References of "Frankenne, Francis"
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See detailPlasminogen activator inhibitor type I (PAI-1) controls bone marrow-dependent and independent vascularization
Jost, M.; Maillard, Catherine ULg; Lambert, Vincent ULg et al

in Acta Clinica Belgica (2006), 61(2, MAR-APR), 87

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See detailPresence of alpha and beta estrogen receptors in human gingiva
Fraikin, N.; Munaut, Carine ULg; Lambert, Vincent ULg et al

in Journal of Dental Research (2002, December), 81(Sp. Iss. B), 239-239

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See detailExpression of membrane type 1 matrix metalloproteinase (MT1-MMP) in A2058 melanoma cells is associated with MMP-2 activation and increased tumor growth and vascularization
Sounni, Nor Eddine ULg; Baramova, Eugénia; Munaut, Carine ULg et al

in International Journal of Cancer = Journal International du Cancer (2002), 98(1), 23-28

Membrane-type metalloproteinase-1 (MT1-MMP) is a transmembrane metalloproteinase overexpressed in tumors, which plays a major role in the first step of pro-MMP-2 activation, leading to the generation of ... [more ▼]

Membrane-type metalloproteinase-1 (MT1-MMP) is a transmembrane metalloproteinase overexpressed in tumors, which plays a major role in the first step of pro-MMP-2 activation, leading to the generation of an intermediate 62 kDa species. The second step of MMP-2 activation that yields to the mature form is less understood and could involve an autocatalytic process and/or the activity of the plasminogen/plasmin system. Human melanoma A2058 cells, which express MMP-2 only in its pro-form, were used to determine the role of MT1-MMP during pericellular proteolysis and tumor progression. The induction of MT1-MMP overexpression by MT1-MMP cDNA transfection initiated the first step of MMP-2 activation. We provide evidence that a cooperation between the plasminogen/plasmin system and MT1-MMP endowed the cells with the ability to fully activate MMP-2 and with enhanced invasive properties in vitro. When injected subcutaneously in nude mice, MT1-MMP expressing clones induced rapid tumor growth and high tumor vascularization, while the control clones were poorly or not tumorigenic. Our data provide the first demonstration, in an experimental model, that MT1-MMP expression by tumor cells promotes tumor vascularization. [less ▲]

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See detailPresence of Oestrogen Receptor Type Beta in Human Retina
Munaut, Carine ULg; Lambert, Vincent ULg; Noël, Agnès ULg et al

in British Journal of Ophthalmology (2001), 85(7), 877-82

BACKGROUND/AIMS: Recent studies have demonstrated the existence of two oestrogen receptor subtypes alpha (ORalpha) and beta (ORbeta) with significant differences of expression among organs. Since ... [more ▼]

BACKGROUND/AIMS: Recent studies have demonstrated the existence of two oestrogen receptor subtypes alpha (ORalpha) and beta (ORbeta) with significant differences of expression among organs. Since important pathologies of human eye could be linked to hormonal status, the expression of ORbeta in ocular posterior segment was sought. METHODS: Immunohistochemical localisation of ORbeta and ORalpha protein and detection of OR mRNAs by reverse transcription-polymerase chain reaction (RT-PCR) were performed in macular and extramacular regions of the retina and in the choroid on male and female donors eyes. RESULTS: ORbeta protein was localised in the ganglion cell layer and in the choroid. At the transcriptional level, mRNA for ORbeta and for ORalpha were both present. Local differences in the expression level were observed, however, suggesting the possibility of variation in the ratio of ORalpha v ORbeta. CONCLUSIONS: The coexistence of two oestrogen receptor subtypes in the human ocular posterior segment raises acute questions about their potential physiological role, but offers a perspective for preferential targeting of a specific receptor subtype. [less ▲]

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See detailMembrane Type 1 Matrix Metalloproteinase-Associated Degradation of Tissue Inhibitor of Metalloproteinase 2 in Human Tumor Cell Lines
Maquoi, Erik ULg; Frankenne, Francis ULg; Baramova, Eugénia et al

in Journal of Biological Chemistry (2000), 275(15), 11368-78

Tissue inhibitor of metalloproteinase 2 (TIMP-2) is required for the membrane type 1 matrix metalloproteinase (MT1-MMP)-dependent activation of pro-MMP-2 on the cell surface. MT1-MMP-bound TIMP-2 has been ... [more ▼]

