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Science 25 November 1988:
Vol. 242. no. 4882, pp. 1176 - 1178
DOI: 10.1126/science.2847317

Articles

Science, Vol 242, Issue 4882, 1176-1178
Copyright © 1988 by American Association for the Advancement of Science


articles

Inositol 1,3,4,5-tetrakisphosphate induces Ca2+ sequestration in rat liver cells

TD Hill, NM Dean, and AL Boynton

Cancer Research Center of Hawaii, University of Hawaii, Honolulu 96813.

Inositol 1,4,5-trisphosphate [I(1,4,5)P3] is a second messenger generated along with diacylglycerol upon the binding of various physiological agents with their cell surface receptors. I(1,4,5)P3 mobilizes Ca2+ from intracellular storage sites through a receptor-coupled mechanism, and the subsequent increased intracellular free calcium ion concentration [( Ca2+]i) activates a multitude of cellular responses. Electropermeabilized neoplastic rat liver epithelial (261B) cells were used to study Ca2+ sequestration, a process that reverses the elevated [Ca2+]i to resting levels and replenishes intracellular Ca2+ pools. Although I (1,4,5)P3-mobilized Ca2+ is readily sequestered into storage pools by the action of Ca2+-adenosine triphosphatases, Ca2+ mobilized by addition of the nonmetabolized inositol trisphosphate isomer I(2,4,5)P3 is not sequestered, suggesting that metabolism is necessary to eliminate the stimulus for Ca2+ release. Several inositol phosphate compounds were examined for their ability to lower the buffer [Ca2+] to determine if a specific I(1,4,5)P3 metabolite might be involved in stimulating Ca2+ sequestration; of these, I(1,3,4,5)P4 alone was found to induce Ca2+ sequestration, demonstrating a physiological role for this inositol trisphosphate metabolite.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Arabidopsis Inositol Polyphosphate 6-/3-Kinase (AtIpk2beta) Is Involved in Axillary Shoot Branching via Auxin Signaling.
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Plant Physiology 144, 942-951
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A Role of Arabidopsis Inositol Polyphosphate Kinase, AtIPK2{alpha}, in Pollen Germination and Root Growth.
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Arabidopsis Inositol Polyphosphate 6-/3-Kinase Is a Nuclear Protein That Complements a Yeast Mutant Lacking a Functional ArgR-Mcm1 Transcription Complex.
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Structure-Function Relationships of the Mouse Gap1m. DETERMINATION OF THE INOSITOL 1,3,4,5-TETRAKISPHOSPHATE-BINDING DOMAIN.
M. Fukuda and K. Mikoshiba (1996)
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IP3 receptor: localization to plasma membrane of T cells and cocapping with the T cell receptor.
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Molecular cloning and expression of a complementary DNA for inositol 1,4,5-trisphosphate 3-kinase.
K. Choi, H. Kim, S. Lee, K. Moon, S. Sim, J. Kim, H. Chung, and S. Rhee (1990)
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Fibroblasts transformed with v-src show enhanced formation of an inositol tetrakisphosphate.
R. Johnson, W. Wasilenko, R. Mattingly, M. Weber, and J. Garrison (1989)
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Science. ISSN 0036-8075 (print), 1095-9203 (online)