References of "Rentier-Delrue, Françoise"
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See detailSequence of the triosephosphate isomerase-encoding gene isolated from the thermophile Bacillus stearothermophilus
Rentier-Delrue, Françoise ULg; Moyens, Sylvianne; Lion, Michelle ULg et al

in Gene (1993), 134(1), 137-8

By analysis of genomic clones, we have determined the complete nucleotide sequence of the gene encoding triosephosphate isomerase (TIM; EC 5.3.1.1) in the thermophilic bacterium, Bacillus ... [more ▼]

By analysis of genomic clones, we have determined the complete nucleotide sequence of the gene encoding triosephosphate isomerase (TIM; EC 5.3.1.1) in the thermophilic bacterium, Bacillus stearothermophilus. The gene encodes a 253-amino-acid TIM which is 39% identical to that of the mesophile, Escherichia coli. [less ▲]

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See detailEffect of prolactin on alpha and beta chloride cells in the gill epithelium of the saltwater adapted tilapia " Oreochromis niloticus"
Pisam, B.; Auperin, B.; Prunet, P. et al

in Anatomical Record (1993), 235

Tilapia (Oreochromis niloticus), 21 g average body weight, were divided into two groups. A group was maintained in fresh water, whereas another group was adapted for 2 weeks to 20% salt water. Among the ... [more ▼]

Tilapia (Oreochromis niloticus), 21 g average body weight, were divided into two groups. A group was maintained in fresh water, whereas another group was adapted for 2 weeks to 20% salt water. Among the latter, fishes were injected every 2 days for a week with tilapia prolactin (ti-PRL I). Gills were prepared for electron microscopy in order to determine the types and surface areas of chloride cells in each experimental condition. Two types of chloride cells, the alpha and beta cells were easily distinguished on the basis of their location and ultrastructural features in the gills of freshwater fishes, while only one type of cell, the saltwater alpha cells presumably derived from the transformation of the freshwater alpha cells, were encountered in saltwater adapted animals. After PRL injection of saltwater adapted fishes, small chloride cells, which displayed ultrastructural features similar to those of beta cells in freshwater tilapia, reappeared in interlamellar regions of the gills. In the same experimental conditions, the voluminous saltwater alpha cells showed a tendency to resume ultrastructural features more characteristic of the freshwater alpha cells from which they were derived. These observations tend to indicate that prolactin behaves as a "freshwater adapting hormone" and that beta cells are specifically involved in fish adaptation to freshwater living conditions. [less ▲]

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See detailStructure of the tilapia (Oreochromis mossambicus) prolactin I gene
Swennen, D.; Poncelet, A. C.; Sekkali, B. et al

in DNA & Cell Biology (1992), 11(9), 673-84

The tilapia (Oreochromis mossambicus) prolactin-I (PRL-I) gene has been cloned and sequenced. Its transcript (3,677 bases long) begins with a guanine and is organized in five exons and four introns like ... [more ▼]

The tilapia (Oreochromis mossambicus) prolactin-I (PRL-I) gene has been cloned and sequenced. Its transcript (3,677 bases long) begins with a guanine and is organized in five exons and four introns like the other known prolactin genes. Analysis of the 1,555-bp 5'-flanking region suggests that pituitary-specific expression of the gene could be regulated through a trans-factor related to the mammalian pituitary-specific factor Pit-1. Two potential binding sites for such a factor were found in the first intron, suggesting a possible regulatory role for this region. Moreover, two potential Z-DNA regions are located at positions -837 to -812 and -246 to -179 from the transcription start site. These two regions could play an important role in the regulation of PRL gene expression. [less ▲]

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See detailProduction and purification of biologically active recombinant tilapia (Oreochromis niloticus) prolactins
Swennen, D.; Rentier-Delrue, Françoise ULg; Auperin, B. et al

in Journal of Endocrinology (1991), 131(2), 219-27

Recombinant expression vectors carrying tilapia prolactin-I or -II (tiPRL-I or tiPRL-II) cDNA were constructed and the tiPRL-I and II proteins were produced in E. coli as inclusion bodies. These inclusion ... [more ▼]

Recombinant expression vectors carrying tilapia prolactin-I or -II (tiPRL-I or tiPRL-II) cDNA were constructed and the tiPRL-I and II proteins were produced in E. coli as inclusion bodies. These inclusion bodies were dissolved in 6 mol urea/l. Refolding of the proteins was followed by SDS-PAGE under non-reducing conditions so as to visualize the oxidized state of the molecules. Proteins tiPRL-I and tiPRL-II were purified by gel filtration and ion-exchange chromatography. The N-terminal sequence and bioactivities of both purified proteins were then analysed. Recombinant tiPRL-I and tiPRL-II induced a significant rise in plasma calcium levels as well as in mucocyte density in the abdominal skin epithelium. When tested on kidney membrane, both proteins exhibited potency in competing with 125I-labelled tiPRL-I for binding sites, but tiPRL-I seemed to be more potent than tiPRL-II in competing for these sites. The results obtained for the biological activities tested suggest that both recombinant prolactins were correctly refolded and had retained the full biological activity previously observed with the natural hormone preparations extracted from the animals. [less ▲]

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See detailRecombinant fish hormone proteins.
Rentier-Delrue, Françoise ULg; Martial, Joseph ULg; Renard, André

Patent (1990)

The present invention relates to a recombinant stable polypeptide comprising in its polypeptide chain an aminoacid sequence contained in one of the following amino sequences : * from amino acid (-20) to ... [more ▼]

The present invention relates to a recombinant stable polypeptide comprising in its polypeptide chain an aminoacid sequence contained in one of the following amino sequences : * from amino acid (-20) to amino acid (187) represented in Fig. 2, * from amino acid (1) to amino acid (187) represented in Fig. 2, * from amino acid (1) to amino acid (187) represented in Fig. 2, preceded by Met. [less ▲]

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See detailGrowth hormone and somatostatin gene expression in pituitary adenomas with active acromegaly and minimal plasma growth hormone elevation
Pagesy, Patrick; Li, Jacques Y.; Rentier-Delrue, Françoise ULg et al

in Acta Endocrinologica (1990), 122(6), 745-752

Some patients with active acromegaly have elevated plasma IGF-I concentrations with only minimal elevation of plasma GH. We compared adenomatous GH and SRIH expression in 3 such patients (patients No. 1 ... [more ▼]

Some patients with active acromegaly have elevated plasma IGF-I concentrations with only minimal elevation of plasma GH. We compared adenomatous GH and SRIH expression in 3 such patients (patients No. 1, 2 and 3; basal plasma GH level < 4 µg/l) and in 3 acromegalic patients with high basal plasma GH level (patients No. 4, 5 and 6; 51.7 ± 16.1 µg/l, mean ± SEM). By immunocytochemistry, all the tumours proved to be somatotropic adenomas. At the ultrastructural level, signs of low secretory activity were observed in adenomas from patients No. 2 and 3. Perifused adenoma cells of patients No. 1, 2 and 3 released very little GH compared with those of patients No. 4, 5 and 6 (1± 0.37 vs 51.5± 34.1 µg · (10–6 cells) · min–1, p< 0.001). Adenoma SRIH content was 65.7 and 30.6 pg/mg proteins in patients No. 1 and 2, whereas it was undetectable in the others (patients No. 4, 5 and 6). Northern blot analysis showed that the GH gene was poorly expressed in the adenomas from patients No. 1, 2 and 3 compared with the adenomas from patients No. 4, 5 and 6. SRIH mRNA was detected in all 6 adenomas. However, the signal was more intense in the adenomas from patients No. 1, 2 and 3 than in those from patients No. 4, 5 and 6. In conclusion, because of the variability of the biosynthetic and secretory potential of the somatotropic adenomas, patients harbouring this type of pituitary tumours can exhibit a wide range of plasma GH levels. In acromegaly with minimal elevation of plasma GH, the synthesis of SRIH by the adenoma cells themselves could play a role in the inhibition of GH expression. [less ▲]

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See detailBacterial production and purification of recombinant human prolactin
Paris, N.; Rentier-Delrue, Françoise ULg; Defontaine, A. et al

in Biotechnology & Applied Biochemistry (1990), 12(4), 436-49

Escherichia coli cells transformed with a recombinant plasmid (pT7L) containing the coding sequence of human prolactin (hPrl) expressed a new protein. This protein, comigrating with human Prl on sodium ... [more ▼]

Escherichia coli cells transformed with a recombinant plasmid (pT7L) containing the coding sequence of human prolactin (hPrl) expressed a new protein. This protein, comigrating with human Prl on sodium dodecyl sulfate (SDS)-polyacrylamide gels, represented 50% of the total bacterial extract. Immunoprecipitation of [35S]methionine-labeled bacterial lysate with a rabbit antiserum to hPrl followed by SDS-polyacrylamide gel electrophoresis (PAGE) analysis showed that the major component had a Mr identical to that of standard hPrl. The majority of the recombinant hPrl (r-hPrl) accumulated in inclusion bodies. Analysis of these inclusion bodies by SDS-PAGE under nonreducing conditions showed that they are composed mostly of fully reduced monomers. Solubilization of the inclusion bodies and protein denaturation were performed in 8 M urea. Refolding during the renaturation procedure was confirmed by SDS-PAGE under nonreducing conditions. r-hPrl was further purified by gel permeation chromatography on a fast protein liquid chromatography column. More than 95% of the molecules were recovered as oxidized monomeric forms. The refolded molecule was tested for its bioactivity in the Nb2 lymphoma mitogenic assay. The dose-response curves obtained with either r-hPrl or pituitary-derived hPrl showed a complete parallelism. Furthermore, Nb2 cell proliferation was completely blocked by addition of hPrl antiserum to both preparations. Recombinant hPrl is identical to natural hPrl except for an additional methionine group at the amino terminal end. [less ▲]

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See detailEvidence of pre-prosomatostatin mRNA in human normal and tumoral anterior pituitary gland
Pagesy, P.; Li, J. Y.; Rentier-Delrue, Françoise ULg et al

in Molecular Endocrinology (1989), 3(8), 1289-94

Expression of the SRIH gene was investigated in six human normal anterior pituitaries, six GH-, three PRL-, three mixed GH/PRL-secreting and four nonsecreting adenomas. Total cellular RNA and poly(A ... [more ▼]

Expression of the SRIH gene was investigated in six human normal anterior pituitaries, six GH-, three PRL-, three mixed GH/PRL-secreting and four nonsecreting adenomas. Total cellular RNA and poly(A+) mRNAs were analyzed by dot and Northern blot hybridization to a 3'-end labeled oligonucleotide probe specific for the human pre-proSRIH mRNA. A weak but detectable pre-proSRIH hybridization signal was present in human normal anterior pituitaries and in the four groups of adenomas. The size of this pre-proSRIH mRNA was indistinguishable from that found in our hypothalamic samples and close to that described in the literature. The wide variation of the signal intensity from one case to the other in each group of the different types of normal and tumoral antehypophyseal samples prevented establishment of any correlation between the level of pre-proSRIH mRNA and the nature of the pituitary tissue. The presence of SRIH mRNA in human normal and tumoral anterior pituitary tissues provides a sound basis to substantiate the hypothesis of a SRIH biosynthesis in the human anterior pituitary gland. [less ▲]

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See detailTilapia growth hormone: molecular cloning of cDNA and expression in Escherichia coli
Rentier-Delrue, Françoise ULg; Swennen, D.; Philippart, Jean-Claude ULg et al

in DNA (1989), 8(4), 271-8

A cDNA library was prepared from poly(A)+RNA extracted from tilapia Oreochromis niloticus anterior pituitaries. The recombinant clones carrying the cDNA sequence of tilapia growth hormone (tiGH) were ... [more ▼]

A cDNA library was prepared from poly(A)+RNA extracted from tilapia Oreochromis niloticus anterior pituitaries. The recombinant clones carrying the cDNA sequence of tilapia growth hormone (tiGH) were selected using a fragment of the trout growth hormone (tGH) cDNA as hybridization probe. The nucleotide sequence of the full-length tiGH cDNA was determined. This cDNA encodes a protein of 204 amino acids, including the putative signal peptide of 17 amino acids. Mature tiGH cDNA was inserted in an Escherichia coli expression vector which led to the production of tiGH protein with a yield estimated to be 20% of the total bacterial proteins. [less ▲]

