Developmental and Regional Studies of the Metabolism of Inositol 1,4,5-Trisphosphate in Rat Brain
dc.contributor.author | Heacock, Anne M. | en_US |
dc.contributor.author | Seguin, Edward B. | en_US |
dc.contributor.author | Agranoff, Bernard W. | en_US |
dc.date.accessioned | 2010-04-01T15:04:55Z | |
dc.date.available | 2010-04-01T15:04:55Z | |
dc.date.issued | 1990-04 | en_US |
dc.identifier.citation | Heacock, Anne M.; Seguin, Edward B.; Agranoff, Bernard W. (1990). "Developmental and Regional Studies of the Metabolism of Inositol 1,4,5-Trisphosphate in Rat Brain." Journal of Neurochemistry 54(4): 1405-1411. <http://hdl.handle.net/2027.42/65545> | en_US |
dc.identifier.issn | 0022-3042 | en_US |
dc.identifier.issn | 1471-4159 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/65545 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=2313293&dopt=citation | en_US |
dc.description.abstract | Coupling of CNS receptors to phosphoinositide turnover has previously been found to vary with both age and brain region. To determine whether the metabolism of the second messenger inositol 1,4,5-trisphosphate also displays such variations, activities of inositol 1,4,5-trisphosphate 5′-phosphatase and 3′-kinase were measured in developing rat cerebral cortex and adult rat brain regions. The 5′-phosphatase activity was relatively high at birth (∼50% of adult values) and increased to adult levels by 2 weeks postnatal. In contrast, the 3′-kinase activity was low at birth and reached ∼50% of adult levels by 2 weeks postnatal. In the adult rat, activities of the 3′-kinase were comparable in the cerebral cortex, hippocampus, and cerebellum, whereas much lower activities were found in hypothalamus and pons/medulla. The 5′-phosphatase activities were similar in cerebral cortex, hippocampus, hypothalamus, and pons/medulla, whereas 5-to 10-fold higher activity was present in the cerebellum. The cerebellum is estimated to contain 50–60% of the total inositol 1,4,5-trisphosphate 5′-phosphatase activity present in whole adult rat brain. The localization of the enriched 5′-phosphatase activity within the cerebellum was examined. Application of a histochemical lead-trapping technique for phosphatase indicated a concentration of inositol 1,4,5-trisphosphate 5′-phosphatase activity in the cerebellar molecular layer. Further support for this conclusion was obtained from studies of Purkinje cell-deficient mutant mice, in which a marked decrement of cerebellar 5′-phosphatase was observed. These results suggest that the metabolic fate of inositol 1,4,5-trisphosphate depends on both brain region and stage of development. | en_US |
dc.format.extent | 986401 bytes | |
dc.format.extent | 3110 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.publisher | Blackwell Publishing Ltd | en_US |
dc.rights | 1990 International Society for Neurochemistry Ltd. | en_US |
dc.subject.other | Inositol Phosphate Metabolism | en_US |
dc.subject.other | Development | en_US |
dc.subject.other | Cerebellum | en_US |
dc.subject.other | Inositol 1,4,5-trisphosphate Receptor | en_US |
dc.title | Developmental and Regional Studies of the Metabolism of Inositol 1,4,5-Trisphosphate in Rat Brain | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Neurosciences | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Neuroscience Laboratory, University of Michigan, Ann Arbor, Michigan, U.S.A. | en_US |
dc.identifier.pmid | 2313293 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/65545/1/j.1471-4159.1990.tb01976.x.pdf | |
dc.identifier.doi | 10.1111/j.1471-4159.1990.tb01976.x | en_US |
dc.identifier.source | Journal of Neurochemistry | en_US |
dc.identifier.citedreference | Agranoff B. W., Murthy P., and Seguin E. B. ( 1983 ) Thrombin-induced phosphodiesteratic cleavage of phosphatidylinositol bisphosphate in human platelets. J. Biol. Chem. 258, 2076 – 2078. | en_US |
dc.identifier.citedreference | Biden T. J., Comte M., Cox J. A., and Wollheim C. B. ( 1987 ) Calcium-calmodulin stimulates inositol 1,4,5-trisphosphate kinase activity from insulin-secreting RINm5F cells. J. Biol. Chem. 262, 9437 – 9440. | en_US |
dc.identifier.citedreference | Bredt D. S., Mourey R. J., and Snyder S. H. ( 1989 ) A simple, sensitive, and specific radioreceptor assay for inositol 1,4,5-trisphosphate in biological tissues. Biochem. Biophys. Res. Commun. 159, 976 – 982. | en_US |
