Type-II 3-oxoacyl-CoA thiolase of the nematode Caenorhabditis elegans is located in peroxisomes, highly expressed during larval stages and induced by clofibrate

European Journal of Biochemistry Volume 264 Issue 2 Page 509-515 published_at 1999
アクセス数 : 720
ダウンロード数 : 157

今月のアクセス数 : 2
今月のダウンロード数 : 3
File
ejb_264_509.pdf 5.55 MB 種類 : fulltext
Title ( eng )
Type-II 3-oxoacyl-CoA thiolase of the nematode Caenorhabditis elegans is located in peroxisomes, highly expressed during larval stages and induced by clofibrate
Creator
Maebuchi Motohiro
Togo Summnanuna H.
Yokota Sadaki
Ghenea Simona
Bun-ya Masanori
Kamiryo Tatsuyuki
Kawahara Akira
Source Title
European Journal of Biochemistry
Volume 264
Issue 2
Start Page 509
End Page 515
Abstract
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.
Keywords
type-II 3-oxoacyl-CoA thiolase
SCPx
peroxisomes
clofibrate
caenorhabditis elegans
NDC
Biology [ 460 ]
Language
eng
Resource Type journal article
Publisher
Federation of European Biochemical Societies
Date of Issued 1999
Rights
Copyright (c) 1999 Federation of European Biochemical Societies
Publish Type Author’s Original
Access Rights open access
Source Identifier
[ISSN] 0014-2956
[NCID] AA00639541
[DOI] 10.1046/j.1432-1327.1999.00655.x
[PMID] 10491098
[DOI] http://dx.doi.org/10.1046/j.1432-1327.1999.00655.x isVersionOf