cDNA cloning of human and rat brain myo-inositol monophosphatase. Expression and characterization of the human recombinant enzyme
- 15 June 1992
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 284 (3), 749-754
- https://doi.org/10.1042/bj2840749
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.Keywords
This publication has 23 references indexed in Scilit:
- Identity of Inositol 1,2-Cyclic Phosphate 2-Phosphohydrolase with Lipocortin IIIScience, 1990
- Molecular Cloning and Expression of a Complementary DNA for Inositol 1,4,5-Trisphosphate 3-KinaseScience, 1990
- Neural and developmental actions of lithium: A unifying hypothesisCell, 1989
- DNA sequence, organization and regulation of the qa gene cluster of Neurospora crassaJournal of Molecular Biology, 1989
- Primer-Directed Enzymatic Amplification of DNA with a Thermostable DNA PolymeraseScience, 1988
- Turnover of Inositol Phospholipids and Signal TransductionScience, 1984
- Isolation of biologically active ribonucleic acid from sources enriched in ribonucleaseBiochemistry, 1979
- RNA molecular weight determinations by gel electrophoresis under denaturing conditions, a critical reexaminationBiochemistry, 1977
- A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye BindingAnalytical Biochemistry, 1976
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970