Fig. 5: Inhibition of Kv1.5 by H2S requires NO formation and nitrosylation of hKv1.5. | Communications Biology

Fig. 5: Inhibition of Kv1.5 by H2S requires NO formation and nitrosylation of hKv1.5.

From: Inhibition of the voltage-gated potassium channel Kv1.5 by hydrogen sulfide attenuates remodeling through S-nitrosylation-mediated signaling

Fig. 5

a Cumulative data showing the percentage inhibition (mean ± s.e.m.) induced by the H2S donor NaHS on normalized hKv1.5 peak amplitude in HEK293, currents evoked by repeated step depolarizations from −70 mV to +50 mV (100 ms duration, 0.2 Hz) in untreated (n = 8), L-NAME (1 mM; 1 h, 37 °C; n = 8) or triciribine pre-treated cells (5 µM; 1 h, 37 °C; n = 8) **P < 0.01, ***P < 0.001. b, c Example time-series plots showing the lack of effect of H2S donor NaHS during perfusion on normalized peak current amplitudes obtained from either L-NAME or Triciribine pre-treated HEK293 cell stably expressing human Kv1.5 (hKv1.5). Inset shows example currents before and during NaHS exposure (horizontal scale bar = 50 ms). d Representative western blots showing the time dependent effect of NaHS treatment on eNOS phosphorylation at Ser 1177 (upper), eNOS expression (middle). β-actin used as loading control (lower). Cell lysates obtained from H2S treated HEK293 cell stably expressing hKv1.5 at the time indicated, control represent cells not exposed to H2S. e Western blot showing detection of Kv1.5 nitrosylation via the biotin-switch assay.

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