Comparison between plasma membrane Ca2+ and Na,K-ATPases: short review.
1. This paper is a short review of the comparative biochemistry of the Na,K-ATPase and Ca2+-ATPase of plasma membranes. 2. The two ATPases share the same biphasic activation by ATP. Ca2+-ATPase activation by ATP is strongly affected by calmodulin. 3. The possibility of Mg2+ occlusion is proposed in connection with low-affinity activation by ATP. 4. Both ATPases are activated by alkaline earth metal ions and display phosphatase activity toward p-nitrophenylphosphate for which Ca2+-ATPase is strongly dependent on K+ and regulated by calmodulin. 5. The requirements for ligands of the phosphatase activity of both ATPases are strikingly similar except for the effect of calmodulin. 6. Both ATPases are inhibited by vanadate and for both the effect of vanadate is modulated by Mg2+ and K+ in the same way. 7. These similarities indicate that, although Ca2+-ATPase and Na,K-ATPase are different enzymes, their mechanisms of action may have more features in common than previously thought.
Garrahan
P J
PJ
Instituto de Química y Fisicoquímica Biológicas UBA-CONICET, Facultad de Farmacia y Bioquímica, Buenos Aires, Argentina.
Rega
A F
AF
D000252:Calcium-Transporting ATPases / Q000378:metabolism*; D002147:Calmodulin / Q000494:pharmacology; D002462:Cell Membrane / Q000201:enzymology*; D004721:Endoplasmic Reticulum / Q000201:enzymology; D004789:Enzyme Activation / Q000187:drug effects; D000254:Sodium-Potassium-Exchanging ATPase / Q000378:metabolism*; D014638:Vanadates / Q000494:pharmacology
D002147:Calmodulin; D014638:Vanadates; D000252:Calcium-Transporting ATPases; D000254:Sodium-Potassium-Exchanging ATPase