C.S.N.B. Garcia, L.F.M. Prota, M.M. Morales, P.V. Romero, W.A. Zin and P.R.M. Rocco (2006). Understanding the mechanisms of lung mechanical stress. Brazilian Journal of Medical and Bilogical Research, 39: 697-706  

Figure 2. ECM-integrin-cytoskeleton pathway. Integrins maintain a close relationship with extracellular matrix (ECM), and actin-associated molecules (e.g., vinculin, talin, paxilin, and a-actin), focal adhesion kinase (FAK), kinases from the Src family, oncogene products, signaling molecules (e.g., tyrosine and serine protein kinases, and inositol lipid kinases), and some growth factor receptors. Mechanical forces may alter the activity of receptor tyrosine kinases (Flk-1), changing the association of integrins with Shc, activating Ras and downstream extracellular signal-regulated protein kinase (ERK) and c-Jun amino-terminal kinase (JNK) pathways, which, in turn, lead to gene expression mediated by 12-O-tetradecanoylphorbol 13-acetate (TPA)-responsive elements (TRE). Mitogen-activating protein kinases (MAPK), p38 kinase, stress-activated protein kinase (SAPK), JNK, and transcription factors [early growth response (Egr)-1, specificity protein (SP)-1] are activated through a series of unidentified pathways. Subsequently, this variety of molecules may activate nuclear factor (NF)-kB and/or gene expression through other mechanisms. Members of the integrin family can also regulate the action of NF-kB by means of the activation of an inhibitor of NF-kB kinase (IKK) that mediates the release of NF-kB from the inhibitor of NF-kB (IkB), and the subsequent translocation of NF-kB to the nucleus. Activation of members of the MAPK family and NF-kB can induce transcription of early response genes and bind to stretch response elements (SRE) to activate transcription.