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1.
Comp Biochem Physiol B Biochem Mol Biol ; 156(4): 237-43, 2010 Aug.
Artigo em Inglês | MEDLINE | ID: mdl-20363355

RESUMO

Supplies of marine fish oils are limited, and continued growth in aquaculture production dictates that lipid substitutes in fish diets must be used without compromising fish health and product quality. In this study, the total substitution of a fish meal and fish oil by a blend of vegetable meals (corn, soybean, wheat and lupin) and linseed oil in the diet of European sea bass (Dicentrachus labrax) was investigated. Two groups of European sea bass were fed with fish diet (FD) or vegetable diet (VD) for 9months. VD, totally deprived of eicosapentaenoate (EPA; 20:5n-3) and docosahexaenoate (DHA; 22:6n-3), revealed a nutritional deficiency and affected growth performance. Whilst VD induced a significant increase in fatty acid desaturase 2 (FADS2) and sterol binding regulatory element-binding protein 1 (SREBP-1) mRNA levels, the desaturation rate of [1-(14)C]18:3n-3 into [1-(14)C]18:4n-3, analysed in microsomal preparations using HPLC method, did not show an upregulation of FADS2 activities in liver and intestine of fish fed VD. Moreover Western-blot analysis did not revealed any significant difference of FADS2 protein amount between the two dietary groups. These data demonstrate that sea bass exhibits a desaturase (FADS2) activity whatever their diet, but a post-transcriptional regulation of fads2 RNA prevents an increase of enzyme in fish fed a HUFA-free diet. This led to a lower fish growth and poor muscle HUFA content.


Assuntos
Bass/metabolismo , Dieta , Ácidos Graxos Dessaturases/metabolismo , Proteínas de Peixes/metabolismo , Ração Animal , Animais , Aquicultura , Bass/genética , Bass/crescimento & desenvolvimento , Ácidos Graxos Dessaturases/genética , Ácidos Graxos/análise , Proteínas de Peixes/genética , Regulação da Expressão Gênica , Intestinos/enzimologia , Fígado/enzimologia , PPAR alfa/genética , PPAR alfa/metabolismo , Proteína de Ligação a Elemento Regulador de Esterol 1/genética , Proteína de Ligação a Elemento Regulador de Esterol 1/metabolismo , Verduras
2.
Exp Cell Res ; 260(2): 222-32, 2000 Nov 01.
Artigo em Inglês | MEDLINE | ID: mdl-11035917

RESUMO

The amphibian oocyte represents an excellent model for the study of transcription regulation. Indeed, any modification of transcriptional activity is directly reflected in lampbrush chromosome structure by concomitant morphological changes. Previous studies have led to the hypothesis of a putative role for heat-shock proteins HSP70 and/or HSC70 in transcriptional processes in the oocyte. In order to dissect out the relative role of HSP70 or HSC70 in these processes, we used an oligo-antisense strategy to specifically inhibit the function of the targeted protein. Effects of hsc70 and hsp70 antisense oligodeoxynucleotides were analyzed in terms of both mRNA quantity and protein synthesis. Their effects on oocyte transcription were analyzed at the level of structural organization of lampbrush chromosomes and nucleolar transcriptional activity. Our results show that specific inactivation of hsc70 mRNA by hsc70 antisense oligos led to a reversible inhibition of lampbrush chromosome transcription. However, such reversible inhibition of transcription is considered non-sequence specific since it is also induced by any oligo. In contrast, specific inactivation of hsp70 mRNA by hsp70 antisense oligos, which is correlated with a drop of HSP70 neosynthesis, results in an irreversible inhibition of lampbrush chromosome transcription. Furthermore, our results show that the inactivation of hsp70 or hsc70 mRNAs does not affect nucleolar transcription. Such data suggest a role for HSP70 in the control of chromatin modifications related to RNA polymerase II transcriptional activity.


Assuntos
Proteínas de Transporte/biossíntese , Regulação da Expressão Gênica , Proteínas de Choque Térmico HSP70/biossíntese , Transcrição Gênica , Animais , Proteínas de Transporte/genética , Nucléolo Celular/metabolismo , Cromossomos , Proteínas de Choque Térmico HSC70 , Proteínas de Choque Térmico HSP70/genética , Oligonucleotídeos Antissenso , Oócitos , RNA Mensageiro , Xenopus laevis
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