Huszti Zsuzsanna

Cink az agyban

Irodalom

Albrecht J., Bender A. S., Norenberg M. D. (1994) Ammonia stimulates the release of taurine from cultured astrocytes. Brain Res., 660: 288–292.

Almarghini K., Remy A., Tappaz M. (1991) Immunocyte-chemistry of the taurine biosynthesis enzyme cysteine sulfinate decarboxylase for a glial localization. Neurosci., 43: 111–119.

Amara S. G., Kuhar M. J. (1993) Neurotransmitter transporters: recent progress. Ann. Rev. Neurosci., 16: 73–83.

Arrizza J. L., Eliasof S., Kavanaough M. P., Amara S. (1997) Excitatory aminoacid transporter 5, a retinal glutamate transporter coupled to a chloride conductance. Proc. Natl. Acad. Sci. USA, 94: 4155–4160

Balcar V. J., Johnston G. A. R. (1972) The structural specificity of the high affinity of L-glutamate and L-aspartate uptake systems in the rat CNS. J. Neurochem., 19: 2607–2666.

Barakat L., Wang D., Borday A. (2002) Carrier-mediated uptake and release of taurine from Bergman glia in rat cerebral slices. J. Physiol., 541: 753–767.

Cohen-Kifer E., Lee W., Eskandari S., Nelson N. (2005) Zinc inhibition of gamma-aminobutyric acid transporter 4 (GAT4) revels a link between excitatory and inhibitory neurotransmission. Proc. Natl. Acad. Sci. USA, 102: 6154–6159.

Falkenburger B. H., Barskow K. J., Mintz J. M. (2001) Dendrodendritic inhibition through reversal of dopamine transport. Science, 293: 2465–2470.

Gabrielsson B., Robson T., Norris D., Chung S. H. (1986) Effects of divalent metal ions on the uptake of glutamate and GABA from synaptosomal fractions. Brain Res., 384: 218–223.

Garcia-Colunga J., Reyes-Haro D., Godoy-Garcia U., Miledi R. (2005) Zinc modulation of serotonin uptake in the adult rat corpus callosum. J. Neurosci. Res., 80: 145–149.

Giros B., Caron M.G. (1993). Molecular characterization of the dopamine transporter. Trends Pharmacol. Sci., 14: 43–49.

Green J. P., Prell J. K., Khandewal J. K., Blandina P. (1987) Aspects of histamine metabolism Agents and Actions, 22: 1–15.

Haas H. L., Bucher U. M. (1975) Histamine H2 receptors in single central neurones. Nature, 55: 634–635.

Harris G., Jacobson D., Kahlson G. (1952) The occurence of histamine in cerebral regions related to the hypophysis. Ciba Found. Colloq. Endocri., 4: 186–194.

Higuchi Y., Soga T., Parhar I. S. (2017) Regulatory Pathways of Monoamine Oxidase A during Social Stress. Review. Front. Neurosci., október 31. https://doi.org/10.3389/fnins.2017.00604

Huszti Z., Rimanoczy A., Juhász A., Magyar K. (1990) Uptake, metabolism and release of [3H]-histamine by glial cells in primary cultures of chicken cerebral hemispheres. Glia, 3: 159–163.

Huszti Z., Imrik P., Madarász E. (1994) [3H]-histamine uptake and release by astrocytes from brain: sodium deprivation, high potassium and potassium channel lockers. Neurochem. Res., 19: 1249–1256.

Huszti Z. (1998) Carrier-mediated high affinity uptake system for histamine in astroglial and cerebral endothelial cells. Mini Rev. J. Neurochem. Res., 51: 551–556.

Huszti Z., Prast H., Fischer H., Philippu A. (1998) Glial cells participate in histamine inactivation in vivo. Naunyn-Scmiedeberg Arch. Pharmacol., 357: 49–53.

Huszti Z., Horváth-Sziklai A., Noszál B., Madarász E., Deli A. M. (2001) Enhancing effect of zinc on astroglial and cerebral endothelial histamine uptake. Biochem. Pharmacol., 62: 1491–1450.

Huszti Z. (2003) Histamine uptake into brain cells. Rev. Inflamm. Res., 52 (Suppl): 3–6.

Huszti Z. (2008) Asztrogliális transzport rendszerek. In Huszti Zs., Kálmán M. (szerk.), Glia. Akadémiai Kiadó, Budapest, 265–269, 279–313, 279–313.

Kataoka K., De Robertis E. (1967) Histamine isolated from small nerve endings and synaptic vesicles of rat brain cortex. J. Pharm. Exp. Ther., 156: 114–125.

Komulainen H. (1983) Enhancement of 5-hydroxytryptamine uptake in rabbit hypothalamic synaptosomes but not in blood platelets by zinc and lead ex vivo. Acta pharmacol. toxicol., 53: 166–174.

Kwiatkowski H. (1943) Histamine in nervous tissue. J. Physiol., 102: 32–41.

Lepping P., Huber M. (2010) Role of zinc in the pathogenesis of attention deficit hyperactivity disorder. CNS Drugs, 24: 721–728.

