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Barium and Calcium Stimulate Secretion from Digitonin-Permeabilized Bovine Adrenal Chromaffin Cells by Similar Pathways

dc.contributor.authorTerBush, Daniel R.en_US
dc.contributor.authorHolz, Ronald W.en_US
dc.date.accessioned2010-04-01T15:49:44Z
dc.date.available2010-04-01T15:49:44Z
dc.date.issued1992-02en_US
dc.identifier.citationTerBush, Daniel R.; Holz, Ronald W. (1992). "Barium and Calcium Stimulate Secretion from Digitonin-Permeabilized Bovine Adrenal Chromaffin Cells by Similar Pathways." Journal of Neurochemistry 58(2): 680-687. <http://hdl.handle.net/2027.42/66323>en_US
dc.identifier.issn0022-3042en_US
dc.identifier.issn1471-4159en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/66323
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=1729410&dopt=citationen_US
dc.description.abstractWe compared the characteristics of secretion stimulated by EGTA-buffered Ba 2+ - and Ca 2+ -containing solutions in digitonin-permeabilized bovine adrenal chromaffin cells. Half-maximal secretion occurred at approximately 100 Μ M Ba 2+ or 1 Μ M Ca 2+ . Ba 2+ -stimulated release was not due to release of sequestered intracellular Ca 2+ because at a constant free Ba 2+ concentration, increasing unbound EGTA did not diminish the extent of release due to Ba 2+ . The maximal extents of Ba 2+ - and Ca 2+ -dependent secretion in the absence of MgATP were identical. MgATP enhanced Ba 2+ -induced secretion to a lesser extent than Ca 2+ -induced secretion. Half-maximal concentrations of Ba 2+ and Ca 2+ , when added together to cells, yielded approximately additive amounts of secretion. Maximal concentrations of Ba 2+ and Ca 2+ when added together to cells for 2 or 15 min were not additive. Tetanus toxin inhibited Ba 2+ - and Ca 2+ -dependent secretion to a similar extent. Ba 2+ , unlike Ca 2+ , did not activate polyphosphoinositide-specific phospholipase C. These data indicate that (1) Ba 2+ directly stimulates exocytosis, (2) Ba 2+ -induced secretion is stimulated to a lesser extent than Ca 2+ -dependent secretion by MgATP, (3) Ba 2+ and Ca 2+ use similar pathways to trigger exocytosis, and (4) exocytosis from permeabilized cells does not require activation of polyphosphoinositide-specific phospholipase C.en_US
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dc.format.extent3110 bytes
dc.format.mimetypeapplication/pdf
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dc.publisherBlackwell Publishing Ltden_US
dc.rights1992 International Society for Neurochemistryen_US
dc.subject.otherATPen_US
dc.subject.otherBariumen_US
dc.subject.otherCalciumen_US
dc.subject.otherChromaffin Cellen_US
dc.subject.otherExocytosisen_US
dc.subject.otherTetanus Toxinen_US
dc.titleBarium and Calcium Stimulate Secretion from Digitonin-Permeabilized Bovine Adrenal Chromaffin Cells by Similar Pathwaysen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelNeurosciencesen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumDepartment of Pharmacology, University of Michigan, Ann Arbor, Michigan, U.S.A.en_US
dc.identifier.pmid1729410en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/66323/1/j.1471-4159.1992.tb09771.x.pdf
dc.identifier.doi10.1111/j.1471-4159.1992.tb09771.xen_US
dc.identifier.sourceJournal of Neurochemistryen_US
dc.identifier.citedreferenceAli S. M., Geisow M. J., and Burgoyne R. D. ( 1989 ) A role for calpactin in calcium-dependent exocytosis in adrenal chromaffin cells. Nature 340, 313 – 315.en_US
dc.identifier.citedreferenceAmy C. M. and Kirshner N. ( 1981 ) Phosphorylation of adrenal medulla cell proteins in conjunction with stimulation of catecholamine secretion. J. Neurochem. 36, 847 – 854.en_US
dc.identifier.citedreferenceArtalejo C. R., Garcia A. G., and Aunis D. ( 1987 ) Chromaffin cell calcium channel kinetics measured isotopically through fast calcium, strontium and barium fluxes. J. Biol. Chem. 262, 915 – 926.en_US
dc.identifier.citedreferenceBjerrum J., Schwarzenbach G., and SillÉn L. G. ( 1957 ) Stability Constants, Part I: Organic Ligands, p. 98. The Chemical Society, London.en_US
dc.identifier.citedreferenceBrooks J. C. and Treml S. ( 1983 ) Catecholamine secretion by chemically skinned cultured chromaffin cells. J. Neurochem. 40, 468 – 473.en_US
