NF-κB and Disease

Dear Colleagues,

NF-κB proteins are members of a family that includes p52/p100, p50/p105, c-Rel, RelA/p65, and RelB. These proteins are able to dimerize to form transcription factors that regulate the expression of many targets. In the canonical pathway, stimuli as proinflammatory cytokines, LPS, growth factors, and antigen receptors activate an IKK complex (IKKβ, IKKα, and NEMO), which phosphorylates IκB proteins and consequently causes their ubiquitination and proteasomal degradation. NF-κB that in the cytoplasm is bound to IκB, can, therefore, translocate to the nucleus where alone or, in combination with other transcription factors (AP-1, Ets, and Stat), induce target gene expression. In the noncanonical pathway, p100/RelB complexes are inactive in the cytoplasm. A series of stimuli, including ligands of a subset of TNFR superfamily members such as LTβR, BAFFR, CD40, and RANK, cause the activation of the kinase NIK and, after, IKKα complexes. These phosphorylate p100 that is proteolytically processed to p52 which, together with RelB complexes, translocates to the nucleus and induces target gene expression. The pathological activation of NF-κB has been demonstrated in many diseases marked by an inflammatory process, from cancer to autoimmune diseases.

This Special Issue focuses on all diseases in which NF-κB has a role, with particular attention to molecular mechanisms involved in overexpression and/or activation of NF-κB and therapeutic implication to such events, through the use of molecules, natural and synthetic compounds, also in the form of conjugates biocompatible, which act as NF-κB inhibitors.

Dr. Paola Poma
Dr. Serena Riela
Dr. Monica Notarbartolo
Guest Editors

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