Fig. 1: HSPB7 and FLNC are up-regulated and interact in biomechanical stress models in mouse.

A Co-immunoprecipitation of HSPB7 and FLNC from MLP KO mouse ventricular tissue. The co-precipitation of the two proteins when precipitating FLNC suggests they form (at least part of) a complex. An isotype control, where a non-specific antibody (rather than for FLNC) raised in the same species was used as a negative control and showed no bands, whereas a positive control using an aliquot of lysate showed clear bands for HSPB7. Molecular mass bands are marked, in units of kDa. One biological repeat, immunoprecipitation experiment performed in triplicate, one representative shown. B Western blots for FLNC and HSPB7 in MLP KO, TAC and IsoPE mouse ventricular tissue. GAPDH was used as the loading control. Sham and saline are the respective specific negative controls for TAC and IsoPE. In all stress treatments, HSPB7 and FLNC are observed at higher levels. Molecular mass bands are marked, in units of kDa. Two biological replicates (i.e. two mice), blots repeated twice, one representative blot shown. C Immunofluorescence of HSPB7 and FLNC from frozen sections of ventricular tissues from TAC, IsoPE and MLP KO mouse models. Sections were stained for FLNC (Green) and HSPB7 (Red). In all stress treatments, the two proteins are up-regulated and co-localise. For quantification of co-localisation see Supplementary Fig. 1. Scale bars are 25 μm. Two biological replicates (i.e. two mice), two images taken from each sample, one representative image shown.