Elsevier

Metabolism

Volume 44, Issue 7, July 1995, Pages 865-868
Metabolism

Inositol phosphates modulate human red blood cell Ca2+—adenosine triphosphatase activity in vitro by a guanine nucleotide regulatory protein

https://doi.org/10.1016/0026-0495(95)90238-4Get rights and content

Abstract

d-myo-inositol 1,4,5-trisphosphate [lns(1,4,5)P3) inhibits human red blood cell (RBC) Ca2+-stimulable, Mg2+-dependent adenosine triphosphatase (Ca2+-ATPase) activity in vitro. Because we have previously shown that adrenergic receptors exist on the human mature RBC membrane and can modulate Ca2+-ATPase activity, we examined the possibility that a guanine nucleotide regulatory protein (G protein) mediated the lns(1,4,5)P3 effect. Guanosine 5′-O-(3-thiotrisphosphate) (GTPγyS) 10−4 mol/L also inhibited RBC Ca2+-ATPase activity. Pertussis toxin 200 ng/mL blocked the effects of both lns(1,4,5)P3 and GTPγS on Ca2+-ATPase activity. In separate studies, pertussis toxin-catalyzed adenosine diphosphate (ADP) ribosylation was shown to occur in RBC membranes under conditions in which measurements of Ca2+-ATPase activity were performed. When lns(1,4,5)P3 10−7 mol/L and GTPγS 10−6 mol/L were added to membranes concurrently, their inhibitory actions on the enzyme were additive. At greater concentrations of lns(1,4,5)P3 (10−6 to 10−5 mol/L) and GTPγS (10−4 mol/L), the inositol phosphate reversed the inhibitory effect of GTPγS. These observations indicate that the novel effect of lns(1,4,5)P3 on the activity of a plasma membrane Ca2+-ATPase depends at least in part on the action of a pertussis toxin-susceptible G protein.

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    Supported in part by Department of Veterans Affairs Merit Review funding (P.J.D.).

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