Characterisation of inosine monophosphate dehydrogenase expression during retinal development: Differences between variants and isoforms

International Journal of Biochemistry and Cell Biology

Volumn 40, Issue 9, 2008, Pages 1716-1728

  Gunter, Jennifer H ^a   Thomas, Elaine C ^a   Lengefeld, Nadia ^a   Kruger, Sarah J ^a   Worton, Leah ^a   Gardiner, Edith M ^a   Jones, Alun ^a   Barnett, Nigel L ^a   Whitehead, Jonathan P ^a  

^a UNIVERSITY OF QUEENSLAND   (Australia)

Author keywords

CBS domain; IMPDH; Photoreceptor; Retina; Retinitis pigmentosa

Indexed keywords

GUANOSINE TRIPHOSPHATE; INOSINATE DEHYDROGENASE;

ANIMAL CELL; ANIMAL TISSUE; ARTICLE; CELL DIFFERENTIATION; CONTROLLED STUDY; EMBRYO DEVELOPMENT; ENZYME ANALYSIS; ENZYME LOCALIZATION; NONHUMAN; PERINATAL DEVELOPMENT; PHOTORECEPTOR; PROTEIN EXPRESSION; PROTEIN FUNCTION; RAT; RETINA DEVELOPMENT; RETINITIS PIGMENTOSA; TISSUE DISTRIBUTION;

ANIMALS; ANTIBODY SPECIFICITY; CHO CELLS; CLONING, MOLECULAR; CRICETINAE; CRICETULUS; ENZYME ACTIVATION; GENE EXPRESSION REGULATION, DEVELOPMENTAL; GENE EXPRESSION REGULATION, ENZYMOLOGIC; HUMANS; IMP DEHYDROGENASE; INTRACELLULAR SPACE; ISOENZYMES; MASS SPECTROMETRY; MUTATION; RATS; REPRODUCIBILITY OF RESULTS; RETINA;

MAMMALIA; RATTUS;

EID: 49949152179     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biocel.2007.12.018     Document Type: Article

References (30)

