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Am J Physiol Cell Physiol 280: C1027-C1030, 2001;
0363-6143/01 $5.00
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Vol. 280, Issue 4, C1027-C1030, April 2001

RAPID COMMUNICATION
Caloxin: a novel plasma membrane Ca2+ pump inhibitor

Jyoti Chaudhary1, Mandeep Walia1, Jaswinder Matharu1, Emanuel Escher2, and Ashok K. Grover1

1 Departments of Medicine and Biology, McMaster University, Hamilton, Ontario, Canada L8N 3Z5; and 2 Department of Pharmacology, Sherbrooke University, Sherbrooke, Quebec, Canada J1H 5N4

Plasma membrane (PM) Ca2+ pump is a Ca2+-Mg2+-ATPase that expels Ca2+ from cells to help them maintain low concentrations of cytosolic Ca2+. There are no known extracellularly acting PM Ca2+ pump inhibitors, as digoxin and ouabain are for Na+ pump. In analogy with digoxin, we define caloxins as extracellular PM Ca2+ pump inhibitors and describe caloxin 2A1. Caloxin 2A1 is a peptide obtained by screening a random peptide phage display library for binding to the second extracellular domain (residues 401-413) sequence of PM Ca2+ pump isoform 1b. Caloxin 2A1 inhibits Ca2+-Mg2+-ATPase in human erythrocyte leaky ghosts, but it does not affect basal Mg2+-ATPase or Na+-K+-ATPase in the ghosts or Ca2+-Mg2+-ATPase in the skeletal muscle sarcoplasmic reticulum. Caloxin 2A1 also inhibits Ca2+-dependent formation of the 140-kDa acid-stable acylphosphate, which is a partial reaction of this enzyme. Consistent with inhibition of the PM Ca2+ pump in vascular endothelium, caloxin 2A1 produces an endothelium-dependent relaxation that is reversed by NG-nitro-L-arginine methyl ester. Thus caloxin 2A1 is a novel PM Ca2+ pump inhibitor selected for binding to an extracellular domain.

adenosine 5'-triphosphatase; plasma membrane calcium ATPase; transport; calcium; endothelium; erythrocytes; homeostasis; signal transduction


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