Levenson C. W. (2006) Zinc: The New Antidepressant. Nutr. Rev., 64: 39–42.

Loland C. J., Norregaard L., Gether U. (1999) Defining proximity relationship in the tertiary structure of the dopamine transporter: Identification of a conserved glutamic acid as a third coordinate in the endogeneous Zn2+-binding site. J. Biol. Chem., 274: 36928–36934.

Loland C. J., Norregaard L., Litman T., Gether U. (2002) Generation of an activiting Zn2+ switch in the dopamine transporter: mutation of an intracellular tyrosine constitutively alters the conformational equilibrium of the transport cycle. Proc. Natl. Acad. Sci. USA, 99: 1683–1688.

Lombardini J. B. (1991) Taurine: retinal function. Review. Brain Res., 16: 151–169.

Levi G., Gallo V. (1995) Release of neuroactive aminoacid from glia. In Kettenmann H., Ransom B. R. (Eds), Neuroglia. New York–Oxford University Press, 815–826.

Lin J. S.2, Kitahama K., Fort P., Panula P., Denney R. M., Jouvet M. (1991) Histaminergic system in the rat hypothalamus with references to type B monoamine oxidase. J. Comp. Neurol., 330: 405–420.

Liu Q. R., Lopez-Coravera B., Nelson H. (1992) Cloning and expression of cDNA encoding the transporter taurine and β-alanine in mouse brain. Proc. Nat. Acad. Sci. USA, 89: 1245–1249.

Meinwild A., Sitte H., Gether U. (2004) Zinc potentiates an uncoupled anion conductance associated dopamine transporter. J. Biol. Chem., 279: 49671–49679.

Mitrovic A. D., Plesko F., Vanderberg J. (2001) Zn2+ inhibits the anion conductance of glutamate transporter EAAT4. J. Biol. Chem., 275: 26071–26076.

Norregaard L., Fredericksen D., Nielsen E. D., Gether U. (1998) Delineation of an endogeneous zinc-binding site in the human dopamine transporter. EMBO J., 17: 4266–4273.

Norregaard-Nielsen K., Gether U. (2006) Zn2+ modulation of the neurotransmitter transporters. Review. Handbook of Exp. Pharm., 175: 1–22.

Nowak G., Zieba A., Dudek D., Krosniak M., Szymaczuk M. (1999) Serum trace elements in animal models and human depression. Human Psychoparmacol., 14: 83–86.

Nowak G., Siewek M., Dudek D., Zieba A., Pilc A. (2006) Effect of zinc supplementation on antidepressant therapy in unipolar depression: a preliminary placebo-controlled study. Pol. Pharmacol., 55: 1146–1147.

Nusetti S., Sedazar V., Lima L. (2009) Localization of taurine transporter, taurine and zinc in goldfish retina. Adv. Exp. Med. Biol., 643: 233–242.

Nusetti S., Urbina M., Lima L. (2010a) Effect of zinc ex vivo on taurine uptake in goldfish retinal cells. J. Biomed. Sci., 17 (Suppl): 513.

Nusetti S., Urbina M., Obregon F., Quantal M., Benzo Z., Lima L. (2010b) Effects of zinc ex vivo and intracellular zinc chelator in vivo on taurine uptake in gold fish retina. Amino Acids, 38: 1429–1437.

Palkovits M., Elekes I., Láng T., Patthy A. (1986). Taurine levels in discrete brain nuclei of rats. J. Neurochem, 47: 1333–1335.

Panula P., Yang H. Y. T., Costa E. (1984) Histamine containing neurons in the rat hypotahalamus. Proc. Natl. Acad. Sci. USA, 81: 2572–2576.

Pasantes-Morales H., Cruz C. (1984) Protective effect of taurine and zinc on peroxidation-induced damage in photo-receptor outer segments. J. Neurosci. Res., 303–311.

Pasantes-Morales H., Moran J., Schousboe A. (1990) Volume-sensitive release of taurine from cultured astrocytes properties and mechanism. Glia, 427–432.

Pifl Ch., Wolf A., Rebernick P., Reither H., Berger M. L. (2009) Zinc regulates the dopamine transporter in a membrane potential and chloride-dependent manner. Neuropharm., 56: 531–540.

Ramirez-Guerrero S., Guardo-Maya S. et al. (2022) Taurine and Astrocytes: A Homeostatic and Neuroprotective Relationship. Review. Front. Mol. Neurosci., július 05. https://doi.org/10.3389/fnmol.2022.937789

Richfield E. K. (1993) Zinc modulation of drug binding cocain affinity states and dopamine uptake on the dopamine-uptake complex. Mol. Pharmacol., 43: 100–108.

Rudnick G. (1997) Mechanism by biogenic amine neurotransporters. In Reith M. E. A. (Ed.), Neurotransmitter transporters. Structure, Function and Regulation. Humana Press, Totowa, N. J., 73–100.

Schwartz J. C., Lampart C., Rose C. (1970) Properties and regional distribution of histidine decarboxylase in rat brain cortex. J. Neurochem., 17: 1527–1534.

