Cytochalasin B inhibits phosphoinositide hydrolysis in rat hippocampal slices
Tóm tắt
The effect of cytochalasin B on phosphoinositide (PI) hydrolysis was examined in rat hippocampal slices. Pretreatment of the slices with cytochalasin B caused a significant decrease in PI hydrolysis elicited by carbachol, norepinephrine, or by high K+. This effect was cytochalasin B dose- and time-dependent and was not mimicked by cytochalasin D, vinblastine, colchicine, or phloretin. In contrast, in [3H]inositol-prelabeled hippocampal membranes, cytochalasin B did not affect PI hydrolysis elicited by GTPγS and GTPγS plus carbachol. Similar result was obtained using the membranes prepared from the slices pretreated with cytochalasin B. The inhibitory effect of cytochalasin B on the carbachol-response was observed in SK-N-SH human neuroblastoma cells, but not in cultured rat astrocytes. These results indicate that cytochalasin B inhibits PI hydrolysis in neuron-specific manner and that its action may be an indirect cellular mechanism other than interaction with cytoskeleton elements.
Tài liệu tham khảo
Carraway, K. L., and Carraway, C. A. C. 1988. Membranecytoskeleton interactions in animal cells. Biochim. Biophys. Acta 988:147–171.
Rasenick, M. M., Stein, P. J., and Bitensky, M. W., 1981. The regulatory subunit of adenylate cyclase interacts with cytoskeletal components. Nature 294:560–562.
Berridge, M. J., and Irvine, R. F. 1989. Inositol phosphates and cell signalling, Nature 341:197–205.
Flanagan, M. D., and Lin, S. 1980. Cytochalasins block actin filament elongation by binding to high affinity sites associated with F-actin. J. Biol. Chem. 255:835–838.
MacLean-Fletcher, S., and Pollard, T. D. 1980. Mechanism of action of cytochalasin B on actin. Cell 20:329–341.
Spooner, B. S., and Wessells, N. K. 1970. Effects of cytochalasin B upon microfilaments involved in morphogenesis of salivary epithelium. Proc. Natl. Acad. Sci. USA 66:360–364.
Davis, A. T., Estensen, R., and Quie, P. g. 1970. Cytochalasin B III. Inhibition of human polymorphonuclear leukocyte phagocytosis. Proc. Soc. Exp. Biol. Med. 137:161–164.
Wagner, R., Rosenberg, M., and Estensen, R. 1971. Endocytosis in Chang liver cells. Quantitation by sucrose-3H uptake and inhibition by cytochalasin B. J. Cell Biol. 50:804–817.
De Sousa, P. A., and Masui, Y. 1990. The effect of cytochalasin D on protein synthesis in Xenopus laevis oocytes. Mol. Reprod. Dev. 26:248–252.
Williams, J. A., and Wolff, J. 1971. Cytochalasin B inhibits thyroid secretion. Biochem. Biophys. Res. Commun. 44:422–425.
Siess, W., Lapetina, E. G., and Cuatrecasas, P. 1982. Cytochalasins inhibit arachidonic acid metabolism in thrombin-stimulated platelets. Proc. Natl. Acad. Sci. USA 79:7709–7713.
Baudry, M., Evans, J., and Lynch, G. 1986. Excitatory amino acids inhibit stimulation of phosphatidylinositol metabolism by aminergic agonists in hippocampus. Nature 319:329–331.
Claro, E., Garcia, A., and Picatoste, F. 1989. Carbachol and histamine stimulation of guanine-nucleotide-dependent phosphoinositide hydrolysis in rat brain cortical membranes. Biochem. J. 261:29–35.
Kitanaka, J., Onoe, H., and Baba, A. 1991. Astrocytes possess prostaglandin F2α receptors coupled to phospholipase C. Biochem. Biophys. Res. Commun. 178:946–952.
Richards, M. L., and Sadee, W. 1986. Human neuroblastoma cell lines as models of catechol uptake. Brain Res. 384:132–137.
Etoh, S., Ohashi, M., Baba, A., and Iwata, H. 1990. Inhibition by ibudilast of leukotriene D4-induced formation of inositol phosphates in guinea-pig lung. Br. J. Pharmacol. 100:564–568.
Fox, J. E. B., and Phillips, D. R. 1981. Inhibition of actin polymerization in blood platelets by cytochalasins. Nature 292:650–652.
Jung, C. Y., and Rampal, A. L. 1977. Cytochalasin B binding sites and glucose transport carrier in human erythrocyte ghosts. J. Biol. Chem. 252:5456–5463.
Estensen, R. D., Rosenberg, M., and Sheridan, J. D. 1971. Cytochalasin B: Microfilaments and “contractile” processes. Science 173:356–358.
Weisenberg, R. C., Borisy, G. G., and Taylor, E. W. 1968. The colchicine-binding protein of mammalian brain and its relation to microtubules. Biochemistry 7:4466–4479.
Owellen, R. J., Owens, Jr., A. H., and Donigian, D. W. 1972. The binding of vincristine, vinblastine and colchicine to tubulin. Biochem. Biophys. Res. Commun. 47:685–691.
Wilson, L., Creswell, K. M., and Chin, D. 1975. The mechanism of action of vinblastine. Binding of [acetyl-3H]vinblastine to embryonic chick brain tubulin and tubulin from sea urchin sperm tail outer doublet microtubules. Biochemistry 14:5586–5592.
Huleux, C., Dreux, C., Imhoff, V., Chambaut-Guerin, A.-M., and Rossignol, B. 1989. Microfilaments and cellular signal transduction: effect of cytochalasin D on the production of cAMP, inositol phosphates, and on calcium movements in rat parotid glands. Biol. Cell 67:61–65.
Deckmyn, H., Tu, S.-M., and Majerus, P. W., 1986. Guanine nucleotides stimulate soluble phosphoinositide-specific phospholipase C in the absence of membranes J. Biol. Chem. 261:16553–16558.
Fowler C. J., and Tiger, G. 1991. Modulation of receptor-mediated inositol phospholipid breakdown in the brain. Neurochem Int. 19:171–206.