Compartmentation of the mouse cerebellar cortex by sphingosine kinase
Identifieur interne : 002C79 ( Main/Exploration ); précédent : 002C78; suivant : 002C80Compartmentation of the mouse cerebellar cortex by sphingosine kinase
Auteurs : Nobuo Terada [Japon] ; Yoshiko Banno [Japon] ; Nobuhiko Ohno [Japon] ; Yasuhisa Fujii [Japon] ; Takashi Murate [Japon] ; Justyna R. Sarna [Canada] ; Richard Hawkes [Canada] ; Zagreb Zea [Japon] ; Takeshi Baba [Japon] ; Shinichi Ohno [Japon]Source :
- Journal of Comparative Neurology [ 0021-9967 ] ; 2004-01-26.
English descriptors
Abstract
Classic cerebellar anatomy is based on the characteristic array of lobes and lobules. However, there is substantial evidence to suggest that more fundamental architecture is built around arrays of parasagittal stripes, which encompass both the inputs and outputs of the Purkinje cells (PCs). Sphingosine kinase (SPHK) is an enzyme that converts sphingosine (Sph) into sphingosine‐1‐phosphate (S1P). Recent reports have indicated that ceramide, Sph, and S1P play a role in cell survival, growth, and differentiation in several cell types, including neurons. In this study, we examined the localization of SPHK in the mouse cerebellum by using immunohistochemistry. Anti‐SPHK immunoreactivity appeared in the cerebellar molecular layer and the PC membranes. The staining pattern is striped. In the molecular layer, the staining pattern probably reflects dendritic spines and dendrites. By electron microscopy, peroxidase reaction product was deposited within dendrites especially along the plasma membranes near spines. Seen at higher magnification, the staining was in and near the postsynaptic complexes. By double immunostaining, the striped pattern of SPHK expression was shown to be identical to that revealed by anti‐zebrin II, although the subcellular distribution within PC's is not. This is the first demonstration of the cerebellar compartmentation of an enzyme related to lipid metabolism, and as such, it provides an insight into the roles of SPHK and formation of S1P. The selective expression of SPHK in the zebrin II‐immunoreactive PCs may explain their resistance to cell death when ceramide metabolism is disrupted, as in the acid sphingomyelinase knockout model of Niemann‐Pick type A/B disease. J. Comp. Neurol. 469:119–127, 2004. © 2003 Wiley‐Liss, Inc.
Url:
DOI: 10.1002/cne.11002
Affiliations:
- Canada, Japon
- Alberta, Préfecture de Gifu, Région du Chūbu
- Calgary, Gifu (ville)
- Université de Calgary, Université de Gifu
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However, there is substantial evidence to suggest that more fundamental architecture is built around arrays of parasagittal stripes, which encompass both the inputs and outputs of the Purkinje cells (PCs). Sphingosine kinase (SPHK) is an enzyme that converts sphingosine (Sph) into sphingosine‐1‐phosphate (S1P). Recent reports have indicated that ceramide, Sph, and S1P play a role in cell survival, growth, and differentiation in several cell types, including neurons. In this study, we examined the localization of SPHK in the mouse cerebellum by using immunohistochemistry. Anti‐SPHK immunoreactivity appeared in the cerebellar molecular layer and the PC membranes. The staining pattern is striped. In the molecular layer, the staining pattern probably reflects dendritic spines and dendrites. By electron microscopy, peroxidase reaction product was deposited within dendrites especially along the plasma membranes near spines. Seen at higher magnification, the staining was in and near the postsynaptic complexes. By double immunostaining, the striped pattern of SPHK expression was shown to be identical to that revealed by anti‐zebrin II, although the subcellular distribution within PC's is not. This is the first demonstration of the cerebellar compartmentation of an enzyme related to lipid metabolism, and as such, it provides an insight into the roles of SPHK and formation of S1P. The selective expression of SPHK in the zebrin II‐immunoreactive PCs may explain their resistance to cell death when ceramide metabolism is disrupted, as in the acid sphingomyelinase knockout model of Niemann‐Pick type A/B disease. J. Comp. Neurol. 469:119–127, 2004. © 2003 Wiley‐Liss, Inc.</div></front></TEI><affiliations><list><country><li>Canada</li><li>Japon</li></country><region><li>Alberta</li><li>Préfecture de Gifu</li><li>Région du Chūbu</li></region><settlement><li>Calgary</li><li>Gifu (ville)</li></settlement><orgName><li>Université de Calgary</li><li>Université de Gifu</li></orgName></list><tree><country name="Japon"><noRegion><name sortKey="Terada, Nobuo" sort="Terada, Nobuo" uniqKey="Terada N" first="Nobuo" last="Terada">Nobuo Terada</name></noRegion><name sortKey="Baba, Takeshi" sort="Baba, Takeshi" uniqKey="Baba T" first="Takeshi" last="Baba">Takeshi Baba</name><name sortKey="Banno, Yoshiko" sort="Banno, Yoshiko" uniqKey="Banno Y" first="Yoshiko" last="Banno">Yoshiko Banno</name><name sortKey="Fujii, Yasuhisa" sort="Fujii, Yasuhisa" uniqKey="Fujii Y" first="Yasuhisa" last="Fujii">Yasuhisa Fujii</name><name sortKey="Murate, Takashi" sort="Murate, Takashi" uniqKey="Murate T" first="Takashi" last="Murate">Takashi Murate</name><name sortKey="Ohno, Nobuhiko" sort="Ohno, Nobuhiko" uniqKey="Ohno N" first="Nobuhiko" last="Ohno">Nobuhiko Ohno</name><name sortKey="Ohno, Shinichi" sort="Ohno, Shinichi" uniqKey="Ohno S" first="Shinichi" last="Ohno">Shinichi Ohno</name><name sortKey="Terada, Nobuo" sort="Terada, Nobuo" uniqKey="Terada N" first="Nobuo" last="Terada">Nobuo Terada</name><name sortKey="Zea, Zagreb" sort="Zea, Zagreb" uniqKey="Zea Z" first="Zagreb" last="Zea">Zagreb Zea</name></country><country name="Canada"><region name="Alberta"><name sortKey="Sarna, Justyna R" sort="Sarna, Justyna R" uniqKey="Sarna J" first="Justyna R." last="Sarna">Justyna R. Sarna</name></region><name sortKey="Hawkes, Richard" sort="Hawkes, Richard" uniqKey="Hawkes R" first="Richard" last="Hawkes">Richard Hawkes</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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