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Titolo:
Type-II 3-oxoacyl-CoA thiolase of the nematode Caenorhabditis elegans is located in peroxisomes, highly expressed during larval stages and induced byclofibrate
Autore:
Maebuchi, M; Togo, SH; Yokota, S; Ghenea, S; Bun-Ya, M; Kamiryo, T; Kawahara, A;
Indirizzi:
Hiroshima Univ, Fac Integrated Arts & Sci, Higashihiroshima 7398521, JapanHiroshima Univ Higashihiroshima Japan 7398521 hihiroshima 7398521, Japan Yamanashi Med Sch, Dept Anat, Tamaho, Yamanashi, Japan Yamanashi Med Sch Tamaho Yamanashi Japan Anat, Tamaho, Yamanashi, Japan
Titolo Testata:
EUROPEAN JOURNAL OF BIOCHEMISTRY
fascicolo: 2, volume: 264, anno: 1999,
pagine: 509 - 515
SICI:
0014-2956(199909)264:2<509:T3TOTN>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
STEROL CARRIER PROTEIN-2; LIPID-TRANSFER PROTEIN; YEAST CANDIDA-TROPICALIS; ACYL-COENZYME-A; RAT-LIVER; 2/3-OXOACYL-COA THIOLASE; NUCLEOTIDE-SEQUENCE; GLYOXYLATE CYCLE; PURIFICATION; METABOLISM;
Keywords:
Caenorhabditis elegans; clofibrate; peroxisomes; SCPx; type-II 3-oxoacyl-CoA thiolase;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
35
Recensione:
Indirizzi per estratti:
Indirizzo: Kamiryo, T Hiroshima Univ, Fac Integrated Arts & Sci, Kagamiyama 1-7-1, Higashihiroshima 7398521, Japan Hiroshima Univ Kagamiyama 1-7-1 Higashihiroshima Japan 7398521
Citazione:
M. Maebuchi et al., "Type-II 3-oxoacyl-CoA thiolase of the nematode Caenorhabditis elegans is located in peroxisomes, highly expressed during larval stages and induced byclofibrate", EUR J BIOCH, 264(2), 1999, pp. 509-515

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 alpha carbon, whereas conventional thiolases do not. Mammalian type-II thiolase, which is also termed sterolcarrier protein x (SCPx) or SCP2/3-oxoacyl-CoA thiolase, is located in theperoxisomes and involved in phytanic acid degradation and most probably inbile 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 enzymewas mainly expressed in intestinal cells, which are multifunctional like many of the cell types in C. elegans. Subcellular fractionation and indirectimmunoelectron 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.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/07/20 alle ore 18:27:20