Vol. 4, Issue 1 (2015)
Glycated ferritin induces activation and expression of tlr2 and tlr4 in human peripheral blood macrophages
Galván-Moroyoqui JM, Candia-Plata MC, Martínez-Soto JM, Soto-Guzmán JA, Bolado Martínez E, Camacho-Villa AY, López-Soto LF
Recently it has been proposed that serum ferritin might play a role in the pathogenesis of metabolic diseases, however so far unknown mechanism by which ferritin involved in these disorders. It has been reported that ferritin can be modified by glycation and peroxidation, through a process that occurs naturally but is increased in subjects with diabetes, called non-enzymatic glycation. This work was carried out modifying ferritin using an in vitro model of glycation process and used these modified protein by glycation as a stimulus in peripheral blood mononuclear cells (PBMN). We observed that ferritin glycated activates the expression of TLR2 and TLR4 in cells CD14+ derived from PBMN cells and further these PBMN cells increase the secretion of pro-inflammatory cytokines IL-6 and IL-8. Our results suggest that the activation of the TLR signaling pathway, is stimulated with glycated ferritin, increasing the production of pro-inflammatory cytokines in the supernatants of the PBMC, these data strongly suggesting that this modified protein acts as a potent inflammatory stimulus activating the CD14+ cells, it acting in a similar way as is done by advanced glycation endproducts, by activating TLRs and induction of cytokine secretion, which suggests that it could play a key role in the onset of chronic inflammation observed in patients with diabetes and which could contribute to the development of vascular complications in these patients.
How to cite this article:
Galván-Moroyoqui JM, Candia-Plata MC, Martínez-Soto JM, Soto-Guzmán JA, Bolado Martínez E, Camacho-Villa AY, López-Soto LF. . The Pharma Innovation Journal. 2015; 4(1): 44-48.