dc.identifier.citedreference | Connolly T. M., Bross T. E., and Majerus P. W. ( 1985 ) Isolation of a phosphomonoesterase from human platelets that specifically hydrolyzes the 5′-phosphate of inositol 1,4,5-trisphosphate. J. Biol. Chem. 260, 7868 – 7874. | en_US |
dc.identifier.citedreference | Daniel J. L., Dangelmaier C. A., and Smith J. B. ( 1988 ) Calcium modulates the generation of inositol 1,3,4-trisphosphate in human platelets by the activation of inositol 1,4,5-trisphosphate 3-kinase. Biochem. J. 253, 789 – 794. | en_US |
dc.identifier.citedreference | Dean N. M. and Moyer J. D. ( 1987 ) Separation of multiple isomers of inositol phosphates formed in GH 3 cells. Biochem. J. 242, 361 – 366. | en_US |
dc.identifier.citedreference | Downes C. P., Mussat M. C., and Michell R. H. ( 1982 ) The inositol trisphosphate phosphomonoesterase of the human erythrocyte membrane. Biochem. J. 203, 169 – 177. | en_US |
dc.identifier.citedreference | Erneux C., Delvaux A., Moreau C., and Dumont J. E. ( 1986 ) Characterization of D- myo -inositol 1,4,5-trisphosphate phosphatase in rat brain. Biochem. Biophys. Res. Commun. 134, 351 – 358. | en_US |
dc.identifier.citedreference | Erneux C., Delvaux A., Moreau C., and Dumont J. E. ( 1987 ) The dephosphorylation pathway of D- myo -inositol 1,3,4,5-tetrakisphosphate in rat brain. Biochem. J. 247, 635 – 639. | en_US |
dc.identifier.citedreference | Fisher S. K. and Agranoff B. W. ( 1987 ) Receptor activation and inositol lipid hydrolysis in neural tissues. J. Neurochem. 48, 999 – 1016. | en_US |
dc.identifier.citedreference | Geiger P. J. and Bessman S. P. ( 1972 ) Protein determination by Lowry's method in the presence of sulfhydryl reagents. Anal. Biochem. 49, 467 – 473. | en_US |
dc.identifier.citedreference | Gerfen C. R., Choi W. C., Suh P. G., and Rhee S. G. ( 1988 ) Phospholipase C I and II brain isozymes: immunohistochemical localization in neuronal systems in rat brain. Proc. Acad. Sci. USA 85, 3208 – 3212. | en_US |
dc.identifier.citedreference | Ghosh T. K., Eis P. S., Mullaney J. M., Ebert C. L., and Gill D. L. ( 1988 ) Competitive, reversible, and potent antagonism of inositol 1,4,5-trisphosphate-activated calcium release by heparin. J. Biol. Chem. 263, 11075 – 11079. | en_US |
dc.identifier.citedreference | Hansen C. A., Johanson R. A., Williamson M. T., and Williamson J. R. ( 1987 ) Purification and characterization of two types of soluble inositol phosphate 5′-phosphomonoesterases from rat brain. J. Biol. Chem. 262, 17319 – 17326. | en_US |
dc.identifier.citedreference | Heacock A. M., Fisher S. K., and Agranoff B. W. ( 1987 ) Enhanced coupling of neonatal muscarinic receptors in rat brain to phosphoinositide turnover. J. Neurochem. 48, 1904 – 1911. | en_US |
dc.identifier.citedreference | Heacock A. M., Seguin E. B., and Agranoff B. W. ( 1988 ) Components of the IP 3 second messenger system in rat brain differ in developmental regulation and regional localization. Soc. Neurosci. Abstr. 14, 129. | en_US |
dc.identifier.citedreference | Heacock A. M., Seguin E. B., and Agranoff B. W. ( 1989 ) Biochemical and histochemical measurements of components of the IP 3 second messenger system in rat and human brain. J. Neurochem. 52 ( Suppl. ), S163. | en_US |
dc.identifier.citedreference | Hoer D., Kwiatkowski A., Seib C., Rosenthal W., Schultz G., and Oberdisse E. ( 1988 ) Degradation of inositol 1,3,4,5-tetrakisphosphates by porcine brain cytosol yields inositol 1,3,4-trisphosphate and inositol 1,4,5-trisphosphate. Biochem. Biophys. Res. Commun. 154, 668 – 675. | en_US |
dc.identifier.citedreference | Irvine R. F. ( 1989 ) How do inositol 1,4,5-trisphosphate and inositol 1,3,4,5-tetrakisphosphate regulate intracellular Ca 2+ ? Biochem. Soc. Trans. 17, 6 – 9. | en_US |
dc.identifier.citedreference | Irvine R. F., Letcher A. J., Heslop J. P., and Berridge M. J. ( 1986 ) The inositol tris/tetrakisphosphate pathway---demonstration of Ins(1,4,5)P 3 3-kinase activity in animal tissues. Nature 320, 631 – 634. | en_US |
dc.identifier.citedreference | Johanson R. A., Hansen C. A., and Williamson J. R. ( 1988 ) Purification of D- myo -inositol 1,4,5-trisphosphate 3-kinase from rat brain. J. Biol. Chem. 263, 7465 – 7471. | en_US |
