In light of the association of ACE2 with integrins, experiments were performed to determine if ACE2 could elicit integrin signalling. Focal adhesion kinase (FAK) is stimulated early in any integrin signalling cascade. Given that the extracellular domain of ACE2 binds integrin, cells were stimulated with the ectodomain of ACE2. The levels of phosphorylated FAK (pFAK) in the presence and absence of sACE2 were quantified by ELISA. At 0.1 mg/ml sACE2 significantly reduced levels of pFAK in Huh7 cells and in primary myofibroblasts ( Figure 6A and B). No further decrease was observed when cells were incubated with 1 mg/ml ACE2. Downstream translation of this signal to Akt was investigated by quantifying the levels of phosphorylated Akt. Western blot analysis revealed that levels of phosphorylated Akt in Huh7 cells increased in response to stimulation with sACE2 and Ang II for 30 min (data not shown). However, this increase was accounted for by an up-regulation in Akt protein expression ( Figure 6 ). The catalytic product of ACE2, Ang-(1-7), alone did not elicit the same effects as ACE2 ( Figure 6 ).