Multiple inflammatory stimuli lead to activation of the IKK complex, which phosphorylates IκB and promotes its polyubiquitination and proteasomal degradation. NF-κB proteins (such as p50/p65 heterodimers) that are released from IκB are imported into the nucleus via their nuclear localization signals, where they activate the transcription of proinflammatory genes, including vascular adhesion molecules (i.e., Vcam1, Icam1, Sele). Nuclear import of NF-κB is facilitated by importin proteins, including importin-α3. MicroRNAs bind to the 3ι UTRs of target mRNAs and inhibit their stability and/or translation. miR-181b elicits an antiinflammatory effect in endothelial cells by repressing importin-α3 expression, thereby inhibiting nuclear import of NF-κB. In addition, an endothelial-specific microRNA, miR-126, inhibits the expression of VCAM-1, and inflammation induces the expression of several microRNAs, including miR-31, miR-17-3p, and miR-146a, which participate in negative feedback loops. miR-31 negatively regulates E-selectin, miR-17-3p represses ICAM-1 expression, and miR-146a targets adaptor molecules (i.e., IRAK1, TRAF6) that are involved in inflammatory signal transduction. miR-10a, which is reduced in regions of blood vessels that are exposed to disturbed flow, represses MAP3K7 (TAK1) and β-TRC, which promote IκB degradation.