Abstract
Activity of membrane-bound γ-glutamyl transpeptidase (γ-GTP) was examined in various regions of mouse brain, in capillaries of the cerebral cortex and in telencephalic choroid plexuses. The level of activity in the capillaries was double and that of the choroid plexus nine times that of the γ-GTP activity found in the brain, septum, hippocampus, hypothalamus, thalamus, cerebellum, frontal cortex, pons, medulla oblongata, and amygdala. Histochemically the γ-GTP activity was demonstrated in the surface membranes of choroidal cells and in the endothelium of small capillaries.
The activities of γ-GTP of cerebral cortex, choroid plexus, and capillaries from rabbit were 5–17 times greater than those from corresponding areas of mouse brain. While 30 mM methionine stimulated (in vitro) the enzyme from mouse brain, no such effect was observed with the enzyme activity from rabbit brain. The γ-GTP activity from the capillaries of cerebral cortex of both mouse and rabbit was not effected by the presence of methionine.
These findings suggest existence of differences in the specificity of γ-GTP activity in these two species.
Similar content being viewed by others
References
Meister, A. 1973. On the enzymology of amino acid transport. Science 180:33–39.
Meister, A., Tate, S. S., andRoss, L. L. 1976. Membrane-bound γ-glutamyl transpeptidase. Pages 315–347,in Martanosi, A. (ed.), The Enzymes of Biological Membranes, Vol. 3, Plenum, New York.
Prusiner, S., Doak, C. W., andKirk, G. 1976. A novel mechanism for group translocation: Substrate-product reutilization by γ-glutamyl transpeptidase in peptide and amino acid transport. J. Cell. Physiol. 89:853–864.
Samuels, S. 1977. Transport of the large-neutral amino acids by the γ-glutamyl cycle: A proposal. J. Theor. Biol. 64:729–738.
Albert, Z., Orlowski, M., Rzucidlo, Z., andOrlowska, J. 1966. Studies on γ-glutamyl transpeptidase activity and its histochemical localization in the central nervous system of man and different animal species. Acta Histochem. 25:312–320.
Lisý, V., andLodin, Z. 1977. In vitro influencing of brain γ-glutamyl transpeptidase activity by some amino acids. Collection Czechoslov. Chem. Commun. 42:2967–2974.
Okonkwo, P. O., Orlowski, M., andGreen, J. P. 1974. Enzymes of the γ-glutamyl cycle in the choroid plexus and brain. J. Neurochem. 22: 1053–1058.
Orlowski, M., andWilk, S. 1975. Intermediates of the γ-glutamyl cycle in mouse tissues. Influence of administration of amino acids on pyrrolidone carboxylate and γ-glutamyl amino acids. Eur. J. Biochem. 53:581–590.
Grandgeorge, M., andMorélis, P. 1976. Purification partielle et etude de la γ-glutamyl transpeptidase des capillaires cerebraux de Mouton. Biochimie 58:275–284.
Orlowski, M., Sessa, G., andGreen, J. P. 1974. γ-Glutamyl transpeptidase in brain capillaries: possible site of a blood-brain barrier for amino acids. Science 184:66–68.
Sessa, G., andPerez, M. 1975. Biochemical changes in rat brain associated with the development of the blood-brain barrier. J. Neurochem. 25:779–782.
Sessa, G., Orlowski, M., andGreen, J. P. 1976. Isolation from bovine brain of a fraction containing capillaries and a fraction containing membrane fragments of the choroid plexus. J. Neurobiol. 7:51–61.
Lorenzo, A. V. 1974. Amino acid transport mechanisms of the cerebrospinal fluid. Fed. Proc. 33:2079–2085.
Tate, S. S., Ross, L. L., andMeister, A. 1973. The γ-glutamyl cycle in choroid plexus: its possible function in amino acid transport. Proc. Natl. Acad. Sci. U.S.A. 70:1447–1449.
Prusiner, P. E., andPrusiner, S. B. 1978. Partial purification and kinetics of γ-glutamyl transpeptidase from bovine choroid plexus. J. Neurochem. 30:1253–1259.
Šťastný, F., andRychter, Z. 1976. Quantitative development of choroid plexus in chick embryo cerebral ventricles. Acta Neurol. Scand. 53:251–259.
Mršulja, B. B., Mršulja, B. J., Fujimoto, T., Klatzo, I., andSpatz, M. 1976. Isolation of brain capillaries: A simplified technique. Brain Res. 110:361–365.
Orlowski, M., Okonkwo, P. O., andGreen, J. P. 1973. Activation of γ-glutamyl transpeptidase by monovalent cations. FEBS Lett. 31:237–240.
Tate, S. S., andMeister, A. 1974. Interaction of γ-glutamyl transpeptidase with amino acids, dipeptides, and derivatives and analogs of glutathione. J. Biol. Chem. 249:7593–7602.
Lowry, O. H., Rosebrough, N. R., Farr, A. L. L., andRandall, R. J. 1951. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193:265–275.
Reyes, E., andPalmer, G. C. 1976. Biochemical localization of γ-glutamyl transpeptidase within cellular elements of the rat cerebral cortex. Res. Commun. Chem. Pathol. Pharmacol. 14:759–762.
Reyes, E., andPrather, E. E. 1976. Subcellular and regional localization of γ-glutamyl transpeptidase in sheep brain. Neurochem. Res. 1:251–259.
Smith, R. L., andHeizer, W. D. 1978. Gamma-glutamyl transferase of rat and human intestine: greater enhancement of activity by dipeptides than by amino acids or longer peptides. Biochem. Med. 19:383–394.
Sershen, H., andLajtha, A. 1976. Perinatal changes of transport systems for amino acids in slices of mouse brain. Neurochem. Res. 1:417–428.
Christensen, H. N. 1973. On the development of amino acid transport systems. Fed. Proc. 32:19–28.
Ford, D. H. 1976. Blood-brain barrier: A regulatory mechanism. Pages 1–42, inEhrenpreis, S., andKopin, I. J. (eds.), Review of Neuroscience, Vol. II, Raven Press, New York.
Rapoport, S. I. 1976. Transport of sugars, amino acids and other substances at the blood-brain barrier. Pages 177–206,in Rapoport, S. I. (ed.), Blood-Brain Barrier in Physiology and Medicine, Raven Press, New York.
Levin, E. 1977. Are the terms blood-brain barrier and brain capillary permeability synonymous? Pages 191–199,in Bito, L. Z., Davson, H., andFenstermacher, J. D. (eds.), The Ocular and Cerebrospinal Fluids, Academic Press, New York.
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Lisý, V., Šťastný, F. & Lodin, Z. Regional distribution of membrane-bound γ-glutamyl transpeptidase activity in mouse brain. Neurochem Res 4, 747–753 (1979). https://doi.org/10.1007/BF00964471
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF00964471