Schwartz J. C., Pollard H., Quach T. T. (1980) Histamine as a neurotransmitter in mammalian brain: Neurochemical evidence. J. Neurochem., 35: 26–33.

Scholze P., Norregaard L., Singer E. A., Freissmuth M., Gether U., Sitte H. H. (2002) The role of zinc ions in reverse transport mediated by monoamine transporters. J. Biol. Chem., 277: 21505–21513.

Scofield M. D., Kalivas P. W. (2014) Astrocytic Dysfunction and Addiction: Consequences of Impaired Glutamate Homeostasis. The Neuroscientist, 20(6). https://doi.org/10.1177/1073858413520347

Smart T. G., Xir X., Krisher R. J. (1994) Modulation of inhibitory and excitatory amino acid receptor ion channels by zinc. Progress in Neurobiology, 42: 393–441.

Smith K. E., Borden L. A., Wang C. H., Hartig P. R., Branchek T. A., Weinshank R. I. (1992) Cloning and expression of a high affinity taurine transporter from rat brain. Mol. Pharmacol., 42: 563–569.

Smits R. P. J. M., Steinbusch H. W. M., Mulder A. H. (1988) Studies on the specificity of the uptake and release of radiolabelled histamine in rat brain slices. Neurochem. Int., 12: 193–201.

Spiridon M., Kamm D., Billups B., Mobbs P., Attwell D. (1998) Modulation by zinc of the glutamate transporters in glial cells and cones isolated from the tiger salamandra retina. J. Physiol., 506: 363–376.

Stockner T., Montgomery T. R., Kudlacek O., Weissrnsteiner R., Ecker G., Freissmuth M., Sitte H. H. (2013) Mutational analysis of the high-affinity zinc binding refined hunan dopamine transporter homology model. PLOS Comput. Biol., 9(2): e1002909.

Tappaz M., Almarghini K., Do K. (1994) Cysteine sulfinate decarboxylase in brain identification characterization and immunocytochemical localization in astrocytes. Adv. in Exp. Med. and Biol., 359: 257–268.

Taylor K. M., Snyder S. H. (1973) The release of histamine from tissue slices of rat hypothalamus. J. Neurochem., 21: 1215–1223.

Ugarte M., Osborne N. N. (2001) Zinc in retina. Prog. Neurobiol., 64: 219–249.

Vandenberg R. J., Mitrovic A. D., Johnston G. A. (1998) Molecular basis for differential inhibition of glutamate transporter subtypes. Mol. Pharmacol., 54: 189–196.

Verdiere M., Rose C., Schwartz J. C. (1975) Synthesis and release of histamine studied on slices from rat hypothalamus. Eur. J. Pharm., 34: 157–168.

Watanabe T., Taguchi Y., Hayashi H., Tanaka Y., Shiosaka S., Tohyama M., Kubota H., Terano Y., Wada H. (1983) Evidence for the presence of histaminergic neuron system in the brain: an immunochemical analysis. Neurosci. Lett., 39: 249–254.

Watanabe T., Taguchi Y., Shiosaka S., Tasaka J., Kubota H., Terano Y., Wada H. (1984) Distribution of histaminergic neuron system in the central bervous system of rats: a fluorescent immunohistochemical analysis with histidine decarboxylase as a marker. Brain Res., 295: 13–25.

Wu S. M., Qiao X., Noebels J. L., Yang X. L. (1993) Localization and modulatory action of zinc in vertabrate retina. Vision Res., 33: 2611–2616.

Yoshikawa T., Nakamura T., Yanai K. (2018) New perspectives of pharmacological drug discovery research using genetically engineered mice: analysis of brain histamine clearance using genetically engineered mice. Folia Pharmacologica Japonica, 152: 16–20.

Tartalomjegyzék

Kiadó: Akadémiai Kiadó

Online megjelenés éve: 2025

Nyomtatott megjelenés éve: 2025

ISBN: 978 963 664 087 3

Orvostudomány

A cink az élő szervezetek esszenciális mikroeleme. Nagy mennyiségben megtalálható az emberi agyban, az izmokban, a csontokban, a vesében, a májban, a prosztatában és a szemben is. Több száz enzim működésében vesz részt – részben közvetlenül a katalitikus reakciókban, részben az enzimfehérjék koordinátoraként. Jelentős strukturális funkciót tölt be számos transzkripciós faktor szerkezetének kialakításában és a sejtek közötti kommunikációban. Huszti Zsuzsa vizsgálódásának tárgya ezúttal az agy. A kötet külön fejezetekben tárgyalja a cink szerepét az idegsejtekben, a neurofziológiában, a neuoropatológiában, az Alzheimer-kórban (a betegség terápiájában), a memóriában. A szerző széles szakirodalmi bázisra támaszkodva összegzi az ismeretanyagot, és gazdag hivatkozási listával látja el a fejezeteket.

Hivatkozás: https://mersz.hu/huszti-cink-az-agyban//

BibTeX EndNote Mendeley Zotero