Lipid-Dependent Modulation of Ca 2+ Availability in Isolated Mossy Fiber Nerve Endings
dc.contributor.author | Ruehr, Mary Louise | en_US |
dc.contributor.author | Zhang, Lian | en_US |
dc.contributor.author | Dorman, Robert V. | en_US |
dc.date.accessioned | 2006-09-11T16:01:57Z | |
dc.date.available | 2006-09-11T16:01:57Z | |
dc.date.issued | 1997-10 | en_US |
dc.identifier.citation | Ruehr, Mary Louise; Zhang, Lian; Dorman, Robert V.; (1997). "Lipid-Dependent Modulation of Ca 2+ Availability in Isolated Mossy Fiber Nerve Endings." Neurochemical Research 22(10): 1215-1222. <http://hdl.handle.net/2027.42/45414> | en_US |
dc.identifier.issn | 0364-3190 | en_US |
dc.identifier.issn | 1573-6903 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/45414 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=9342725&dopt=citation | en_US |
dc.description.abstract | An enhancement of glutamate release from hippocampal neurons has been implicated in long-term potentiation, which is thought to be a cellular correlate of learning and memory. This phenomenom appears to be involved the activation of protein kinase C and lipid second messengers have been implicated in this process. The purpose of this study was to examine how lipid-derived second messengers, which are known to potentiate glutamate release, influence the accumulation of intraterminal free Ca 2+ , since exocytosis requires Ca 2+ and a potentiation of Ca 2+ accumulation may provide a molecular mechanism for enhancing glutamate release. The activation of protein kinase C with phorbol esters potentiates the depolarization-evoked release of glutamate from mossy fiber and other hippocampal nerve terminals. Here we show that the activation of protein kinase C also enhances evoked presynaptic Ca 2+ accumulation and this effect is attenuated by the protein kinase C inhibitor staurosporine. In addition, the protein kinase C-dependent increase in evoked Ca 2+ accumulation was reduced by inhibitors of phospholipase A 2 and voltage-sensitive Ca 2+ channels, as well as by a lipoxygenase product of arachidonic acid metabolism. That some of the effects of protein kinase C activation were mediated through phospholipase A 2 was also indicated by the ability of staurosporine to reduce the Ca 2+ accumulation induced by arachidonic acid or the phospholipase A 2 activator melittin. Similarly, the synergistic facilitation of evoked Ca 2+ accumulation induced by a combination of arachidonic acid and diacylglycerol analogs was attenuated by staurosporine. We suggest, therefore, that the protein kinase C-dependent potentiation of evoked glutamate release is reflected by increases in presynaptic Ca 2+ and that the lipid second messengers play a central role in this enhancement of chemical transmission processes. | en_US |
dc.format.extent | 841002 bytes | |
dc.format.extent | 3115 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Kluwer Academic Publishers-Plenum Publishers; Plenum Publishing Corporation ; Springer Science+Business Media | en_US |
dc.subject.other | Biomedicine | en_US |
dc.subject.other | Neurosciences | en_US |
dc.subject.other | Neurology | en_US |
dc.subject.other | Arachidonic Acid | en_US |
dc.subject.other | Protein Kinase C | en_US |
dc.subject.other | Glutamate | en_US |
dc.subject.other | Diacylglycerol | en_US |
dc.subject.other | Phospholipase a 2 , Calcium | en_US |
dc.subject.other | Biochemistry, General | en_US |
dc.title | Lipid-Dependent Modulation of Ca 2+ Availability in Isolated Mossy Fiber Nerve Endings | en_US |
dc.type | Article | en_US |
dc.subject.hlbsecondlevel | Public Health | en_US |
dc.subject.hlbsecondlevel | Psychology | en_US |
dc.subject.hlbsecondlevel | Neurosciences | en_US |
dc.subject.hlbsecondlevel | Molecular, Cellular and Developmental Biology | en_US |
dc.subject.hlbsecondlevel | Internal Medicine and Specialties | en_US |
dc.subject.hlbsecondlevel | Biological Chemistry | en_US |
dc.subject.hlbtoplevel | Social Sciences | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Biological Sciences, Kent State University, Kent, Ohio, 44242; Dept. Psychiatry, University of Michigan Medical Center, Ann Arbor, MI | en_US |
dc.contributor.affiliationother | Department of Biological Sciences, Kent State University, Kent, Ohio, 44242 | en_US |
dc.contributor.affiliationother | Department of Biological Sciences, Kent State University, Kent, Ohio, 44242 | en_US |
dc.contributor.affiliationumcampus | Ann Arbor | en_US |
dc.identifier.pmid | 9342725 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/45414/1/11064_2004_Article_413029.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1023/A:1021976828513 | en_US |
dc.identifier.source | Neurochemical Research | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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