dc.identifier.citedreferenceChang D., Hsieh P. S., and Dawson D. C. ( 1988 ) Calcium: a program in BASIC for calculating the composition of solutions with specified free concentrations of calcium, magnesium and other divalent cations. Comput. Biol. Med. 18, 351 – 366.en_US
dc.identifier.citedreferenceChao S.-H., Suzuki Y., Zysk J. R., and Cheung W. Y. ( 1984 ) Activation of calmodulin by various metal cations as a function of ionic radius. Mol. Pharmacol. 26, 75 – 82.en_US
dc.identifier.citedreferenceCote A., Doucet J. P., and TrifarÓ J. M. ( 1986 ) Phosphorylation and dephosphorylation of chromaffin cell proteins in response to stimulation. Neuroscience 19, 629 – 645.en_US
dc.identifier.citedreferenceCreutz C. E., Pazoles C. J., and Pollard H. B. ( 1979 ) Self-association of synexin in the presence of calcium: correlation with synexin-induced membrane fusion and examination of the structure of synexin aggregates. J. Biol. Chem. 254, 553 – 558.en_US
dc.identifier.citedreferenceDavidson J. S., Wakefield I., King J. A., and Millar R. P. ( 1987 ) Barium-induced LH release from chicken pituitary cells: synergism with phorbol ester. J. Endocrinol. 114, 11 – 16.en_US
dc.identifier.citedreferenceDouglas W. W. and Rubin R. P. ( 1964a ) The effects of alkaline earths and other divalent cations on adrenal medullary secretion. J. Physiol. 175, 231 – 241.en_US
dc.identifier.citedreferenceDouglas W. W. and Rubin R. P. ( 1964b ) Stimulant action of barium on the adrenal medulla. Nature 203, 305 – 307.en_US
dc.identifier.citedreferenceDunn L. A. and Holz R. W. ( 1983 ) Catecholamine secretion from digitonin-treated adrenal chromaffin cells. J. Biol. Chem. 258, 4989 – 4993.en_US
dc.identifier.citedreferenceEberhard D. A. and Holz R. W. ( 1987 ) Cholinergic stimulation of inositol phosphate formation in bovine adrenal chromaffin cells: distinct nicotinic and muscarinic mechanisms. J. Neurochem. 49, 1634 – 1643.en_US
dc.identifier.citedreferenceEberhard D. A., Cooper C. L., Low M. G., and Holz R. W. ( 1990 ) Evidence that the inositol phospholipids are necessary for exocytosis. Biochem. J. 268, 15 – 25.en_US
dc.identifier.citedreferenceFrye R. A. and Holz R. W. ( 1984 ) The relationship between arachidonic acid release and catecholamine secretion from cultured bovine adrenal chromaffin cells. J. Neurochem. 43, 146 – 150.en_US
dc.identifier.citedreferenceFrye R. A. and Holz R. W. ( 1985 ) Arachidonic acid release and catecholamine secretion from digitonin-treated chromaffin cells: effects of micromolar calcium, phorbol ester, and protein alkylating agents. J. Neurochem. 44, 265 – 273.en_US
dc.identifier.citedreferenceHales C. N. and Milner R. D. G. ( 1968 ) Cations and the secretion of insulin from rabbit pancreas in vitro. J. Physiol. (Lond.) 199, 177 – 197.en_US
dc.identifier.citedreferenceHeldman E., Levine M., Raveh L., and Pollard H. B. ( 1989 ) Barium ions enter chromaffin cells via voltage-dependent calcium channels and induce secretion by a mechanism independent of calcium. J. Biol. Chem. 264, 7914 – 7920.en_US
dc.identifier.citedreferenceHolz R. W., Senter R. A., and Frye R. A. ( 1982 ) Relationship between Ca 2+ uptake and catecholamine secretion in primary dissociated cultures of adrenal medulla. J. Neurochem. 39, 635 – 646.en_US
dc.identifier.citedreferenceHolz R. W., Bittner M. A., Peppers S. C., Senter R. A., and Eberhard D. A. ( 1989 ) MgATP-independent and MgATP-dependent exocytosis. J. Biol. Chem. 264, 5412 – 5419.en_US
dc.identifier.citedreferenceIzumi F., Toyohira Y., Yanagihara N., Wada A., and Kobayashi H. ( 1986 ) Barium-evoked release of catecholamines from digitonin-permeabilized adrenal medullary cells. Neurosci. Lett. 69, 172 – 175.en_US
dc.identifier.citedreferenceKao L.-S. and Schneider A. S. ( 1986 ) Calcium mobilization and catecholamine secretion in adrenal chromaffin cells. J. Biol. Chem. 261, 4881 – 4888.en_US
dc.identifier.citedreferenceKilpatrick D. L., Slepetis R. J., Corcoran J. J., and Kirshner N. ( 1982 ) Calcium uptake and catecholamine secretion by cultured bovine adrenal medulla cells. J. Neurochem. 38, 427 – 435.en_US