1. Aherne A., Kennan A., Kenna P.F., McNally N., Lloyd D.G., Alberts I.L., et al. On the molecular pathology of neurodegeneration in IMPDH1-based retinitis pigmentosa. Hum. Mol. Genet. 13 (2004) 641-650
2. Bateman A. The structure of a domain common to archaebacteria and the homocystinuria disease protein. Trends Biochem. Sci. 22 (1997) 12-13
3. Bowne S.J., Liu Q., Sullivan L.S., Zhu J., Spellicy C.J., Rickman C.B., et al. Why do mutations in the ubiquitously expressed housekeeping gene IMPDH1 cause retina-specific photoreceptor degeneration?. Invest. Ophthalmol. Vis. Sci. 47 (2006) 3754-3765
4. Bowne S.J., Sullivan L.S., Blanton S.H., Cepko C.L., Blackshaw S., Birch D.G., et al. Mutations in the inosine monophosphate dehydrogenase 1 gene (IMPDH1) cause the RP10 form of autosomal dominant retinitis pigmentosa. Hum. Mol. Genet. 11 (2002) 559-568
5. Bowne S.J., Sullivan L.S., Mortimer S.E., Hedstrom L., Zhu J., Spellicy C.J., et al. Spectrum and frequency of mutations in IMPDH1 associated with autosomal dominant retinitis pigmentosa and Leber congenital amaurosis. Invest. Ophthalmol. Vis. Sci. 47 (2006) 34-42
6. Carr S.F., Papp E., Wu J.C., and Natsumeda Y. Characterization of human type I and type II IMP dehydrogenases. J. Biol. Chem. 268 (1993) 27286-27290
7. Collart F.R., and Huberman E. Cloning and sequence analysis of the human and Chinese hamster inosine-5′-monophosphate dehydrogenase cDNAs. J. Biol. Chem. 263 (1988) 15769-15772
8. Gu J.J., Tolin A.K., Jain J., Huang H., Santiago L., and Mitchell B.S. Targeted disruption of the inosine 5′-monophosphate dehydrogenase type I gene in mice. Mol. Cell Biol. 23 (2003) 6702-6712
9. Hager P.W., Collart F.R., Huberman E., and Mitchell B.S. Recombinant human inosine monophosphate dehydrogenase type I and type II proteins. Purification and characterization of inhibitor binding. Biochem. Pharmacol. 49 (1995) 1323-1329
10. Hedstrom L., and Gan L. IMP dehydrogenase: structural schizophrenia and an unusual base. Curr. Opin. Chem. Biol. 10 (2006) 520-525
11. Ignoul S., and Eggermont J. CBS domains: structure, function, and pathology in human proteins. Am. J. Physiol. Cell Physiol. 289 (2005) C1369-C1378
12. Jackson R.C., Weber G., and Morris H.P. IMP dehydrogenase, an enzyme linked with proliferation and malignancy. Nature 256 (1975) 331-333
13. Ji Y., Gu J., Makhov A.M., Griffith J.D., and Mitchell B.S. Regulation of the interaction of inosine monophosphate dehydrogenase with mycophenolic acid by GTP. J. Biol. Chem. 281 (2006) 206-212
14. Kennan A., Aherne A., Palfi A., Humphries M., McKee A., Stitt A., et al. Identification of an IMPDH1 mutation in autosomal dominant retinitis pigmentosa (RP10) revealed following comparative microarray analysis of transcripts derived from retinas of wild-type and Rho(-/-) mice. Hum. Mol. Genet. 11 (2002) 547-557
15. Kochanowski N., Blanchard F., Cacan R., Chirat F., Guedon E., Marc A., et al. Intracellular nucleotide and nucleotide sugar contents of cultured CHO cells determined by a fast, sensitive, and high-resolution ion-pair RP-HPLC. Anal. Biochem. 348 (2006) 243-251
16. Kohler G.A., Gong X., Bentink S., Theiss S., Pagani G.M., Agabian N., et al. The functional basis of mycophenolic acid resistance in Candida albicans IMP dehydrogenase. J. Biol. Chem. 280 (2005) 11295-11302
17. Kozma P., Hughbanks-Wheaton D.K., Locke K.G., Fish G.E., Gire A.I., Spellicy C.J., et al. Phenotypic characterization of a large family with RP10 autosomal-dominant retinitis pigmentosa: an Asp226Asn mutation in the IMPDH1 gene. Am. J. Ophthalmol. 140 (2005) 858-867
18. McLean J.E., Hamaguchi N., Belenky P., Mortimer S.E., Stanton M., and Hedstrom L. Inosine 5′-monophosphate dehydrogenase binds nucleic acids in vitro and in vivo. Biochem. J. 379 (2004) 243-251
19. Mele T.S., and Halloran P.F. The use of mycophenolate mofetil in transplant recipients. Immunopharmacology 47 (2000) 215-245
20. Mortimer S.E., and Hedstrom L. Autosomal dominant retinitis pigmentosa mutations in inosine 5′-monophosphate dehydrogenase type I disrupt nucleic acid binding. Biochem. J. 390 (2005) 41-47
21. Nair K.S., Hanson S.M., Mendez A., Gurevich E.V., Kennedy M.J., Shestopalov V.I., et al. Light-dependent redistribution of arrestin in vertebrate rods is an energy-independent process governed by protein-protein interactions. Neuron 46 (2005) 555-567
22. Natsumeda Y., Ohno S., Kawasaki H., Konno Y., Weber G., and Suzuki K. Two distinct cDNAs for human IMP dehydrogenase. J. Biol. Chem. 265 (1990) 5292-5295
23. Pugh Jr. E.N., and Lamb T.D. Cyclic GMP and calcium: the internal messengers of excitation and adaptation in vertebrate photoreceptors. Vision Res. 30 (1990) 1923-1948
24. Rau H., Kocova M., O'Rahilly S., and Whitehead J.P. Naturally occurring amino acid substitutions at Arg1174 in the human insulin receptor result in differential effects on receptor biosynthesis and hybrid formation, leading to discordant clinical phenotypes. Diabetes 49 (2000) 1264-1268
25. Scott J.W., Hawley S.A., Green K.A., Anis M., Stewart G., Scullion G.A., et al. CBS domains form energy-sensing modules whose binding of adenosine ligands is disrupted by disease mutations. J. Clin. Invest. 113 (2004) 274-284
26. Senda M., and Natsumeda Y. Tissue-differential expression of two distinct genes for human IMP dehydrogenase (E.C.1.1.1.205). Life Sci. 54 (1994) 1917-1926
27. Spellicy C.J., Daiger S.P., Sullivan L.S., Zhu J., Liu Q., Pierce E.A., et al. Characterization of retinal inosine monophosphate dehydrogenase 1 in several mammalian species. Mol. Vis. 13 (2007) 1866-1872
28. Thisse, B., Pflumio, S., Fürthauer, M., Loppin, B., Heyer, V., Degrave, A., et al. (2001). Expression of the zebrafish genome during embryogenesis (NIH R01 RR15402). ZFIN Direct Data Submission (http://zfin.org), ZDB-PUB-010810-1.
29. Thomas E.C., Zhe Y., Molero J.C., Schmitz-Peiffer C., Ramm G., James D.E., et al. The subcellular fractionation properties and function of insulin receptor substrate-1 (IRS-1) are independent of cytoskeletal integrity. Int. J. Biochem. Cell Biol. 38 (2006) 1686-1699
30. Whitehead J.P., Simpson F., Hill M.M., Thomas E.C., Connolly L.M., Collart F., et al. Insulin and oleate promote translocation of inosine-5′ monophosphate dehydrogenase to lipid bodies. Traffic 5 (2004) 739-749