Summary
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1.
The125I-labeled S-100 specific binding to a Triton X-100 (TX-100) extract of synaptosomal particulate fractions (SYN) was investigated.
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2.
The results indicate that (a) S-100 binding to the TX-100 extract is partially irreversible after a critical association time at 37°C, while it is fully reversible after any association time at 4°C; (b) trypsin and phospholipase C partially reverse the S-100 binding, while phospholipase D enhances the interaction to some extent, in a dose-dependent way; (c) EDTA and high concentrations of NaC1 or KC1 are more efficient as inhibitors of the S-100 binding to the TX-100 extract than as125I-labeled S-100 dissociating agents, in analogy with previous observations with SYN; and (d) two main populations of solubilized S-100 binding sites can be evidenced by gel filtration and sucrose gradient centrifugation when low amounts of the TX-100 extract are processed and/or low S-100 concentrations are used, while two additional molecular species are separated when greater amounts of either factors are tested.
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3.
These results suggest the possibility that S-100 may be involved in the regulation of some membrane activities.
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References
Baudier, J., Briving, C., Deinum, J., Haglid, K., Sörskog, L., and Wallin, M. (1982). Effect of S-100 proteins and calmodulin on Ca2+-induced disassembly of brain microtubule proteins in vitro.FEBS Lett. 147165–167.
Burgess, W. H., Schleicher, M., and Watterson, D. M. (1982). Distribution, specificity and calcium dependence of proteins which bind calmodulin, troponin C and S-100.J. Cell Biol. 95:317a.
Calissano, P., and Bangham, A. D. (1971). Effect of two brain specific proteins (S-100 and 14.3.2) on cation diffusion across artificial membranes.Biochem. Biophys. Res. Commun. 43504–509.
Calissano, P., Moore, B. W., and Friesen, A. (1969). Effect of calcium ion on S-100, a protein of the nervous system.Biochemistry 84318–4326.
Calissano, P., Alemà, S., and Fasella, P. (1974). Interaction of S-100 protein with cations and liposomes.Biochemistry 13 4553–4560.
Cocchia, D. (1981). Immunocytochemical localization of S-100 protein in the brain of adult rat. An ultrastructural study.Cell Tissue Res. 214529–540.
Cocchia, D., and Miani, N. (1980). Immunocytochemical localization of the brain-specific S-100 protein in the pituitary gland of adult rat.J. Neurocytol. 9771–782.
Cocchia, D., Michetti, F., and Donato, R. (1981). Immunochemical and immunocytochemical localization of S-100 antigen in normal human skin.Nature 29485–87.
Cocchia, D., Pansera, F., Palumbo, A., and Donato, R. (1982). Immunocytochemical localization of S-100 protein binding sites in synaptosomal fractions and subfractions.Cell. Mol. Neurobiol. 2265–276.
Cocchia, D., Tiberio, G., Santrarelli, R., and Michetti, F. (1983). S-100 protein in “follicular dendritic” cells of rat lymphoid organs.Cell Tissue Res. 23095–103.
Cohen, R. S., Blomberg, F., Berzins, K., and Siekevitz, P. (1977). The structure of postsynaptic densities isolated from dog cerebral cortex. I. Overall morphology and protein composition.J. Cell Biol. 74181–203.
Cotman, C. W., and Matthews, D. A. (1971). Synaptic plasma membranes: Isolation and partial characterization.Biochim. Biophys. Acta 240380–394.
Dannies, P. S., and Levine, L. (1969). Demonstration of subunits in beef brain acidic protein (S-100).Biochem. Biophys. Res. Commun. 37587–592.
Donato, R. (1976). Further studies on the specific interaction of S-100 protein with synaptosomal particulates.J. Neurochem. 27437–447.
Donato, R. (1977). Solubilization and partial characterization of the S-100 protein binding activity of synaptosomal particulate fractions.J. Neurochem. 28553–557.
Donato, R. (1978). The specific interaction of S-100 protein with synaptosomal particulate fractions. Site-site interactions among S-100 binding sites.J. Neurochem. 301105–1111.
Donato, R. (1981). The specific interaction of S-100 protein with synaptosomal particulate fractions. Evidence of the formation of a tight complex between S-100 and its binding sites.J. Neurochem. 36532–537.
Donato, R. (1982a). Heterogeneity of the S-100 protein specific binding sites in synaptosomal fractions and subfractions.J. Neurochem. 39117–124.
Donato, R. (1982b). The specific interaction of S-100 protein with synaptosomal particulate fractions. Modulation of binding by fractional occupancy of sites and the physical state of membranes.J. Neurochem. 39125–131.
