References of "Scippo, Marie-Louise"
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See detailEndocrine, paracrine and autocrine factors in the maturation and functional development of the testis
Closset, Jean ULg; Dombrowicz, David; Vandenbroeck, Marc et al

in Bulletin et Mémoires de l'Académie Royale de Médecine de Belgique (1989), 144(1-2), 196-7

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See detailPITUITARY-HORMONES DEPENDENT EXPRESSION OF INSULIN-LIKE GROWTH FACTOR-I AND FACTOR-II IN THE IMMATURE HYPOPHYSECTOMIZED RAT TESTIS
Closset, Jean ULg; Gothot, André ULg; SENTE, Béatrice et al

in Molecular Endocrinology (1989), 3(7), 1125-1131

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See detailExpression and Secretion of the Human Placental Growth Hormone in Escherichia Coli
Igout, Ahmed ULg; Scippo, Marie-Louise ULg; Frankenne, Francis ULg et al

in Nucleic Acids Research (1989), 17(10), 3998

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See detailHuman placental growth hormone: proof of identity with the GH-V gene product by N-terminal microsequence analysis.
Scippo, Marie-Louise ULg; Frankenne, F.; Van Beumen, J. et al

in Archives Internationales de Physiologie et de Biochimie (1989), 97

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See detailL'hormone de croissance placentaire : caractérisation et signification biochimiques et physiologique.
Hennen, Georges ULg; Frankenne, Francis; Igout, Ahmed ULg et al

in Annales d'Endocrinologie (1988, October)

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See detailCloning and Nucleotide Sequence of Placental Hgh-V Cdna
Igout, Ahmed ULg; Scippo, Marie-Louise ULg; Frankenne, Francis ULg et al

in Archives Internationales de Physiologie et de Biochimie (1988), 96(1), 63-7

We have previously demonstrated the presence in human placenta and maternal serum of a GH variant, called human placental growth hormone (hPGH). We have also shown that the hGH-V gene is expressed at the ... [more ▼]

We have previously demonstrated the presence in human placenta and maternal serum of a GH variant, called human placental growth hormone (hPGH). We have also shown that the hGH-V gene is expressed at the placental level thus possibly coding for hPGH. The hGH-V cDNA has now been isolated from a lambda gt 11 human placenta cDNA library. Its sequence has been determined which firmly establishes the GH-V gene mode of splicing as well as the GH-V protein structure. Our data give final evidence of placental hGH-V gene expression and reinforce the hypothesis of identity between the hGH-V protein and hPGH. [less ▲]

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See detailThe Physiology of Growth Hormones (Ghs) in Pregnant Women and Partial Characterization of the Placental Gh Variant
Frankenne, Francis ULg; Lange, Jean-Marie ULg; Gomez, F. et al

in Journal of Clinical Endocrinology and Metabolism (1988), 66(6), 1171-80

This work was undertaken to study the heterogeneity of GH in serum and placental and pituitary extracts and to study GH physiology in pregnant women. Two distinct monoclonal antihuman GH (anti-hGH ... [more ▼]

This work was undertaken to study the heterogeneity of GH in serum and placental and pituitary extracts and to study GH physiology in pregnant women. Two distinct monoclonal antihuman GH (anti-hGH) antibodies (MAb) coded 5B4 and K24 were selected for their high binding affinity and specificity. The 5B4 MAb recognized the epitope comprising the NH2-terminal end of hGH, and the K24 MAb recognized an internal epitope. Both MAbs were used in RIAs to measure serum GH concentrations in various circumstances, including pregnancy. The two RIAs yielded slightly different serum GH results in normal men and nonpregnant women, but the overall correlation between the data was excellent. Since the RIAs were not affected by human placental lactogen, the evolution of serum GH in pregnant women could be studied. In such women, serum GH levels progressively declined to undetectable levels during the second half of pregnancy, while a pregnancy-associated serum GH-like antigen [tentatively called human placental growth hormone (PGH)] appeared in the circulation at midpregnancy and increased thereafter up to term. PGH contained the NH2-terminal epitope of pituitary GH, but lacked the internal one. Consequently, it reacted selectively with the 5B4 MAb only. After delivery, PGH disappeared from maternal serum within 1 h. Amniotic fluid contained low GH concentrations; cord serum contained high GH levels, but no PGH. Thus, PGH appears to be secreted selectively into the maternal compartment. PGH was purified from term placenta extracts. According to its chromatographic behavior, it appears more basic than pituitary 22K and 20K GHs. Size dimorphism was demonstrated; PGH was composed of two entities of 22K and 25K, respectively. Pure PGH, obtained in small quantities by preparative electrophoresis, was found to bind to hepatic GH receptor with an apparent high potency compared to that of pituitary GH, PGH, thus, should act in vivo as a GH agonist sharing most of its biological properties. These results lead to the conclusion that PGH is likely to replace the pituitary hormone in governing maternal metabolism during the second half of pregnancy. [less ▲]

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See detailPLACENTAL GROWTH-HORMONE - SIGNIFICANCE RELATIVE TO PITUITARY GROWTH-HORMONES AND PLACENTAL-LACTOGEN HORMONE
Hennen, Georges ULg; Frankenne, Francis ULg; Scippo, Marie-Louise ULg et al

in Reproduction Nutrition Development (1988), 28(6B), 1699-1706

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See detailhGH-V gene: specific placental expression, isolation and structure of the related cDNA.
Igout, Ahmed ULg; Scippo, Marie-Louise ULg; Frankenne, Francis et al

Conference (1988)

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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 detailLocation of transcriptional and regulatory sequences within the prolactin family genes
Belayew, A.; Bellefroid, Eric J.; Berwaer, M. et al

in Müller, E. E.; McLeod, R. M. (Eds.) Neuroendocrine Perspectives (1986)

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See detailLocalisation des séquences régulatrices de la transcription. Application aux gènes de la famille prolactine.
Belayew, A.; Bellefroid, Eric J.; Berwaer, M. et al

in Annales d'Endocrinologie (1986), 47

We are studying nucleotide sequences responsible for the regulation of eukaryotic gene expression. Our test system comprises the human genes coding for prolactin (hPRL), growth hormone (hGH-N) and ... [more ▼]

We are studying nucleotide sequences responsible for the regulation of eukaryotic gene expression. Our test system comprises the human genes coding for prolactin (hPRL), growth hormone (hGH-N) and placental lactogen (hCS-B). We have cloned these genes and are searching within their sequences for in vitro binding sites of the human glucocorticoid receptor on the hGH-N and hCS-B genes; the in vivo activity of such DNA sequences by assaying hybrid gene expression in transfected cells; in vivo "enhancer" activity of different hPRL gene fragments linked to a marker gene and transfected in cultured cells. [less ▲]

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See detailLocation of transcriptional regulatory sequences within the prolactin family genes.
Belayew, A.; Bellefroid, Eric J.; Berwaer, M. et al

in Neuroendocrine Perspectives. (1986)