Synapsin I Is Associated with Cholinergic Nerve Terminals in the Electric Organs of Torpedo, Electrophorus , and Malapterurus and Copurifies with Torpedo Synaptic Vesicles
dc.contributor.author | Volknandt, W. | en_US |
dc.contributor.author | Naito, Shigetaka | en_US |
dc.contributor.author | Ueda, Tetsufumi | en_US |
dc.contributor.author | Zimmermann, H. | en_US |
dc.date.accessioned | 2010-04-01T15:50:50Z | |
dc.date.available | 2010-04-01T15:50:50Z | |
dc.date.issued | 1987-08 | en_US |
dc.identifier.citation | Volknandt, W.; Naito, S.; Ueda, T.; Zimmermann, H. (1987). "Synapsin I Is Associated with Cholinergic Nerve Terminals in the Electric Organs of Torpedo, Electrophorus , and Malapterurus and Copurifies with Torpedo Synaptic Vesicles." Journal of Neurochemistry 49(2): 342-347. <http://hdl.handle.net/2027.42/66342> | en_US |
dc.identifier.issn | 0022-3042 | en_US |
dc.identifier.issn | 1471-4159 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/66342 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=3110371&dopt=citation | en_US |
dc.description.abstract | Using an affinity-purified monospecific polyclonal antibody against bovine brain synapsin I, the distribution of antigenically related proteins was investigated in the electric organs of the three strongly electric fish Torpedo marmorata, Electrophorus electricus, Malapterurus electricus and in the rat diaphragm. On application of indirect fluorescein isothiocyanate-immunofluorescence and using Α-bungarotoxin for identification of synaptic sites, intense and very selective staining of nerve terminals was found in all of these tissues. Immunotransfer blots of tissue homogenates revealed specific bands whose molecular weights are similar to those of synapsin Ia and synapsin Ib. Moreover, synapsin I-like proteins are still attached to the synaptic vesicles that were isolated in isotonic glycine solution from Torpedo electric organ by density gradient centrifugation and chromatography on Sephacryl-1000. Our results suggest that synapsin I-like proteins are also associated with cholinergic synaptic vesicles of electric organs and that the electric organ may be an ideal source for studying further the functional and molecular properties of synapsin I. | en_US |
dc.format.extent | 1342953 bytes | |
dc.format.extent | 3110 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.publisher | Blackwell Publishing Ltd | en_US |
dc.rights | 1987 International Society for Neurochemistry Ltd. | en_US |
dc.subject.other | Synapsin I | en_US |
dc.subject.other | Protein I | en_US |
dc.subject.other | Torpedo | en_US |
dc.subject.other | Synaptic Vesicles | en_US |
dc.subject.other | Acetylcholine | en_US |
dc.subject.other | Electrophorus | en_US |
dc.subject.other | Malapterurus | en_US |
dc.title | Synapsin I Is Associated with Cholinergic Nerve Terminals in the Electric Organs of Torpedo, Electrophorus , and Malapterurus and Copurifies with Torpedo Synaptic Vesicles | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Neurosciences | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | * Mental Health Research Institute, University of Michigan, Ann Arbor, Michigan, U.S.A. | en_US |
dc.contributor.affiliationother | AK Neurochemie, Zoologisches Institut der J. W. Goethe-UniversitÄt, Frankfurt am Main, F.R.G. | en_US |
dc.identifier.pmid | 3110371 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/66342/1/j.1471-4159.1987.tb02871.x.pdf | |
dc.identifier.doi | 10.1111/j.1471-4159.1987.tb02871.x | en_US |
dc.identifier.source | Journal of Neurochemistry | en_US |
dc.identifier.citedreference | Baines A. J. and Bennet V. ( 1985 ) Synapsin I is a spectrin-binding protein immunologically related to erythrocyte protein 4.1. Nature 315, 410 – 413. | en_US |
dc.identifier.citedreference | Baines A. J. and Bennet V. ( 1986 ) Synapsin I is a microtubule-bundling protein. Nature 319, 145 – 147. | en_US |
dc.identifier.citedreference | De Camilli P., Cameron R., and Greengard P. ( 1983a ) Synapsin I (protein I), a nerve terminal-specific phosphoprotein. I. Its general distribution in synapses of the central and peripheral nervous system demonstrated by immunofluorescence in frozen and plastic sections. J. Cell Biol. 96, 1337 – 1354. | en_US |
