Inositol monophosphatase 1

IMPA1 has been shown to interact with Bergmann glial S100B{{cite journal |vauthors=Vig PJ, Shao Q, Subramony SH, Lopez ME, Safaya E | title = Bergmann glial S100B activates myo-inositol monophosphatase 1 and Co-localizes to purkinje cell vacuoles in SCA1 transgenic mice | journal = Cerebellum | volume = 8 | issue = 3 | pages = 231–44 |date=September 2009 | pmid = 19593677 | pmc = 3351107 | doi = 10.1007/s12311-009-0125-5 }} and calbindin.{{cite journal |vauthors=Schmidt H, Schwaller B, Eilers J | title = Calbindin D28k targets myo-inositol monophosphatase in spines and dendrites of cerebellar Purkinje neurons | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 102 | issue = 16 | pages = 5850–5 |date=April 2005 | pmid = 15809430 | pmc = 556286 | doi = 10.1073/pnas.0407855102 | bibcode = 2005PNAS..102.5850S | doi-access = free }}{{cite journal |vauthors=Berggard T, Szczepankiewicz O, Thulin E, Linse S | title = Myo-inositol monophosphatase is an activated target of calbindin D28k | journal = J. Biol. Chem. | volume = 277 | issue = 44 | pages = 41954–9 |date=November 2002 | pmid = 12176979 | doi = 10.1074/jbc.M203492200 | doi-access = free }}

L-690,330 is a competitive inhibitor of IMPase activity with very good activity in vitro however with limited bioavailability in vivo.{{cite journal |vauthors=Atack JR, Cook SM, Watt AP, Fletcher SR, Ragan CI | title = In vitro and in vivo inhibition of inositol monophosphatase by the bisphosphonate L-690,330 | journal = J. Neurochem. | volume = 60 | issue = 2 | pages = 652–8 |date=February 1993 | pmid = 8380439 | doi = 10.1111/j.1471-4159.1993.tb03197.x| s2cid = 23498954 }} 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.{{cite journal |vauthors=Atack JR, Prior AM, Fletcher SR, Quirk K, McKernan R, Ragan CI | title = Effects of L-690,488, a prodrug of the bisphosphonate inositol monophosphatase inhibitor L-690,330, on phosphatidylinositol cycle markers | journal = J. Pharmacol. Exp. Ther. | volume = 270 | issue = 1 | pages = 70–6 |date=July 1994 | doi = 10.1016/S0022-3565(25)22382-5 | pmid = 8035344 }}

Inhibition of IMPA1 activity can have pleiotropic effects on cellular function, including altering phosphoinositide signalling,{{cite journal |vauthors=King JS, Teo R, Ryves J, Reddy JV, Peters O, Orabi B, Hoeller O, Williams RS, Harwood AJ | title = The mood stabiliser lithium suppresses PIP3 signalling in Dictyostelium and human cells | journal = Dis Models Mech | volume = 2 | issue = 5–6 | pages = 306–12 | year = 2009 | pmid = 19383941 | pmc = 2675811 | doi = 10.1242/dmm.001271 }} autophagy, apoptosis,{{cite journal |vauthors=Sarkar S, Rubinsztein DC | title = Inositol and IP3 levels regulate autophagy: biology and therapeutic speculations | journal = Autophagy | volume = 2 | issue = 2 | pages = 132–4 | year = 2006 | pmid = 16874097 | doi = 10.4161/auto.2387| doi-access = free }} and other effects.

Initially it was noticed that several drugs useful in treatment of bipolar disorder such as lithium, carbamazepine and valproic acid had a common mechanism of action on enzymes in the phosphatidylinositol signalling pathway{{cite journal |vauthors=Williams RS, Cheng L, Mudge AW, Harwood AJ | title = A common mechanism of action for three mood-stabilizing drugs | journal = Nature | volume = 417 | issue = 6886 | pages = 292–5 |date=May 2002 | pmid = 12015604 | doi = 10.1038/417292a | bibcode = 2002Natur.417..292W | s2cid = 4302048 }} and the inositol depletion hypothesis for the pathophysiology of bipolar 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.

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• {{cite journal |vauthors=Atack JR, Schapiro MB |title=Inositol monophosphatase activity in normal, Down syndrome and dementia of the Alzheimer type CSF |journal=Neurobiol. Aging |volume=23 |issue= 3 |pages= 389–396 |year= 2002 |pmid= 11959401 |doi=10.1016/S0197-4580(01)00335-9 |s2cid=24701473 }}
• {{cite journal |vauthors=Berggard T, Szczepankiewicz O, Thulin E, Linse S |title=Myo-inositol monophosphatase is an activated target of calbindin D28k |journal=J. Biol. Chem. |volume=277 |issue= 44 |pages= 41954–41959 |year= 2003 |pmid= 12176979 |doi= 10.1074/jbc.M203492200 |doi-access= free }}
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• {{cite journal | author=Sjøholt G |title=Examination of IMPA1 and IMPA2 genes in manic-depressive patients: association between IMPA2 promoter polymorphisms and bipolar disorder |journal=Mol. Psychiatry |volume=9 |issue= 6 |pages= 621–629 |year= 2005 |pmid= 14699425 |doi= 10.1038/sj.mp.4001460 | author2=Ebstein RP | author3=Lie RT | last4=Berle | first4=J Ø | last5=Mallet | first5=J | last6=Deleuze | first6=J F | last7=Levinson | first7=D F | last8=Laurent | first8=C | last9=Mujahed | first9=M |s2cid=28747842 | doi-access= }}
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• {{cite journal | author=Rual JF |title=Towards a proteome-scale map of the human protein-protein interaction network |journal=Nature |volume=437 |issue= 7062 |pages= 1173–1178 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 | author2=Venkatesan K | author3=Hao T | last4=Hirozane-Kishikawa | first4=Tomoko | last5=Dricot | first5=Amélie | last6=Li | first6=Ning | last7=Berriz | first7=Gabriel F. | last8=Gibbons | first8=Francis D. | last9=Dreze | first9=Matija |bibcode=2005Natur.437.1173R |s2cid=4427026 }}
• {{cite journal | author=Ohnishi T |title=Spatial expression patterns and biochemical properties distinguish a second myo-inositol monophosphatase IMPA2 from IMPA1 |journal=J. Biol. Chem. |volume=282 |issue= 1 |pages= 637–646 |year= 2007 |pmid= 17068342 |doi= 10.1074/jbc.M604474200 | author2=Ohba H | author3=Seo KC | last4=Im | first4=J. | last5=Sato | first5=Y. | last6=Iwayama | first6=Y. | last7=Furuichi | first7=T. | last8=Chung | first8=S.-K. | last9=Yoshikawa | first9=T. | doi-access=free }}

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• [https://www.ebi.ac.uk/pdbe/pdbe-kb/proteins/P29218 PDBe-KB] provides an overview of all the structure information available in the PDB for Human Inositol monophosphatase 1

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Category:Biology of bipolar disorder

Category:EC 3.1.3