Regulation of Cl-dependent K transport by oxy-deoxyhemoglobin transitions in trout red cells.
The oxygenation of trout red cells opens a Cl-dependent K pathway inhibited by furosemide, and by inhibitors of the erythrocyte anion exchanger such as DIDS and niflumic acid. The trigger is the deoxy-oxy conformational change of hemoglobin. The binding of carbon monoxide to heme, which induces a similar conformational change, mimics the effect of oxygen. The possible mechanisms enabling molecular oxygen to control the transport protein are discussed. This oxygenation-activated K transport appears to play a regulatory role in the control of the extracellular K concentration.
Borgese
F
F
Laboratoire Jean Maetz, Département de Biologie Cellulaire et Moléculaire du C.E.A., Villefranche-sur-Mer, France.
Motais
R
R
García-Romeu
F
F
D000818:Animals; D002248:Carbon Monoxide / Q000097:blood; D002352:Carrier Proteins / Q000097:blood*; D002712:Chlorides / Q000378:metabolism; D004912:Erythrocytes / Q000378:metabolism*; D006454:Hemoglobins / Q000378:metabolism*; D007700:Kinetics; D009566:Nitrates / Q000097:blood; D009584:Nitrogen / Q000097:blood; D010100:Oxygen / Q000097:blood; D010108:Oxyhemoglobins / Q000378:metabolism*; D011188:Potassium / Q000097:blood*; D027981:Symporters; D014337:Trout / Q000097:blood; D000096922:K Cl- Cotransporters
D002248:Carbon Monoxide; D002352:Carrier Proteins; D002712:Chlorides; D006454:Hemoglobins; D009566:Nitrates; D009584:Nitrogen; D010100:Oxygen; D010108:Oxyhemoglobins; D011188:Potassium; D027981:Symporters; D000096922:K Cl- Cotransporters; C100003:deoxyhemoglobin