L-690,330 is a competitive inhibitor of IMPase activity with very good activity in vitro however with limited bioavailabilityin vivo. Due to its increased specificity compared to Lithium, L-690,330 has been used extensively in characterizing the results of IMPase inhibition in various cell culture models. L-690,488, a prodrug or L-690,330, has also been developed which has greater cell permeability. Treatment of cortical slices with L-690,488 resulted in accumulation of inositol demonstrating the activity of this inhibitor in tissue.
Initially it was noticed that several drugs useful in treatment of biopolar disorder such as lithium, carbamazepine and valproic acid had a common mechanism of action on enzymes in the phosphatidylinositol signalling pathway and the inositol depletion hypothesis for the pathophysiology of biopolar disorder was suggested. Intensive research has so far not confirmed this hypothesis, partly because lithium can also act on a number of other enzymes in this pathway, complicating results from in vitro studies.
^Berggard T, Szczepankiewicz O, Thulin E, Linse S (November 2002). "Myo-inositol monophosphatase is an activated target of calbindin D28k". J. Biol. Chem. 277 (44): 41954–9. doi:10.1074/jbc.M203492200. PMID12176979.
Hallcher LM, Sherman WR (1981). "The effects of lithium ion and other agents on the activity of myo-inositol-1-phosphatase from bovine brain". J. Biol. Chem. 255 (22): 10896–901. PMID6253491.
Bone R, Frank L, Springer JP, et al. (1994). "Structural analysis of inositol monophosphatase complexes with substrates". Biochemistry. 33 (32): 9460–9467. doi:10.1021/bi00198a011. PMID8068620.
Bone R, Frank L, Springer JP, Atack JR (1994). "Structural studies of metal binding by inositol monophosphatase: evidence for two-metal ion catalysis". Biochemistry. 33 (32): 9468–9476. doi:10.1021/bi00198a012. PMID8068621.
Ganzhorn AJ, Lepage P, Pelton PD, et al. (1996). "The contribution of lysine-36 to catalysis by human myo-inositol monophosphatase". Biochemistry. 35 (33): 10957–10966. doi:10.1021/bi9603837. PMID8718889.
Parthasarathy L, Parthasarathy R, Vadnal R (1997). "Molecular characterization of coding and untranslated regions of rat cortex lithium-sensitive myo-inositol monophosphatase cDNA". Gene. 191 (1): 81–87. doi:10.1016/S0378-1119(97)00045-0. PMID9210592.
Sjøholt G, Molven A, Løvlie R, et al. (1997). "Genomic structure and chromosomal localization of a human myo-inositol monophosphatase gene (IMPA)". Genomics. 45 (1): 113–122. doi:10.1006/geno.1997.4862. PMID9339367.
Nemanov L, Ebstein RP, Belmaker RH, et al. (1999). "Effect of bipolar disorder on lymphocyte inositol monophosphatase mRNA levels". The International Journal of Neuropsychopharmacology. 2 (1): 25–29. doi:10.1017/S1461145799001315. PMID11281967.
Bahn JH, Kim AY, Jang SH, et al. (2002). "Production of monoclonal antibodies and immunohistochemical studies of brain myo-inositol monophosphate phosphatase". Mol. Cells. 13 (1): 21–7. PMID11911470.
Berggard T, Szczepankiewicz O, Thulin E, Linse S (2003). "Myo-inositol monophosphatase is an activated target of calbindin D28k". J. Biol. Chem. 277 (44): 41954–41959. doi:10.1074/jbc.M203492200. PMID12176979.
Sjøholt G, Ebstein RP, Lie RT, et al. (2005). "Examination of IMPA1 and IMPA2 genes in manic-depressive patients: association between IMPA2 promoter polymorphisms and bipolar disorder". Mol. Psychiatry. 9 (6): 621–629. doi:10.1038/sj.mp.4001460. PMID14699425.
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–1178. doi:10.1038/nature04209. PMID16189514.
Ohnishi T, Ohba H, Seo KC, et al. (2007). "Spatial expression patterns and biochemical properties distinguish a second myo-inositol monophosphatase IMPA2 from IMPA1". J. Biol. Chem. 282 (1): 637–646. doi:10.1074/jbc.M604474200. PMID17068342.