Lipopolysaccharide (LPS)-dependent and nuclear factor (NF)κB-mediated activation of proinflammatory cytokines. LPS binds to LPS-binding protein (LBP) and forms a complex with the surface protein CD14 that further interacts with MD-2 associated Toll-like receptor 4 (TLR4). Myeloid differentiation primary response gene 88 (MyD88) is recruited to TLR4 by its Toll-interleukin 1 receptor (IL1R) (TIR) domain and further activates serine/threonine kinase interleukin 1 receptor-associated kinase (IRAK) by its death domain (DD). After recruitment of tumor necrosis factor receptor associated factor 6 (TRAF-6), another adapter protein, mitogen-activated protein kinase kinase kinase (MAPKKK) transforming growth factor β activated kinase (TAK1) is activated that phosphorylates the inhibitor of κB kinase (IKK) complex. Activated IKK removes inhibitory IκB from the IκB-NFκB complex so that NFκB can enter the nucleus and where it stimulates the expression of proinflammatory chemokines. In a second pathway, which is not listed here, TAK1 is able to activate MAP kinases p38 and c-Jun N-terminal kinase (JNK).