Gama-Enolase, a glycolytic enzyme, is expressed specifically in neurons. It exerts neurotrophic activity and has been suggested to regulate growth, differentiation, survival and regeneration of neurons. In this study, we investigated the involvement of gama enolase in PI 3-kinase/Akt) and MAPK/ERK (mitogen-activated protein kinase/ extracellular-signal-regulated kinase) signaling, the two pathways triggered predominantly by neurotrophic factors. While the PI 3-K/Akt pathway, rather than the MAPK/ERK pathway, is involved in gama-enolase-enhanced cell survival, gama-enolase-stimulated neurite outgrowth requires both pathways, i.e. the activation of both PI 3-K and ERK1/2, leading to subsequent expression of growth cone-specific GAP-43 protein.
COBISS.SI-ID: 3194993
Podosomes, specialized actin-rich structures in macrophages, degrade the extracellular matrix (ECM) and are involved in cell migration. We have shown that the tips of macrophage protrusive podosomes are characterized by increased accumulation of cysteine cathepsins (Cts) B, X, S, H and L, both in human blood macrophages and in human monocytic cell line U-937. Monocyte-to-macrophage differentiation induces an increase in cysteine cathepsin expression and activity, promoting their translocation to the cell surface, where they interact with ECM. The targeting of cysteine cathepsins, as the major mediators of human macrophage 3D invasion, could be an approach to the treatment of inflammatory and cancerous diseases.
COBISS.SI-ID: 3319921
Cystatin F, cysteine protease inhibitor, is present in DCs in endosomal/lysosomal vesicles and thus has a potential to modulate cathepsin activity. The inhibitory potential of cystatin F depends on the properties of the monomer. We showed that the full-length monomeric cystatin F was a 12-fold stronger inhibitor of cathepsin S than the N-terminally processed cystatin F, whereas no significant difference in inhibition was observed for cathepsins L, H and X. The role of cystatin F in regulating the main cathepsin S function in DCs, i.e. the processing of Ii, may depend on the form of the monomer present in vesicles. On the other hand, intact and truncated monomeric cystatin F are both potent inhibitors of cathepsin L and it is likely that cystatin F could regulate its activity in maturing, adherent DCs, controlling the processing of procathepsin X, which promotes cell adhesion via activation of Mac-1 (CD11b/CD18) integrin receptor.
COBISS.SI-ID: 3207025