Both isoforms of ACE lack the RGD motif present in the extracellular domain of ACE2 and we therefore hypothesised that ACE would not bind integrins. Cells over-expressing tACE were used to examine any potential interaction between ACE and ITGB1. Immunoprecipitation revealed that ACE does bind ITGB1 ( Figure 2A ) and that ACE also binds ITGA5 similarly ( Figure 2B ). In order to clarify any role of the RGD motif in the binding of ACE2 to integrins, cross-linked immunoprecipitation was repeated in Huh7 cells, in the presence and absence of an RGD peptide. The interaction between ACE2 and ITGB1 was not blocked by the presence of RGD peptide ( Figure 2C ). Hence, the ability of ACE2 to bind the RGD-independent integrin subunit ITGA2 was additionally investigated. ACE2 bound ITGA2 at a comparable level to ITGA5 and ITGB1 ( Figure 2D ).