Vitamin D binding protein-derived macrophage activating factor (DBP-MAF) is a powerful activator of macrophages. Polymorphisms of the gene coding for vitamin D receptor (VDR) were associated with differential responses to DBP-MAF in human monocytes. Here we examined the relationships between these vitamin D binding proteins, i.e. DBP-MAF and VDR. VDR and two isoforms of DBP share 20% identity of aminoacid (aa) sequence in the tract coded for by exons 1, 2, 3 ,4, 5, i.e. aa 1-197. An higher degree of identity (40%) was observed in the tract coded for by exons 6, 7, 8, i.e. aa 217-330. The aa in position 445 was of particular interest; VDR and isoforms 1 and 3 of the DBP show a histidine in this position, whereas the isoform 2 shows an arginine. The observation that the VDR and isoforms 1 and 3 of the DBP have the same aa, at variance with the isoform 2, suggests that this variation is implicated in the evolutionary divergence in the genes coding for these vitamin D binding proteins. In fact, isoform 2 has a lysine in position 420 at variance with isoforms 1 and 3 that have a threonine that in turn is glycosylated so that DBP-MAF can be produced from isoforms 1 and 3 but not from isoform 2. These results are consistent with the concept that all the component of the vitamin D axis, i.e. vitamin D, DBP, DBP-MAF, and VDR participate in the regulation of the immune system through macrophage activation.

Study of aminoacidic sequences of vitamin D binding proteins involved in macrophage activation / M.G. Fiore; S. Magherini; M. Gulisano; S. Pacini; M. Ruggiero. - STAMPA. - (In corso di stampa), pp. 0-0. (Intervento presentato al convegno 15th International Congress of Immunology (ICI) tenutosi a Milan, Italy nel 22 Aug - 27 Aug, 2013) [10.3389/conf.fimmu.2013.02.01124].

Study of aminoacidic sequences of vitamin D binding proteins involved in macrophage activation.

GULISANO, MASSIMO;PACINI, STEFANIA;RUGGIERO, MARCO
In corso di stampa

Abstract

Vitamin D binding protein-derived macrophage activating factor (DBP-MAF) is a powerful activator of macrophages. Polymorphisms of the gene coding for vitamin D receptor (VDR) were associated with differential responses to DBP-MAF in human monocytes. Here we examined the relationships between these vitamin D binding proteins, i.e. DBP-MAF and VDR. VDR and two isoforms of DBP share 20% identity of aminoacid (aa) sequence in the tract coded for by exons 1, 2, 3 ,4, 5, i.e. aa 1-197. An higher degree of identity (40%) was observed in the tract coded for by exons 6, 7, 8, i.e. aa 217-330. The aa in position 445 was of particular interest; VDR and isoforms 1 and 3 of the DBP show a histidine in this position, whereas the isoform 2 shows an arginine. The observation that the VDR and isoforms 1 and 3 of the DBP have the same aa, at variance with the isoform 2, suggests that this variation is implicated in the evolutionary divergence in the genes coding for these vitamin D binding proteins. In fact, isoform 2 has a lysine in position 420 at variance with isoforms 1 and 3 that have a threonine that in turn is glycosylated so that DBP-MAF can be produced from isoforms 1 and 3 but not from isoform 2. These results are consistent with the concept that all the component of the vitamin D axis, i.e. vitamin D, DBP, DBP-MAF, and VDR participate in the regulation of the immune system through macrophage activation.
In corso di stampa
Frontiers in immunology: Conference Abstract: 15th International Congress of Immunology (ICI)
15th International Congress of Immunology (ICI)
Milan, Italy
M.G. Fiore; S. Magherini; M. Gulisano; S. Pacini; M. Ruggiero
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Utilizza questo identificatore per citare o creare un link a questa risorsa: https://hdl.handle.net/2158/821889
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