Hydrogen Sulfide Is a Regulator of Hemoglobin Oxygen-Carrying Capacity via Controlling 2,3-BPG Production in Erythrocytes

Figure 7

H₂S modulation of Hb and BPGM translocation and the role of S-sulfhydration in these processes. (a–d) The effects of H₂S and iodoacetamide on Hb binding to the membrane and BPGM release from the membrane in mouse and human erythrocyte ghost membranes. Hb binding to the membrane (a) and BPGM release from the membrane to the cytosol (b) in the mouse erythrocyte membrane ghost, which was treated with Hb and different concentrations of GYY4137 in the presence or absence of iodoacetamide (IAM). Hb binding to the membrane (c) and BPGM release from the membrane to the cytosol (d) in the human erythrocyte membrane ghost, which was treated with Hb and different concentrations of GYY4137 in the presence or absence of iodoacetamide (IAM). Data are expressed as (). , , , and . (e, f) Representative images of Hb and BPGM S-sulfhydration in erythrocytes of WT and Cse^-/- mice. WT and Cse^-/- mice were administered with saline or GYY4137 (50 mg/kg). Blood samples were collected 24 h after treatment. Erythrocytes were isolated for the determination of S-sulfhydration of Hb (e) and BPGM (f) using the biotin-switch technique. (g, h) Representative images of S-sulfhydration of Hb and BPGM in cultured human erythrocytes. Isolated human erythrocytes were treated with GYY4137 (500 μM) for 6 h and then were harvested for determination of S-sulfhydration of Hb (g) and BPGM (h) using the biotin-switch technique.

(a)

(b)

(c)

(d)

(e)

(f)

(g)

(h)