Donato, R. (1983). S-100 protein inhibits the assembly of brain microtubule (MT) proteins in vitro.J. Neurochem. 41:S93A.
Donato, R., and Michetti, F. (1974). S-100 protein in cerebral cortex synaptosomes.Experientia 30511–512.
Donato, R., Michetti, F., and Miani, N. (1975). Soluble and membrane-bound S-100 protein in cerebral cortex synaptosomes. Properties of the S-100 receptor.Brain Res. 98561–573.
Goewert, R. R., Landt, M., and McDonald, J. M. (1982). Calmodulin binding to rat adipocyte plasma membrane: Characterization and photoaffinity cross-linking of calmodulin to binding proteins.Biochemistry 215310–5315.
Gray, E. G., and Whittaker, V. P. (1962). The isolation of nerve-endings from brain: An electronmicroscopic study of cell fragments derived from homogenization and centrifugation.J. Anat. 9678–86.
Haglid, K. G., and Stavrou, D. (1973). Water soluble and pentanol extractable proteins in human brain normal tissue and human tumours, with special reference to S-100 protein.J. Neurochem. 201523–1532.
Hajòs, F. (1975). An improved method for the preparation of synaptosomal fractions in high purity.Brain Res. 93485–489.
Isobe, T., and Okuyama, T. (1978). The amino-acid sequence of S-100 protein (PAP I-b protein) and its relationship to the calcium-binding proteins.Eur. J. Biochem. 89379–388.
Isobe, T., and Okuyama, T. (1981). The amino-acid sequence of theα-subunit in bovine brain S-100a protein.Eur. J. Biochem. 11679–86.
Isobe, T., Nakajima, T., and Okuyama, T. (1977). Reinvestigation of extremely acidic proteins in bovine brain.Biochim. Biophys. Acta 494222–232.
Laurent, T. C., and Killander, J. (1964). A theory of gel filtration and its experimental verification.J. Chromatogr. 14317–330.
Linser, P., and Moscona, A. A. (1981). Developmental changes in the distribution of S-100 in avian retina.Dev. Neurosci. 4433–441.
Lowry, O. H., Rosebrough, N. J., Farr, L., and Randall, R. J. (1951). Protein measurement with the Folin phenol reagent.J. Biol. Chem. 193265–275.
Matus, A., and Mughal, S. (1975). Immunohistochemical localization of S-100 protein in brain.Nature 258746–748.
Michetti, F., and Donato, R. (1981). Subnuclear distribution of the S-100 protein specific binding sites in rat brain.J. Neurochem. 361706–1711.
Michetti, F., Miani, N., De Renzis, G., Caniglia, A., and Correr, S. (1974). Nuclear localization of S-100 protein.J Neurochem. 22239–244.
Michetti, F., Dell'Anna, E., Tiberio, G., and Cocchia, D. (1983). Immunochemical and immonocytochemical study of S-100 protein in rat adipocytes.Brain Res. 262352–356.
Moore, B. W. (1965). A soluble protein characteristic of the nervous system.Biochem. Biophys. Res. Commun. 19739–744.
Morero, R. D., and Weber, G. (1982). Interaction of bovine S-100 protein with detergents and phosphatidylcholine vesicles.Biochim. Biophys. Acta 703241–246.
Møller, M., Ingild, A., and Bock, E. (1978). Immunohistochemical demonstration of S-100 protein and GFA protein in interstitial cells of the rat pineal gland.Brain Res. 1401–13
Nakajima, T., Yamaguchi, H., and Takahashi, K. (1980). S-100 protein in foliculostellate cells of the rat pituitary anterior lobe.Brain Res. 191523–531.
Patel, J., and Marangos, P. J. (1982). Modulation of brain protein phosphorilation by the S-100 protein.Biochem. Biophys. Res. Commun. 1091089–1093.
Rosa, U., Scassellati, G. A., Pennisi, F., Riccioni, N., Giagnoni, P., and Giordani, R. (1964). Labelling of human fibrinogen with131I by electrolytic iodination.Biochim. Biophys. Acta. 86519–526.
Rusca, G., Calissano, P., and Alemà, S. (1973). Identification of a membrane-bound fraction of S-100 protein.Brain Res. 49223–227.
Stefansson, K., Wollmann, R. L., Moore, B. W., and Arnason, B. G. W. (1982). S-100 protein in human chondrocytes.Nature 29563–64.
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Donato, R. Biochemical and physicochemical properties of the solubilized S-100 protein binding activity of synaptosomal particulate fractions. Cell Mol Neurobiol 3, 239–254 (1983). https://doi.org/10.1007/BF00710950
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DOI: https://doi.org/10.1007/BF00710950