Skip to main content
PMC home page
Biochemical Journal logoLink to Biochemical Journal
. 1992 Jun 15;284(Pt 3):749–754. doi: 10.1042/bj2840749

cDNA cloning of human and rat brain myo-inositol monophosphatase. Expression and characterization of the human recombinant enzyme.

G McAllister 1, P Whiting 1, E A Hammond 1, M R Knowles 1, J R Atack 1, F J Bailey 1, R Maigetter 1, C I Ragan 1
PMCID: PMC1132602  PMID: 1377913

Abstract

Inositol monophosphatase (EC 3.1.3.25) is a key enzyme in the phosphoinositide cell-signalling system. Its role is to provide inositol required for the resynthesis of phosphatidylinositol and polyphosphoinositides. It is the probable pharmacological target for lithium action in brain. Using probes derived from the bovine inositol monophosphatase cDNA we have isolated cDNA clones encoding the human and rat brain enzymes. The enzyme is highly conserved in all three species (79% identical). The coding region of the human cDNA was inserted into a bacterial expression vector. The expressed recombinant enzyme was purified and its biochemical properties examined. The human enzyme is very similar to the bovine enzyme.

Full text

PDF
749

Images in this article

752Fig. 4.
on p.752
752Fig. 5.
on p.752

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Abdel-Latif A. A. Calcium-mobilizing receptors, polyphosphoinositides, and the generation of second messengers. Pharmacol Rev. 1986 Sep;38(3):227–272. [PubMed] [Google Scholar]
  2. Aviv H., Leder P. Purification of biologically active globin messenger RNA by chromatography on oligothymidylic acid-cellulose. Proc Natl Acad Sci U S A. 1972 Jun;69(6):1408–1412. doi: 10.1073/pnas.69.6.1408. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Berridge M. J., Downes C. P., Hanley M. R. Neural and developmental actions of lithium: a unifying hypothesis. Cell. 1989 Nov 3;59(3):411–419. doi: 10.1016/0092-8674(89)90026-3. [DOI] [PubMed] [Google Scholar]
  4. Berridge M. J. Inositol trisphosphate and diacylglycerol as second messengers. Biochem J. 1984 Jun 1;220(2):345–360. doi: 10.1042/bj2200345. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976 May 7;72:248–254. doi: 10.1006/abio.1976.9999. [DOI] [PubMed] [Google Scholar]
  6. Chirgwin J. M., Przybyla A. E., MacDonald R. J., Rutter W. J. Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease. Biochemistry. 1979 Nov 27;18(24):5294–5299. doi: 10.1021/bi00591a005. [DOI] [PubMed] [Google Scholar]
  7. Choi K. Y., Kim H. K., Lee S. Y., Moon K. H., Sim S. S., Kim J. W., Chung H. K., Rhee S. G. Molecular cloning and expression of a complementary DNA for inositol 1,4,5-trisphosphate 3-kinase. Science. 1990 Apr 6;248(4951):64–66. doi: 10.1126/science.2157285. [DOI] [PubMed] [Google Scholar]
  8. Diehl R. E., Whiting P., Potter J., Gee N., Ragan C. I., Linemeyer D., Schoepfer R., Bennett C., Dixon R. A. Cloning and expression of bovine brain inositol monophosphatase. J Biol Chem. 1990 Apr 15;265(11):5946–5949. [PubMed] [Google Scholar]
  9. Feinberg A. P., Vogelstein B. "A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity". Addendum. Anal Biochem. 1984 Feb;137(1):266–267. doi: 10.1016/0003-2697(84)90381-6. [DOI] [PubMed] [Google Scholar]
  10. Gee N. S., Ragan C. I., Watling K. J., Aspley S., Jackson R. G., Reid G. G., Gani D., Shute J. K. The purification and properties of myo-inositol monophosphatase from bovine brain. Biochem J. 1988 Feb 1;249(3):883–889. doi: 10.1042/bj2490883. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Geever R. F., Huiet L., Baum J. A., Tyler B. M., Patel V. B., Rutledge B. J., Case M. E., Giles N. H. DNA sequence, organization and regulation of the qa gene cluster of Neurospora crassa. J Mol Biol. 1989 May 5;207(1):15–34. doi: 10.1016/0022-2836(89)90438-5. [DOI] [PubMed] [Google Scholar]
  12. Hallcher L. M., Sherman W. R. The effects of lithium ion and other agents on the activity of myo-inositol-1-phosphatase from bovine brain. J Biol Chem. 1980 Nov 25;255(22):10896–10901. [PubMed] [Google Scholar]
  13. Hawkins A. R., Lamb H. K., Smith M., Keyte J. W., Roberts C. F. Molecular organisation of the quinic acid utilization (QUT) gene cluster in Aspergillus nidulans. Mol Gen Genet. 1988 Oct;214(2):224–231. doi: 10.1007/BF00337715. [DOI] [PubMed] [Google Scholar]
  14. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  15. Lehrach H., Diamond D., Wozney J. M., Boedtker H. RNA molecular weight determinations by gel electrophoresis under denaturing conditions, a critical reexamination. Biochemistry. 1977 Oct 18;16(21):4743–4751. doi: 10.1021/bi00640a033. [DOI] [PubMed] [Google Scholar]
  16. Nishizuka Y. Turnover of inositol phospholipids and signal transduction. Science. 1984 Sep 21;225(4668):1365–1370. doi: 10.1126/science.6147898. [DOI] [PubMed] [Google Scholar]
  17. Ragan C. I., Watling K. J., Gee N. S., Aspley S., Jackson R. G., Reid G. G., Baker R., Billington D. C., Barnaby R. J., Leeson P. D. The dephosphorylation of inositol 1,4-bisphosphate to inositol in liver and brain involves two distinct Li+-sensitive enzymes and proceeds via inositol 4-phosphate. Biochem J. 1988 Jan 1;249(1):143–148. doi: 10.1042/bj2490143. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Ross T. S., Tait J. F., Majerus P. W. Identity of inositol 1,2-cyclic phosphate 2-phosphohydrolase with lipocortin III. Science. 1990 May 4;248(4955):605–607. doi: 10.1126/science.2159184. [DOI] [PubMed] [Google Scholar]
  19. Saiki R. K., Gelfand D. H., Stoffel S., Scharf S. J., Higuchi R., Horn G. T., Mullis K. B., Erlich H. A. Primer-directed enzymatic amplification of DNA with a thermostable DNA polymerase. Science. 1988 Jan 29;239(4839):487–491. doi: 10.1126/science.2448875. [DOI] [PubMed] [Google Scholar]
  20. Sanger F., Nicklen S., Coulson A. R. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463–5467. doi: 10.1073/pnas.74.12.5463. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Takimoto K., Okada M., Matsuda Y., Nakagawa H. Purification and properties of myo-inositol-1-phosphatase from rat brain. J Biochem. 1985 Aug;98(2):363–370. doi: 10.1093/oxfordjournals.jbchem.a135290. [DOI] [PubMed] [Google Scholar]
  22. Yano R., Nagai H., Shiba K., Yura T. A mutation that enhances synthesis of sigma 32 and suppresses temperature-sensitive growth of the rpoH15 mutant of Escherichia coli. J Bacteriol. 1990 Apr;172(4):2124–2130. doi: 10.1128/jb.172.4.2124-2130.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. York J. D., Majerus P. W. Isolation and heterologous expression of a cDNA encoding bovine inositol polyphosphate 1-phosphatase. Proc Natl Acad Sci U S A. 1990 Dec;87(24):9548–9552. doi: 10.1073/pnas.87.24.9548. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES