References of "Swennen, D"
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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 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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