| Item type |
デフォルトアイテムタイプ_（フル）(1) |
| 公開日 |
2023-03-18 |
| タイトル |
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|
タイトル |
Type-II 3-oxoacyl-CoA thiolase of the nematode Caenorhabditis elegans is located in peroxisomes, highly expressed during larval stages and induced by clofibrate |
|
言語 |
en |
| 作成者 |
Maebuchi, Motohiro
Togo, Summnanuna H.
Yokota, Sadaki
Ghenea, Simona
Bun-ya, Masanori
Kamiryo, Tatsuyuki
Kawahara, Akira
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| アクセス権 |
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|
アクセス権 |
open access |
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アクセス権URI |
http://purl.org/coar/access_right/c_abf2 |
| 権利情報 |
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|
権利情報 |
Copyright (c) 1999 Federation of European Biochemical Societies |
| 主題 |
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|
主題Scheme |
Other |
|
主題 |
type-II 3-oxoacyl-CoA thiolase |
| 主題 |
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主題Scheme |
Other |
|
主題 |
SCPx |
| 主題 |
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|
主題Scheme |
Other |
|
主題 |
peroxisomes |
| 主題 |
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主題Scheme |
Other |
|
主題 |
clofibrate |
| 主題 |
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主題Scheme |
Other |
|
主題 |
caenorhabditis elegans |
| 主題 |
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主題Scheme |
NDC |
|
主題 |
460 |
| 内容記述 |
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|
内容記述 |
We examined the expression and localization of type-II 3-oxoacyl-CoA thiolase in the nematode Caenorhabditis elegans. Type-II thiolase acts on 3- oxoacyl-CoA esters with a methyl group at the α carbon, whereas conventional thiolases do not. Mammalian type-II thiolase, which is also termed sterol carrier protein x (SCPx) or SCP2/3-oxoacyl-CoA thiolase, is located in the peroxisomes and involved in phytanic acid degradation and most probably in bile acid synthesis. The nematode enzyme lacks the SCP2 domain, which carries the peroxisomal-targeting signal, but produces bile acids in a cell-free system. Northern and Western blot analyses demonstrated that C. elegans expressed type-II thiolase throughout its life cycle, especially during the larval stages, and that the expression was significantly enhanced by the addition of clofibrate at 5 mM or more to the culture medium. Whole-mount in situ hybridization and immunostaining of L4 larvae revealed that the enzyme was mainly expressed in intestinal cells, which are multifunctional like many of the cell types in C. elegans. Subcellular fractionation and indirect immunoelectron microscopy of the nematode detected the enzyme in the matrix of peroxisomes. These results indicate the fundamental homology between mammalian SCPx and the nematode enzyme regardless of whether the SCP2 part is fused, suggesting their common physiological roles. |
|
言語 |
en |
| 出版者 |
|
|
出版者 |
Federation of European Biochemical Societies |
| 言語 |
|
|
言語 |
eng |
| 資源タイプ |
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資源タイプ識別子 |
http://purl.org/coar/resource_type/c_6501 |
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資源タイプ |
journal article |
| 出版タイプ |
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|
出版タイプ |
AO |
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出版タイプResource |
http://purl.org/coar/version/c_b1a7d7d4d402bcce |
| 関連情報 |
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|
識別子タイプ |
DOI |
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関連識別子 |
10.1046/j.1432-1327.1999.00655.x |
| 関連情報 |
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|
識別子タイプ |
PMID |
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関連識別子 |
10491098 |
| 関連情報 |
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|
関連タイプ |
isVersionOf |
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|
識別子タイプ |
DOI |
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|
関連識別子 |
http://dx.doi.org/10.1046/j.1432-1327.1999.00655.x |
| 収録物識別子 |
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収録物識別子タイプ |
ISSN |
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収録物識別子 |
0014-2956 |
| 収録物識別子 |
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収録物識別子タイプ |
NCID |
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収録物識別子 |
AA00639541 |
| 開始ページ |
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開始ページ |
509 |
| 書誌情報 |
European Journal of Biochemistry
European Journal of Biochemistry
巻 264,
号 2,
p. 509-515,
発行日 1999
|
| 旧ID |
14888 |
ejb_264_509.pdf (5.5 MB)
