View source for Biology:Inositol monophosphatase 1

{{Short description|Protein-coding gene in the species Homo sapiens}}
{{Infobox_gene}}
'''Inositol monophosphatase 1''' is an [[Biology:Enzyme|enzyme]] that in humans is encoded by the ''IMPA1'' [[Biology:Gene|gene]].<ref name="pmid1377913">{{cite journal |vauthors=McAllister G, Whiting P, Hammond EA, Knowles MR, Atack JR, Bailey FJ, Maigetter R, Ragan CI | title = cDNA cloning of human and rat brain myo-inositol monophosphatase. Expression and characterization of the human recombinant enzyme | journal = Biochem J | volume = 284 | issue =  3| pages = 749–54 |date=Aug 1992 | pmid = 1377913 | pmc = 1132602 | doi =  10.1042/bj2840749}}</ref><ref name="entrez">{{cite web | title = Entrez Gene: IMPA1 inositol(myo)-1(or 4)-monophosphatase 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3612}}</ref>

== Interacting partners ==

IMPA1 has been shown to interact with Bergmann glial [[Biology:S100B|S100B]]<ref name="pmid19593677">{{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 }}</ref> and [[Biology:Calbindin|calbindin]].<ref name="pmid15809430">{{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 }}</ref><ref name="pmid12176979">{{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 }}</ref>

== Chemical inhibitors ==

L-690,330 is a competitive inhibitor of IMPase activity with very good activity [[In vitro|in vitro]] however with limited [[Chemistry:Bioavailability|bioavailability]] [[Biology:In vivo|in vivo]].<ref name="pmid8380439">{{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 }}</ref> 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 [[Chemistry:Inositol|inositol]] demonstrating the activity of this inhibitor in tissue.<ref name="pmid8035344">{{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 | pmid = 8035344 }}</ref>

Inhibition of IMPA1 activity can have pleiotropic effects on cellular function, including altering phosphoinositide signalling,<ref name="pmid19383941">{{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 }}</ref> [[Biology:Autophagy|autophagy]], [[Biology:Apoptosis|apoptosis]],<ref name="pmid16874097">{{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 }}</ref> and other effects.

== Bipolar disorder ==

Initially it was noticed that several drugs useful in treatment of bipolar disorder such as [[Chemistry:Lithium carbonate|lithium]], [[Chemistry:Carbamazepine|carbamazepine]] and valproic acid had a common mechanism of action on enzymes in the [[Chemistry:Phosphatidylinositol|phosphatidylinositol]] signalling pathway<ref name="pmid12015604">{{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 }}</ref> 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|in vitro]] studies.