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See detailTilapia prolactin: molecular cloning of two cDNAs and expression in Escherichia coli
Rentier-Delrue, Françoise ULg; Swennen, D.; Prunet, P. et al

in DNA (1989), 8(4), 261-70

We have isolated cDNA clones encoding tilapia prolactin (tiPRL) from a cDNA library prepared from tilapia (Oreochromis niloticus) anterior pituitary glands. A trout PRL cDNA fragment was used as ... [more ▼]

We have isolated cDNA clones encoding tilapia prolactin (tiPRL) from a cDNA library prepared from tilapia (Oreochromis niloticus) anterior pituitary glands. A trout PRL cDNA fragment was used as hybridization probe to select the recombinant plasmids carrying the tiPRL coding sequence. Two types of PRL cDNA were isolated and their complete nucleotide sequence determined. The larger cDNA (tiPRL-I) codes for a polypeptide of 212 amino acids, including a putative signal sequence of 24 amino acids, and contains a 3' untranslated region of 787 bp. The second prolactin cDNA (tiPRL-II) encodes a polypeptide of 200 amino acids, including a presumptive signal peptide of 23 amino acids, and contains a noncoding region of 512 bp. tiPRL-I and tiPRL-II cDNA sequences are 81% similar, whereas the encoded proteins share 69% amino acid identity at optimal alignment. Mature tiPRL-I was efficiently expressed in Escherichia coli carrying a plasmid in which the tiPRL-I cDNA was under the control of the phi 10 promoter of T7 bacteriophage. The new recombinant protein representing about 45% of the total cellular proteins was found in inclusion bodies and cross-reacted with salmon PRL antiserum. [less ▲]

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See detailRainbow trout prolactin cDNA cloning in Escherichia coli
Mercier, L.; Rentier-Delrue, Françoise ULg; Swennen, D. et al

in DNA (1989), 8(2), 119-25

We describe the isolation and characterization of a cDNA for trout prolactin (tPrl). An extensive analysis of tPrl recombinant clones by restriction analysis and sequencing revealed the presence of only ... [more ▼]

We describe the isolation and characterization of a cDNA for trout prolactin (tPrl). An extensive analysis of tPrl recombinant clones by restriction analysis and sequencing revealed the presence of only one form of tPrl mRNA. The deduced protein sequence consists of 210 amino acids, including a signal peptide of 23 amino acids. The amino acid sequence of the mature protein is compared among teleosts and mammals, showing two domains of strong similarity that may be involved in biological activity. [less ▲]

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See detailMolecular cloning and characterization of two forms of trout growth hormone cDNA: expression and secretion of tGH-II by Escherichia coli
Rentier-Delrue, Françoise ULg; Swennen, D.; Mercier, L. et al

in DNA (1989), 8(2), 109-17

We constructed a cDNA library using mRNA isolated from rainbow trout pituitaries. Two types of cDNA clones encoding growth hormone (GH) were isolated and their complete nucleotide sequences determined ... [more ▼]

We constructed a cDNA library using mRNA isolated from rainbow trout pituitaries. Two types of cDNA clones encoding growth hormone (GH) were isolated and their complete nucleotide sequences determined. Twenty seven nucleotide substitutions in the coding region and 108 in the noncoding region distinguish the cDNAs of trout GH-I and II. Both cDNAs encode polypeptides of 210 amino acids, including a putative signal peptide of 22 amino acids, which differ by 12 residues. In both trout and salmon, GH-I mRNA is predominant, which suggests that the variation in the amount of secreted GH originates from a transcriptional event. Moreover, comparison of rainbow trout and chum salmon GH reveals that, in both cases, the predominant GH-I has mutated less than its GH-II counterpart. Mature tGH-II was expressed in Escherichia coli using the pIN-III-ompA-Hind secretion vector. [less ▲]

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See detailPIN-IIII-OmpA Secretion Vectors: Modification of the Ompa Signal Peptide Sequence for Easier Insert Cloning
Rentier-Delrue, Françoise ULg; Swennen, D.; Martial, Joseph ULg

in Nucleic Acids Research (1988), 16(17), 8726

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See detailAcromegaly with low plasma GH level. A clinical biological, histological and GH mRNA study
Pagesy, P.; Martial, Joseph ULg; Delalande, O. et al

in Advanced in Biosciences (1988), 69

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See detailFish growth hormones
Renard, A.; Lecomte, C.; Rentier-Delrue, Françoise ULg et al

in Seminar on Use of Somatotropin in Livestock productio (1988)