dc.identifier.citedreferenceKnight D. E. and Baker P. F. ( 1982 ) Calcium-dependence of catecholamine release from bovine adrenal medullary cells after exposure to intense electric fields. J. Membr. Biol. 68, 107 – 140.en_US
dc.identifier.citedreferenceKnight D. E. and Kesteven N. T. ( 1983 ) Evoked transient intracellular free Ca 2+ changes and secretion in isolated adrenal medullary cells. Proc. R. Soc. Lond. [Biol. Sci.] 218, 177 – 199.en_US
dc.identifier.citedreferenceKnight D. E., Tonge D. A., and Baker P. F. ( 1985 ) Inhibition of exocytosis in bovine adrenal medullary cells by botulinum toxin type D. Nature 317, 719 – 721.en_US
dc.identifier.citedreferenceKnight D. E., Sugden D., and Baker P. F. ( 1988 ) Evidence implicating protein kinase C in exocytosis from electropermeabilized bovine chromaffin cells. J. Membr. Biol. 104, 21 – 34.en_US
dc.identifier.citedreferenceLee S. A. and Holz R. W. ( 1986 ) Protein phosphorylation and secretion in digitonin-permeabilized adrenal chromaffin cells: effects of micromolar Ca 2+, phorbol esters, and diacylglycerol. J. Biol. Chem. 261, 17089 – 17098.en_US
dc.identifier.citedreferenceMatthies H. J., Palfrey H. C., and Miller R. J. ( 1988 ) Calmodulin- and protein phosphorylation-independent release of catecholamines from PC12 cells. FEBS Lett. 229, 238 – 242.en_US
dc.identifier.citedreferenceMorgan A. and Burgoyne R. D. ( 1990 ) Stimulation of Ca 2+ -independent catecholamine secretion from digitonin-permeabilized bovine adrenal chromaffin cells by guanine nucleotide analogues. Relationship to arachidonate release. Biochem. J. 269, 521 – 526.en_US
dc.identifier.citedreferenceMorita K., Ishii S., Uda H., and Oka M. ( 1988 ) Requirement of ATP for exocytotic release of catecholamines from digitonin-permeabilized adrenal chromaffin cells. J. Neurochem. 50, 644 – 648.en_US
dc.identifier.citedreferencePocotte S. L., Holz R. W., and Ueda T. ( 1986 ) Cholinergic receptor-mediated phosphorylation and activation of tyrosine hydroxylase in cultured bovine adrenal chromaffin cells. J. Neurochem. 46, 610 – 622.en_US
dc.identifier.citedreferenceSarafian T., Aunis D., and Bader M.-F. ( 1987 ) Loss of proteins from digitonin-permeabilized adrenal chromaffin cells essential for exocytosis. J. Biol. Chem. 262, 16671 – 16676.en_US
dc.identifier.citedreferenceSasakawa N., Nakaki T., Yamamoto S., and Kato R. ( 1989 ) Calcium uptake-dependent and -independent mechanisms of inositol trisphosphate formation in adrenal chromaffin cells: comparative studies with high K +, carbamylcholine and angiotensin II. Cell. Signal. 1, 75 – 84.en_US
dc.identifier.citedreferenceSÜdhof T. C., Walker J. H., and Obrocki J. ( 1982 ) Calelectrin self-aggregates and promotes membrane aggregation in the presence of calcium. EMBO J. 1, 1167 – 1170.en_US
dc.identifier.citedreferenceTerBush D. R. and Holz R. W. ( 1990 ) Activation of protein kinase C is not required for exocytosis from bovine adrenal chromaffin cells: the effects of PKC(19-31), Ca/CaM kinase II(291-317) and staurosporine. J. Biol. Chem. 265, 21179 – 21184.en_US
dc.identifier.citedreferencevan der Merwe P. A., Millar R. P., and Davidson J. S. ( 1990 ) Calcium stimulates luteinizing-hormone (lutropin) exocytosis by a mechanism independent of protein kinase C. Biochem. J. 268, 493 – 498.en_US
dc.identifier.citedreferenceWaymire J. C., Bennett W. F., Boehme R., Hanteins L., Gilmer-Waymire K., and Haycock J. ( 1983 ) Bovine adrenal chromaffin cells: high-yield purification and viability in suspension culture. J. Neurosci. Methods 7, 329 – 351.en_US
dc.identifier.citedreferenceWilson S. P. and Kirshner N. ( 1977 ) The acetylcholine receptor of the adrenal medulla. J. Neurochem. 28, 687 – 695.en_US
dc.identifier.citedreferenceWilson S. P. and Kirshner N. ( 1983 ) Calcium-evoked secretion from digitonin-permeabilized adrenal medullary chromafin cells. J. Biol. Chem. 258, 4994 – 5000.en_US
dc.identifier.citedreferenceZaks W. J. and Creutz C. E. ( 1990 ) Annexin-chromaffin granule membrane interations: a comparative study of synexin, p32 and p67. Biochem. Biophys. Acta 1029, 149 – 160.en_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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