[The involvement of nitric oxide in formation of hemoglobin oxygen-binding properties].
The analysis of literature and results of our investigations indicate the possible involvement of L-arginine-nitric oxide (NO) system in formation of blood oxygen-carrying capacity. In reaction with hemoglobin NO forms methemoglobin, nitrosyl-hemoglobin (HbFe2+NO) and S-nitrosohemoglobin (SNO-Hb). The NO-hemoglobin derivatives have the various biological functions (NO transport, storage, elimination etc.) and are involved in the genesis of different pathologic conditions. The presence of different NO-hemoglobin derivatives can differently influence on the whole blood hemoglobin-oxygen affinity (HOA): methemoglobin and SNO-Hb increases, and HbFe2+NO decreases it. Their effect on the blood oxygen-binding properties may be important for the gas exchange processes. At the level of lung capillaries such effect may be the additional mechanism promoting a blood oxygenation, and in the systemic microcirculation it may optimize blood desaturation and hence the tissue oxygen delivery. Blood oxygen-binding properties affect the state of L-arginine-NO system, however this system also may determine HOA through the intraerythrocytic regulatory mechanisms, oxygen-dependent nature of NO generation, regulation of vascular tone and effect of peroxynitrite.
Zinchuk
V V
VV
Grodno Medical University, Belarus.
D000818:Animals; D001120:Arginine / Q000378:metabolism; D004912:Erythrocytes / Q000378:metabolism*; D006454:Hemoglobins / Q000737:chemistry / Q000378:metabolism* / Q000502:physiology; D008168:Lung / Q000098:blood supply; D008706:Methemoglobin / Q000502:physiology; D009569:Nitric Oxide / Q000737:chemistry / Q000378:metabolism*; D010100:Oxygen / Q000737:chemistry / Q000378:metabolism*; D010108:Oxyhemoglobins / Q000378:metabolism; D011485:Protein Binding
D006454:Hemoglobins; D010108:Oxyhemoglobins; C103574:S-nitrosohemoglobin; C008657:nitrosyl hemoglobin; D009569:Nitric Oxide; D008706:Methemoglobin; D001120:Arginine; D010100:Oxygen