dc.identifier.citedreference | Joseph S. K., Rice H. L., and Williamson J. R. ( 1989 ) The effect of external calcium and pH on inositol trisphosphate-mediated calcium release from cerebellum microsomal fractions. Biochem. J. 258, 261 – 265. | en_US |
dc.identifier.citedreference | Meek J. L. ( 1986 ) Inositol bis-, tris- and tetrakis(phosphate)s: analysis in tissues by HPLC. Proc. Natl. Acad. Sci. USA 83, 4162 – 4166. | en_US |
dc.identifier.citedreference | Minta A., Harootunian A. T., Kao J. P., and Tsien R. Y. ( 1987 ) New fluorescent indicators for intracellular sodium and calcium. J. Cell Biol. 105, 89a. | en_US |
dc.identifier.citedreference | Morris A. J., Downes C. P., Harden T. K., and Michell R. H. ( 1987 ) Turkey erythrocytes possess a membrane-associated inositol 1,4,5-trisphosphate 3-kinase that is activated by Ca 2+ in the presence of calmodulin. Biochem. J. 248, 489 – 493. | en_US |
dc.identifier.citedreference | Morris A. J., Murray K. J., England P. J., Downes C. P., and Michell R. H. ( 1988 ) Partial purification and some properties of rat brain inositol 1,4,5-trisphosphate 3-kinase. Biochem. J. 251, 157 – 163. | en_US |
dc.identifier.citedreference | Nicoletti F., Iadarola M. J., Wroblewski J. T., and Costa E. ( 1986 ) Excitatory amino acid recognition sites coupled with inositol phospholipid metabolism: developmental changes and interaction with Α 1 -adrenoceptors. Proc. Natl Acad. Sci. USA 83, 1931 – 1935. | en_US |
dc.identifier.citedreference | Nishizuka Y. ( 1988 ) The molecular heterogeneity of protein kinase C and its implications for cellular regulation. Nature 334, 661 – 665. | en_US |
dc.identifier.citedreference | Rooney T. A. and Nahorski S. R. ( 1987 ) Postnatal ontogeny of agonist and depolarization-induced phosphoinositide hydrolysis in rat cerebral cortex. J. Pharmacol. Exp. Ther. 243, 333 – 341. | en_US |
dc.identifier.citedreference | Ryu S. H., Lee S. Y., Lee K.-Y., and Rhee S. G. ( 1987 ) Catalytic properties of inositol trisphosphate kinase: activation by Ca 2+ and calmodulin. FASEB J. 1, 388 – 393. | en_US |
dc.identifier.citedreference | Schoen S. W., Graeber M. B., Toth L., and Kreutzberg G. W. ( 1988 ) 5′-Nucleotidase in postnatal ontogeny of rat cerebellum: a marker for migrating nerve cells ? Dev. Brain Res. 39, 125 – 136. | en_US |
dc.identifier.citedreference | Seyfred M. A., Farrell L. E., and Wells W. W. ( 1984 ) Characterization of d-myo -inositol 1,4,5-trisphosphate phosphatase in rat liver plasma membranes. J. Biol. Chem. 259, 13204 – 13208. | en_US |
dc.identifier.citedreference | Shears S. B. ( 1989 ) Metabolism of the inositol phosphates produced upon receptor activation. Biochem. J. 260, 313 – 324. | en_US |
dc.identifier.citedreference | Seiffert U. B. and Agranoff B. W. ( 1965 ) Isolation and separation of inositol phosphates from hydrolysates of rat tissues. Biochim. Biophys. Acta 98, 574 – 581. | en_US |
dc.identifier.citedreference | Stauderman K. A., Harris G. D., and Lovenberg W. ( 1988 ) Characterization of inositol 1,4,5-trisphosphate-stimulated calcium release from rat cerebellar microsomal fractions. Biochem. J. 255, 677 – 683. | en_US |
dc.identifier.citedreference | Wachstein M. and Meisel E. ( 1957 ) Histochemistry of hepatic phosphatases at a physiologic pH with special reference to the demonstration of bile canaliculi. Am. J. Clin. Pathol. 27, 13 – 23. | en_US |
dc.identifier.citedreference | Worley P. F., Baraban J. M., Colvin J. S., and Snyder S. H. ( 1987a ) Inositol trisphosphate receptor localization in brain: variable stoichiometry with protein kinase C. Nature 325, 159 – 161. | en_US |
dc.identifier.citedreference | Worley P. F., Baraban J. M., Supattapone S., Wilson V. S., and Snyder S. H. ( 1987b ) Characterization of inositol trisphosphate receptor binding in brain. J. Biol. Chem. 262, 12132 – 12136. | en_US |
dc.identifier.citedreference | Worley P. F., Baraban J. M., and Snyder S. H. ( 1989 ) Inositol 1,4,5-trisphosphate receptor binding: autoradiographic localization in rat brain. J. Neurosci. 9, 339 – 346. | en_US |
dc.identifier.citedreference | Yamaguchi K., Hirata M., and Kuriyama H. ( 1988 ) Purification and characterization of inositol 1,4,5-trisphosphate 3-kinase from pig aortic smooth muscle. Biochem. J. 251, 129 – 134. | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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