==References==
{{reflist}}

==Further reading==
{{refbegin|35em}}
*{{cite journal  |vauthors=Bone R, Springer JP, Atack JR |title=Structure of inositol monophosphatase, the putative target of lithium therapy |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 21 |pages= 10031–10035 |year= 1992 |pmid= 1332026 |doi=10.1073/pnas.89.21.10031  | pmc=50271  |bibcode=1992PNAS...8910031B |doi-access=free }}
*{{cite journal  |vauthors=Hallcher LM, Sherman WR |title=The effects of lithium ion and other agents on the activity of myo-inositol-1-phosphatase from bovine brain |journal=J. Biol. Chem. |volume=255 |issue= 22 |pages= 10896–901 |year= 1981 |doi=10.1016/S0021-9258(19)70391-3 |pmid= 6253491 |doi-access=free }}
*{{cite journal  | author=Bone R |title=Structural analysis of inositol monophosphatase complexes with substrates |journal=Biochemistry |volume=33 |issue= 32 |pages= 9460–9467 |year= 1994 |pmid= 8068620 |doi=10.1021/bi00198a011  | author2=Frank L  | author3=Springer JP  | last4=Pollack  | first4=Scott J.  | last5=Osborne  | first5=Sallyann  | last6=Atack  | first6=John R.  | last7=Knowles  | first7=Michael R.  | last8=McAllister  | first8=George  | last9=Ragan  | first9=C. Ian  }}
*{{cite journal  |vauthors=Bone R, Frank L, Springer JP, Atack JR |title=Structural studies of metal binding by inositol monophosphatase: evidence for two-metal ion catalysis |journal=Biochemistry |volume=33 |issue= 32 |pages= 9468–9476 |year= 1994 |pmid= 8068621 |doi=10.1021/bi00198a012  }}
*{{cite journal  | author=Ganzhorn AJ |title=The contribution of lysine-36 to catalysis by human myo-inositol monophosphatase |journal=Biochemistry |volume=35 |issue= 33 |pages= 10957–10966 |year= 1996 |pmid= 8718889 |doi= 10.1021/bi9603837  | author2=Lepage P  | author3=Pelton PD  | last4=Strasser  | first4=Françoise  | last5=Vincendon  | first5=Pascale  | last6=Rondeau  | first6=Jean-Michel }}
*{{cite journal  |vauthors=Parthasarathy L, Parthasarathy R, Vadnal R |title=Molecular characterization of coding and untranslated regions of rat cortex lithium-sensitive myo-inositol monophosphatase cDNA |journal=Gene |volume=191 |issue= 1 |pages= 81–87 |year= 1997 |pmid= 9210592 |doi=10.1016/S0378-1119(97)00045-0  }}
*{{cite journal  | author=Sjøholt G |title=Genomic structure and chromosomal localization of a human myo-inositol monophosphatase gene (IMPA) |journal=Genomics |volume=45 |issue= 1 |pages= 113–122 |year= 1997 |pmid= 9339367 |doi= 10.1006/geno.1997.4862  | author2=Molven A  | author3=Løvlie R  | last4=Wilcox  | first4=A  | last5=Sikela  | first5=JM  | last6=Steen  | first6=VM }}
*{{cite journal  | author=Nemanov L |title=Effect of bipolar disorder on lymphocyte inositol monophosphatase mRNA levels |journal= The International Journal of Neuropsychopharmacology|volume=2 |issue= 1 |pages= 25–29 |year=  1999|pmid= 11281967 |doi= 10.1017/S1461145799001315  | author2=Ebstein RP  | author3=Belmaker RH  | last4=Osher  | first4=Yamima  | last5=Agam  | first5=Galila |s2cid=16964945 |doi-access=}}
*{{cite journal  | author=Bahn JH |title=Production of monoclonal antibodies and immunohistochemical studies of brain myo-inositol monophosphate phosphatase |journal=Mol. Cells |volume=13 |issue= 1 |pages= 21–7 |year= 2002 |pmid= 11911470 | author2=Kim AY  | author3=Jang SH  | last4=Lee  | first4=BR  | last5=Ahn  | first5=JY  | last6=Joo  | first6=HM  | last7=Kan  | first7=TC  | last8=Won  | first8=MH  | last9=Kwon  | first9=HY  |doi=10.1016/S1016-8478(23)14999-5 | doi-access=free  }}
*{{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 }}
*{{cite journal  | author=Strausberg RL |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–16903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241  | author2=Feingold EA  | author3=Grouse LH  | last4=Derge  | first4=JG  | last5=Klausner  | first5=RD  | last6=Collins  | first6=FS  | last7=Wagner  | first7=L  | last8=Shenmen  | first8=CM  | last9=Schuler  | first9=GD |bibcode=2002PNAS...9916899M |doi-access=free }}
*{{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=  }}
*{{cite journal  | author=Gerhard DS |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–2127 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504  | pmc=528928  | author2=Wagner L  | author3=Feingold EA  | last4=Shenmen  | first4=CM  | last5=Grouse  | first5=LH  | last6=Schuler  | first6=G  | last7=Klein  | first7=SL  | last8=Old  | first8=S  | last9=Rasooly  | first9=R }}
*{{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  }}
{{refend}}

== External links ==
* [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

{{PDB Gallery|geneid=3612}}
{{Esterases}}
{{Enzymes}}

[[Category:EC 3.1.3]]

{{Sourceattribution|Inositol monophosphatase 1}}