dc.identifier.citedreference | De Camilli P., Harris S. M., Huttner W. B., and Greengard P. ( 1983b ) Synapsin I (protein I), a nerve terminal-specific phosphoprotein. II. Its specific association with synaptic vesicles demonstrated by immunocytochemistry in agarose-embedded synaptosomes. J. Cell Biol. 96, 1355 – 1373. | en_US |
dc.identifier.citedreference | Goelz S. E., Nestler E. J., and Greengard P. ( 1985 ) Phylogenetic survey of proteins related to synapsin I and biochemical analysis of four such proteins from fish brain. J. Neurochem. 45, 63 – 72. | en_US |
dc.identifier.citedreference | Huttner W. B., Schiebler W., Greengard P., and De Camilli P. ( 1983 ) Synapsin I (Protein I), a nerve terminal-specific phosphoprotein. III. Its association with synaptic vesicles studied in a highly purified synaptic vesicle preparation. J. Cell Biol. 96, 1374 – 1388. | en_US |
dc.identifier.citedreference | Janetzko A., Zimmermann H., and Volknandt W. ( 1987 ) The electromotor system of the electric catfish ( Malapterurus electricus ). A fine structural analysis. Cell Tissue Res. 247, 613 – 624. | en_US |
dc.identifier.citedreference | Laemmli U. K. ( 1970 ) Cleavage of structural proteins during the assembly of the head of bacteriophage T 4. Nature 227, 680 – 685. | en_US |
dc.identifier.citedreference | Llinas R., McGuiness T. L., Leonard C. S., Sugimori M., and Greengard P. ( 1985 ) Intraterminal injection of synapsin I or calcium/calmodulin-dependent protein kinase II alters neuro-transmitter release at the squid giant synapse. Proc. Natl. Acad. Sci. USA 82, 3035 – 3039. | en_US |
dc.identifier.citedreference | Naito S. and Ueda T. ( 1983 ) Adenosine triphosphate-dependent uptake of glutamate into protein I-associated synaptic vesicles. J. Biol. Chem. 258, 696 – 699. | en_US |
dc.identifier.citedreference | Naito S. and Ueda T. ( 1985 ) Characterization of glutamate uptake into synaptic vesicles. J. Neurochem. 44, 99 – 109. | en_US |
dc.identifier.citedreference | Schmidt R., Zimmermann H., and Whittaker V. P. ( 1980 ) Metal ion content of cholinergic synaptic vesicles isolated from the electric organ of Torpedo : effect of stimulation-induced transmitter release. Neuroscience 5, 625 – 638. | en_US |
dc.identifier.citedreference | Ueda T. and Greengard P. ( 1977 ) Adenosine 3′:5′-monophosphate-regulated phosphoprotein system of neuronal membranes. I. Solubilization, purification, and some properties of an endogenous phosphoprotein. J. Biol. Chem. 252, 5155 – 5163. | en_US |
dc.identifier.citedreference | Ueda T. and Naito S. ( 1982 ) Specific inhibition of the phosphorylation of protein I, a synaptic protein, by affinity-purified anti-protein I antibody. Prog. Brain Res. 56, 87 – 103. | en_US |
dc.identifier.citedreference | Ueda T., Greengard P., Berzins K., Cohen R. S., Blomberg F., Grab D. J., and Siekevitz P. ( 1979 ) Subcellular distribution in cerebral cortex of two proteins phosphorylated by cAMP-dependent protein kinase. J. Cell Biol. 83, 308 – 319. | en_US |
dc.identifier.citedreference | Volknandt W. and Zimmermann H. ( 1986 ) Acetylcholine, ATP and proteoglycan are common to synaptic vesicles isolated from the electric organs of electric eel and electric catfish as well as from rat diaphragm. J. Neurochem. 47, 1449 – 1462. | en_US |
dc.identifier.citedreference | Zimmermann H. ( 1982 ) Biochemistry of the isolated cholinergic vesicles, in Neurotransmitter Vesicles ( Klein R. L., Lagercrantz H., and Zimmermann H., eds ), pp. 271 – 304. Academic Press, London. | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
Files in this item
Remediation of Harmful Language
The University of Michigan Library aims to describe library materials in a way that respects the people and communities who create, use, and are represented in our collections. Report harmful or offensive language in catalog records, finding aids, or elsewhere in our collections anonymously through our metadata feedback form. More information at Remediation of Harmful Language.
Accessibility
If you are unable to use this file in its current format, please select the Contact Us link and we can modify it to make it more accessible to you.