serve not only as a buffer for heme homeostasis, avoiding heme binding to lipoproteins with the consequent oxidative stress, but also for heme transfer to the liver, complementing the function of hemopexin.
Mauro Fasano - One of the best experts on this subject based on the ideXlab platform.
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Molecular phylogenetic analyses of Albuminoids reveal the molecular evolution of allosteric properties.
IUBMB life, 2013Co-Authors: Paolo Ascenzi, Gabriella Fanali, Loris Leboffe, Alessandra Di Masi, Tiziana Alberio, Mauro FasanoAbstract:Serum albumin, α-fetoprotein, afamin (also named α-albumin and vitamin E binding protein), and vitamin D binding protein are members of the Albuminoid superfamily. Albuminoids are plasma proteins characterized by a marked ability for ligand binding and transport. Here, a focused phylogenetic analysis of sequence evolution by maximum likelihood of fatty acid binding sites FA1–FA7 of mammalian Albuminoids reveals that the FA1, FA2, and FA3+FA4 sites in serum albumins have evolved from the most recent common ancestor through an intermediate that has originated the α-fetoprotein and afamin clades. The same topology has been observed for the whole protein sequences, for the sequences of all the fatty acid binding sites (FA1–FA7) taken together, and for the allosteric core corresponding to residues 1–303 of human serum albumin. The quantitative divergence analysis indicates that the ligand binding cleft corresponding to the FA2 site could be the main determinant of allosteric properties of serum albumins only. In fact, this binding cleft is structurally not effective in vitamin D binding proteins, whereas key residues that serve to allocate the allosteric effectors are not present in afamins and α-fetoproteins. © 2013 IUBMB Life, 65(6):544–549, 2013
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Heme binding to Albuminoid proteins is the result of recent evolution.
IUBMB life, 2007Co-Authors: Mauro Fasano, Gabriella Fanali, Loris Leboffe, Paolo AscenziAbstract:We hypothesize that the structure of the heme binding site of paralogous Albuminoids alpha-fetoprotein and serum albumin has evolved from the ancestor vitamin D binding protein through the 'phylogenetic intermediate' afamin, the most recently discovered Albuminoid. Heme binding to plasma proteins should serve not only as a buffer for heme homeostasis, avoiding heme binding to lipoproteins with the consequent oxidative stress, but also for heme transfer to the liver, complementing the function of hemopexin.
Vincent J. Hearing - One of the best experts on this subject based on the ideXlab platform.
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Serologic Demonstration of the Albuminoid Nature of the B700 Murine Melanoma Antigen
Experimental Biology and Medicine, 1991Co-Authors: Douglas M. Gersten, Karen E. Bijwaard, Thomas L. Walden, Vincent J. HearingAbstract:AbstractLimited available evidence indicates that the B700 murine melanoma antigen is related to serum albumin, but potential relationships to other members of the serum albumin protein family have not yet been established. Using specific antibodies raised against each of the members of the albumin family, we have studied cross-reactivity by solid phase enzyme-linked immunosorbent assay and Western immunoblotting. We demonstrate that B700 is serologically cross-reactive to members of the serum albumin family, which includes α-fetoprotein and vitamin D binding protein. Therefore, B700 is part of the serum albumin family of proteins, although the mechanism underlying its specific expression by transformed melanocytes remains unknown.
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B700, an albumin-like melanoma-specific antigen, is a vitamin D binding protein.
European journal of cancer (Oxford England : 1990), 1991Co-Authors: Nushkin K. Farzaneh, Thomas L. Walden, Vincent J. Hearing, Douglas M. GerstenAbstract:B700, a murine melanoma-specific antigen, is a member of the serum albumin protein family. Other members include serum albumin and vitamin D binding protein. The primary structure and biochemical functions of B700, as well as its in vivo metabolic fate, are largely unknown. We compared murine albumin, vitamin D binding protein and B700 for their ability to specifically bind [3H]-1,25-dihydroxy-vitamin D3. Scatchard analysis revealed a single binding site for B700 with a Ka of 51,000 mol/l and a Bmax of 4.51 x 10(-7) mol/l. There was no significant difference in the Ka and Bmax among the Albuminoid proteins. However, differences in the binding sites could be distinguished by competition experiments where vitamin D3, vitamin D2 or 7-dehydrocholesterol competed for the specific binding of 1.25-dihydroxyvitamin D3 to a greater extent by B700 than by vitamin D binding protein. The albumin binding site more closely resembles vitamin D binding protein than B700, but the data indicate that the binding function of the Albuminoid proteins is conserved in B700.
