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Volume 270, Number 11, Issue of March 17, 1995 pp. 5818-5822
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
Inorganic Polyphosphate in Mammalian Cells and Tissues

(Received for publication, November 30, 1994; and in revised form, January 4, 1995)

Krishnanand D. Kumble ,  Arthur Kornberg

Inorganic polyphosphate (polyP), a linear polymer of hundreds of orthophosphate (P(i)) residues linked by high-energy, phosphoanhydride bonds, has been identified and measured in a variety of mammalian cell lines and tissues by unambiguous enzyme methods. Subpicomole amounts of polyP (0.5 pmol/100 µg of protein) were determined by its conversion to ATP by Escherichia coli polyphosphate kinase and, alternatively, to P(i) by Saccharomyces cerevisiae exopolyphosphatase. Levels of 25 to 120 µM (in terms of P(i) residues), in chains 50 to 800 residues long, were found in rodent tissues (brain, heart, kidneys, liver, and lungs) and in subcellular fractions (nuclei, mitochondria, plasma membranes, and microsomes). PolyP in brain was predominantly near 800 residues and found at similar levels pre- and postnatally. Conversion of P(i) into polyP by cell lines of fibroblasts, T-cells, kidney, and adrenal cells attained levels in excess of 10 pmol per mg of cell protein per h. Synthesis of polyP from P(i) in the medium bypasses intracellular P(i) and ATP pools suggesting the direct involvement of membrane component(s). In confluent PC12 (adrenal pheochromocytoma) cells, polyP turnover was virtually complete in an hour, whereas in fibroblasts there was little turnover in four hours. The ubiquity of polyP and variations in its size, location, and metabolism are indicative of a multiplicity of functions for this polymer in mammalian systems.



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