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See detailA simple method for the preparation of covalently closed circular form of plasmid DNA
Le Brun, J. J.; Rentier-Delrue, Françoise ULg; Mercier, L.

in BioTechniques (1988)

We describe a simple, rapid, inexpensive method for isolation of covalently closed circular plasmid DNA. The method involves the electrophoresis of crude DNA preparations in an agarose gel ... [more ▼]

We describe a simple, rapid, inexpensive method for isolation of covalently closed circular plasmid DNA. The method involves the electrophoresis of crude DNA preparations in an agarose gel, electrotransfer onto a dialysis membrane and elution of the highly purified circular covalently closed plasmid DNA. Native and recombinant plasmid DNA have been purified by this method and shown to be suitable for restriction enzyme digestion and transformation of bacteria. The yield of this rapid purification procedure makes it a good alternative method to standard centrifugation in cesium chloride ethidium bromide gradients. [less ▲]

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See detailExpression of the growth hormone variant gene in human placenta
Frankenne, Francis; Rentier-Delrue, Françoise ULg; Scippo, Marie-Louise ULg et al

in Journal of Clinical Endocrinology and Metabolism (1987), 64(3), 635-637

Besides the hGH-N gene, which codes for the pituitary 22 and 20K GH variants, the human genome contains a second GH gene, namely the GH-V, which has been thought to be silent. We recently discovered a ... [more ▼]

Besides the hGH-N gene, which codes for the pituitary 22 and 20K GH variants, the human genome contains a second GH gene, namely the GH-V, which has been thought to be silent. We recently discovered a placental variant of human growth hormone (hPGH), which appears in maternal serum at mid-pregnancy and which rises in concentration thereafter to term. As hPGH and GH-V proteins display very similar characteristics, including a high affinity for hepatic GH receptors, they could be identical. To verify this hypothesis, we sought hGH-V mRNA in placenta. Hybridization experiments were performed between dot-blotted mRNA originating either from placenta or from one pituitary hGH secreting adenoma and synthetic polynucleotide probes corresponding to specific portions of the hGH-V or hGH-N gene sequences. The results indicate that the V gene is indeed expressed in the placenta and, at a very low level, in the pituitary adenoma. Therefore hPGH is most likely the expression product of the hGH-V gene. [less ▲]

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See detailLow GH hypophyseal adenomas with acromegaly exhibit undetectable levels of messenger RNA of normal GH
Pagesy, P.; Rentier-Delrue, Françoise ULg; Bresson, D. et al

in Annals of Endocrinology (1987), 48

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See detailAnalysis of JC Virus DNA Purified directlt from Human Progressive Multifocal Leukoencephalopathy Brains
Rentier-Delrue, Françoise ULg; Lubiniecki, A.; Howley, P.

in Journal of Virology (1981)

Human polyomavirus JC DNA was purified directly from the diseased brain tissue of two patients with progressive multifocal leukoencephalopathy (PML) by a method employing differential salt precipitation ... [more ▼]

Human polyomavirus JC DNA was purified directly from the diseased brain tissue of two patients with progressive multifocal leukoencephalopathy (PML) by a method employing differential salt precipitation (B. Hirt, J. Mol. Biol. 26:365-369, 1967). Each of the viral genomes (JC-NIH-1 and JC-NIH-2) was molecularly cloned intact in Escherichia coli, using pBR322, at their unique EcoRI (0.00 map unit) and BamHI (0.51 map unit) sites. The JC-NIH-1 genome was approximately 50 base pairs larger and the JC-NIH-2 genome was approximately 50 base pairs smaller than the prototype human polyomavirus JC (Mad-1) DNA. Analysis of the restriction endonuclease cleavage fragments of these two DNAs and the human polyomavirus JC (Mad-1) DNA revealed only slight differences which mapped in a region of the genome extending from 0.67 to 0.74 map unit. From previous homology studies, this region of variance corresponds to the noncoding region to the late side of the origin of DNA replication. [less ▲]

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