Loris Leboffe - One of the best experts on this subject based on the ideXlab platform.
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Molecular phylogenetic analyses of Albuminoids reveal the molecular evolution of allosteric properties.
IUBMB life, 2013Co-Authors: Paolo Ascenzi, Gabriella Fanali, Loris Leboffe, Alessandra Di Masi, Tiziana Alberio, Mauro FasanoAbstract:Serum albumin, α-fetoprotein, afamin (also named α-albumin and vitamin E binding protein), and vitamin D binding protein are members of the Albuminoid superfamily. Albuminoids are plasma proteins characterized by a marked ability for ligand binding and transport. Here, a focused phylogenetic analysis of sequence evolution by maximum likelihood of fatty acid binding sites FA1–FA7 of mammalian Albuminoids reveals that the FA1, FA2, and FA3+FA4 sites in serum albumins have evolved from the most recent common ancestor through an intermediate that has originated the α-fetoprotein and afamin clades. The same topology has been observed for the whole protein sequences, for the sequences of all the fatty acid binding sites (FA1–FA7) taken together, and for the allosteric core corresponding to residues 1–303 of human serum albumin. The quantitative divergence analysis indicates that the ligand binding cleft corresponding to the FA2 site could be the main determinant of allosteric properties of serum albumins only. In fact, this binding cleft is structurally not effective in vitamin D binding proteins, whereas key residues that serve to allocate the allosteric effectors are not present in afamins and α-fetoproteins. © 2013 IUBMB Life, 65(6):544–549, 2013
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Heme binding to Albuminoid proteins is the result of recent evolution.
IUBMB life, 2007Co-Authors: Mauro Fasano, Gabriella Fanali, Loris Leboffe, Paolo AscenziAbstract:We hypothesize that the structure of the heme binding site of paralogous Albuminoids alpha-fetoprotein and serum albumin has evolved from the ancestor vitamin D binding protein through the 'phylogenetic intermediate' afamin, the most recently discovered Albuminoid. Heme binding to plasma proteins should serve not only as a buffer for heme homeostasis, avoiding heme binding to lipoproteins with the consequent oxidative stress, but also for heme transfer to the liver, complementing the function of hemopexin.
Gabriella Fanali - One of the best experts on this subject based on the ideXlab platform.
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Molecular phylogenetic analyses of Albuminoids reveal the molecular evolution of allosteric properties.
IUBMB life, 2013Co-Authors: Paolo Ascenzi, Gabriella Fanali, Loris Leboffe, Alessandra Di Masi, Tiziana Alberio, Mauro FasanoAbstract:Serum albumin, α-fetoprotein, afamin (also named α-albumin and vitamin E binding protein), and vitamin D binding protein are members of the Albuminoid superfamily. Albuminoids are plasma proteins characterized by a marked ability for ligand binding and transport. Here, a focused phylogenetic analysis of sequence evolution by maximum likelihood of fatty acid binding sites FA1–FA7 of mammalian Albuminoids reveals that the FA1, FA2, and FA3+FA4 sites in serum albumins have evolved from the most recent common ancestor through an intermediate that has originated the α-fetoprotein and afamin clades. The same topology has been observed for the whole protein sequences, for the sequences of all the fatty acid binding sites (FA1–FA7) taken together, and for the allosteric core corresponding to residues 1–303 of human serum albumin. The quantitative divergence analysis indicates that the ligand binding cleft corresponding to the FA2 site could be the main determinant of allosteric properties of serum albumins only. In fact, this binding cleft is structurally not effective in vitamin D binding proteins, whereas key residues that serve to allocate the allosteric effectors are not present in afamins and α-fetoproteins. © 2013 IUBMB Life, 65(6):544–549, 2013
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Heme binding to Albuminoid proteins is the result of recent evolution.
IUBMB life, 2007Co-Authors: Mauro Fasano, Gabriella Fanali, Loris Leboffe, Paolo AscenziAbstract:We hypothesize that the structure of the heme binding site of paralogous Albuminoids alpha-fetoprotein and serum albumin has evolved from the ancestor vitamin D binding protein through the 'phylogenetic intermediate' afamin, the most recently discovered Albuminoid. Heme binding to plasma proteins should serve not only as a buffer for heme homeostasis, avoiding heme binding to lipoproteins with the consequent oxidative stress, but also for heme transfer to the liver, complementing the function of hemopexin.