A saturable receptor for 32P-inositol-l,4,5-trisphosphate in hepatocytes and neutrophils

András Spät, Peter G. Bradford, Jerry S. Mckinney, Ronald P. Rubin, James W. Putney

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Several receptors for neurotransmitters, hormones and growth factors cause accelerated phosphodiesteratic breakdown of poly-phosphoinositides when activated1,2. One of the soluble products of this reaction, inositol-1,4,5-trisphosphate (Ins(l,4,5)P3) is thought to act as a second messenger signalling the release of Ca2+ from intracellular stores3. In support of this hypothesis, several studies have shown that Ins(l,4,5)P3 releases sequestered Ca2+ from permeable cells4-6 and microsomes7+9. On the basis of certain structural requirements for Ca2+-releasing activity by inositol phosphates, it has been postulated that Ins(l,4,5)P3 acts by binding to a specific intracellular receptor, probably on a component of the endoplasmic reticulum10. Here we report that 32P-Ins(l,4,5)P 3 binds to a specific saturable site in permeabilized guinea pig hepatocytes and rabbit neutrophils, and that the properties of this binding site suggest that it is the physiological receptor for Ins(l,4,5)P3.

Original languageEnglish
Pages (from-to)514-516
Number of pages3
Issue number6053
Publication statusPublished - Dec 1 1986

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    Spät, A., Bradford, P. G., Mckinney, J. S., Rubin, R. P., & Putney, J. W. (1986). A saturable receptor for 32P-inositol-l,4,5-trisphosphate in hepatocytes and neutrophils. Nature, 319(6053), 514-516. https://doi.org/10.1038/319514a0