The cross-talk between the two cell types might exert an effect also in the opposite direction, regulating mast cells and their role in Dabrafenib inquirer inflammation, as has been observed for other members of the TNF/TNF receptor superfamily. In fact, mast cells can be activated by T-cell-dependent co-stimulatory signals transduced by ligation of lymphotoxin-b and 4-1BBL. Finally, TNFSF4 expressed on endothelial cells was reported to mediate the adhesion of TNFRSF4-expressing T-cells to vascular endothelial cells and the subsequent migration to distant inflammatory sites, suggesting an involvement of TNFSF4 in lymphocyte recruitment as well. Unstable plaques are particularly rich in activated lymphocytes ; therefore all these events, possibly triggered by TNFSF4, may favor destabilization and rupture of the plaque. In conclusion, the present work suggests that lowered TNFSF4 expression is associated with an increased risk of MI. Further analyses are now needed to precisely determine the function of the TNFSF4 protein in MI. Specifically, the gender difference needs to be evaluated on a molecular level. TDP-43 is an RNA binding protein of 43 kDa that belongs to the hnRNP family and plays numerous roles in mRNA metabolism such us transcription, pre-mRNA high throughput screening in vivo splicing, mRNA stability, microRNA biogenesis, transport and translation. TDP-43 is very well conserved during the evolution, especially with regards to the two RNA-recognition motifs, the first being responsible for the binding of TDP-43 with UG rich RNA. In consonance with these described functions, TDP-43 prevalently resides in the cell nucleus where it co-localizes with other members of the RNA processing machinery. Nevertheless, in pathological conditions such as amyotrophic lateral sclerosis and frontotemporal lobar degeneration, TDP-43 appears in the form of large insoluble protein aggregates redistributed within the cytoplasm. At the moment, however, it is not clear how these alterations may lead to neurodegeneration. In theory, the cytosolic accumulation of TDP- 43 may induce a toxic, gain of function effect on motoneurons whilst the exclusion of TDP-43 from the cell nucleus may lead to neurodegeneration due to a loss of function mechanism. At present, several lines of evidence mainly from different cellular and animal models support either view suggesting that both models may be acting to lead the disease condition. Recently, to determine the physiological role of TDP-43 in vivo we have reported that the flies which lack the TDP-43 homologue closely reproduce many of the phenotypes observed in ALS patients, such as progressive defects in the animal locomotion and reduced life span. Moreover, we have observed that loss of TDP-43 function in Drosophila resulted in reduced number of motoneurons terminal branches and synaptic boutons at neuromuscular junctions, indicating TDP-43 may regulate the assembly and organization of these structures.