Abstract
Neuronal perikarya were isolated, using bulk preparative procedures, from bovine brains. Synaptosomes, neuronal perikarya, and brain homogenates had similar ganglioside patterns, with the synaptosomes containing at least four times more total ganglioside per mg protein than the neuronal perikarya and twice that of the homogenate. Synaptosomes had 26–33 nmol total sialic acid/mg protein, while the neurons had only 15–17 nmol. Determination of ganglioside sialidase activity showed that neuronal perikarya had very low levels (negligible), in comparison with synaptosomes or whole-brain homogenates. Trypsin treatment during the isolation procedure enhanced sialidase activity two-to threefold in the particulate fraction of the whole-brain homogenate. Determination of the distribution of sialidase activity in the fractions obtained during the isolation of the neuronal perikarya showed that the sialidase activity was associated with the myelin, broken-off dendritic processes, and glial-cell fractions that banded in the less dense sucrose.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Schengrund, C.-L., Jensen, D.S., andRosenberg, A. (1972) Localization of sialidase in the plasma membrane of rat liver cells. J. Biol. Chem. 247, 2742–2746.
Visser, A., andEmmelot, P. (1973). Studies on plasma membranes XX. Sialidase in hepatic plasma membranes. J. Membr. Biol. 14, 73–84.
Wiegandt, H. (1967) Subcellular localization of gangliosides in the brain. J. Neurochem. 14, 671–674.
Dekirmenjian, H., andBrunngraber, E.G. (1969) Distribution of protein-boundN-acetylneuraminic acid in subcellular particulate fractions prepared from rat whole brain. Biochim. Biophys. Acta 177, 1–10.
Schengrund, C.-L., andRosenberg, A. (1970) Intracellular location and properties of bovine brain sialidase. J. Biol. Chem. 245, 6196–6200.
Tettamanti, G., Morgan, I.G., Gombos, G., Vincendon, G., andMandel, P. (1972) Subsynaptosomal localization of brain particulate neuraminidase. Brain Res. 47, 515–518.
Heijlman, J., andRoukema, P.A. (1972) Action of calf brain sialidase on gangliosides, sialoglycoproteins and sialoglycopeptides. J. Neurochem. 19, 2567–2575.
Öhman, R., Rosenberg, A., andSvennerholm, L. (1970) Human brain sialidase. Biochemistry 9, 3774–3782.
Norton, W.T., andPoduslo, S.E. (1971) Neuronal perikarya and astroglia of rat brain: chemical composition during myelination. J. Lipid Res. 12, 84–90.
Hamburger, A., andSvennerholm, L. (1971) Composition of gangliosides and glial cell enriched fractions. J. Neurochem. 18, 1821–1829.
Norton, W.T., andPoduslo, S.E. (1970) Neuronal soma and whole neuroglia of rat brain: a new isolation technique. Science 167, 1144–1146.
Sevier, A.C., andMunger, B.L. (1965) A silver method for paraffin sections of neural tissue. J. Neuropathol. Exp. Neurol. 24, 130–145.
Eichberg, J., Jr., Whittaker, V.P., andDawson, R.M.C. (1964) Distribution of lipids in subcellular particles of guinea-pig brain. Biochem. J. 92, 91–100.
Fllch, J., Arsove, S., andMeath, J.A. (1951) Isolation of brain stradin, a new type of large molecule tissue component. J. Biol. Chem. 191, 819–831.
Schengrund, C.-L., Lausch, R.N., andRosenberg, A. (1973) Sialidase activity in transformed cells. J. Biol. Chem. 248, 4424–4428.
Horvat, A., andTouster, O. (1968) On the lysosomal occurrence and the properties of the neuraminidase of rat liver and of Ehrlich ascites tumor cells. J. Biol. Chem. 243, 4380–4390.
Warren, L. (1959) The thiobarbituric acid assay of sialic acids. J. Biol. Chem. 234, 1971–1975.
Jourdian, G.W., Dean, L., andRoseman, S. (1971) The sialic acids XI. A periodate-resorcinol method for the quantitative estimation of free sialic acid and their glycosides. J. Biol. Chem. 246, 430–435.
Wagner, H., Hörhammer, L., andWolff, P. (1961) Dünnschichtchromatographie von phosphatiden und glykolipiden. Biochem. Z. 334, 175–184.
Svennerholm, L. (1957) Quantitative estimation of sialic acids II. A colorimetric resorcinol-hydrochloric acid method. Biochim. Biophys. Acta 24, 604–611.
Lowry, O.H., Rosebrough, N.J., Farr.,A.L., andRandall, R.J. (1951) Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193, 265–275.
Wilson, S.H., Schrier, B.K., Farber, J.L., Thompson, E.J., Rosenberg, R.N., Blume, A.J., andNirenberg, M.W. (1972) Markers for gene expression in cultured cells from the nervous system. J. Biol. Chem. 247, 3159–3169.
Suzuki, K. (1964) A simple and accurate micromethod for quantitative determination of ganglioside patterns. Life Sci. 3, 1227–1233.
Barton, N., andRosenberg, A. (1973) Action ofVibrio cholerae neuraminidase (sialidase) upon the surface of intact cells and their isolated sialolipid components. J. Biol. Chem. 248, 7353–7358.
Svensmark, O., andKristensen, P. (1962) Electrophoretic mobility of sialidasetreated human serum cholinesterase. Dan. Med. Bull. 9, 16, 17.
Cotman, C.W., andMatthews, D.A. (1971) Synaptic plasma membranes from rat brain synaptosomes: isolation and partial characterization. Biochim. Biophys. Acta 249, 380–394.
Abe, T., andNorton, W.T. (1974) The characterization of sphingolipids from neurons and astroglia of immature rat brain. J. Neurochem. 23, 1025–1036.
Burger, M.M. (1970) Proteolytic enzymes initiating cell division and escape from contact inhibition of growth. Nature 227, 170, 171.
Schengrund, C.-L. andNelson, J.T. (1975) Influence of cation concentration on the sialidase activity of neuronal synaptic membranes. Biochem. Biophys. Res. Commun. 63, 217–223.
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Schengrund, CL., Nelson, J.T. Ganglioside sialidase activity in bovine neuronal perikarya. Neurochem Res 1, 171–180 (1976). https://doi.org/10.1007/BF00966108
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF00966108