Tissue inhibitor of metalloproteinase 2 (TIMP-2) is required for the membrane type 1 matrix metalloproteinase (MT1-MMP)-dependent activation of pro-MMP-2 on the cell surface. MT1-MMP-bound TIMP-2 has been shown to function as a receptor for secreted pro-MMP-2, resulting in the formation of a trimolecular complex. In the presence of uncomplexed active MT1-MMP, the prodomain of cell surface-associated MMP-2 is cleaved, and activated MMP-2 is released. However, the behavior of MT1-MMP-bound TIMP-2 during MMP-2 activation is currently unknown. In this study, (125)I-labeled recombinant TIMP-2 ((125)I-rTIMP-2) was used to investigate the fate of TIMP-2 during pro-MMP-2 activation by HT1080 and transfected A2058 cells. HT1080 and A2058 cells transfected with MT1-MMP cDNA (but not vector-transfected A2058 cells) were able to bind (125)I-rTIMP-2, to activate pro-MMP-2, and to process MT1-MMP into an inactive 43-kDa form. Under these conditions, (125)I-rTIMP-2 bound to the cell surface was rapidly internalized and degraded in intracellular organelles through a bafilomycin A(1)-sensitive mechanism, and (125)I-bearing low molecular mass fragment(s) were released in the culture medium. These different processes were inhibited by hydroxamic acid-based synthetic MMP inhibitors and rTIMP-2, but not by rTIMP-1 or cysteine, serine, or aspartic proteinase inhibitors. These results support the concept that the MT1-MMP-dependent internalization and degradation of TIMP-2 by some tumor cells might be involved in the regulation of pericellular proteolysis. [less ▲]

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See detailPurification and Biochemical Characterization of Recombinant Human Placental Growth Hormone Produced in Escherichia Coli
Igout, Ahmed ULg; Van Beeumen, Jozef; Frankenne, Francis ULg et al

in Biochemical Journal (1993), 295(3), 719-724

The hGH-V (or hGH-2) gene codes for human placental growth hormone (hPGH). Secretion of hPGH is continuous, in contrast with the pulsed secretion of pituitary growth hormone (hGH) which it progressively ... [more ▼]

The hGH-V (or hGH-2) gene codes for human placental growth hormone (hPGH). Secretion of hPGH is continuous, in contrast with the pulsed secretion of pituitary growth hormone (hGH) which it progressively replaces in the maternal bloodstream. hGH- V cDNA has previously been cloned and isolated. Analysis of its nucleotide sequence has revealed a 191-residue protein, hPGH, differing from hGH at 13 positions. The calculated pI is more basic than that of the pituitary hormone. Here we have inserted hGH- VcDNA into the pIN-III-ompA3 plasmid in order to produce hPGH in its native form in Escherichia coli D1210. Expression of hGH- V cDNA in E. coli is significantly lower than that of hGH cDNA with the same expression system. The hPGH produced in E. coli was purified in quantities sufficient to allow its biochemical and immunochemical characterization. The molecular mass of the protein was determined by electrospray m.s. The determined mass, 22320 Da, agrees well with the molecular mass calculated from the translated cDNA sequence, assuming the presence of two disulphide bridges. Having established the technique for producing hPGH with a primary structure identical to the natural, non-glycosylated, 22 kDa isoform, we can now plan the full physicochemical and pharmaceutical characterization of this new hormonal entity. [less ▲]

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See detailSYNCYTIOTROPHOBLASTIC LOCALIZATION OF THE HUMAN GROWTH-HORMONE VARIANT MESSENGER-RNA IN THE PLACENTA
Scippo, Marie-Louise ULg; Frankenne, Francis ULg; HOOGHEPETERS, ELisabeth et al

in Molecular & Cellular Endocrinology (1993), 92(2), 7-13

The hGH/hCS genes, clustered on chromosome 17 in the 5' to 3' order GH-N, CS-L, CS-A, GH-V and CS-B, show a high degree of sequence identity. The expression product of the GH-V gene is the placental ... [more ▼]

The hGH/hCS genes, clustered on chromosome 17 in the 5' to 3' order GH-N, CS-L, CS-A, GH-V and CS-B, show a high degree of sequence identity. The expression product of the GH-V gene is the placental growth hormone, which replaces pituitary GH in maternal blood throughout pregnancy. By means of mRNA competitive hybridization using P-32-labelled and unlabelled 30 bases long oligonucleotides, we first optimized specific hybridization conditions. In situ hybridization was then performed to locate the GH-V mRNA encoding placental growth hormone. The hGH-V gene appears expressed in the placental syncytiotrophoblast. Unlike the CS-A and CS-B genes (both encoding hPL) which are expressed uniformly in the syncytiotrophoblast, the GH-V mRNA is located in a few syncytiotrophoblast cells only. [less ▲]

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See detailAdenohypophysis hormone gene products in 14 pituitary adenomas: analysis by immunohistochemistry and northern blotting.
Scippo, Marie-Louise ULg; Beckers, Albert ULg; Frankenne, Francis ULg et al

in Archives Internationales de Physiologie, de Biochimie et de Biophysique (1991), 99(2), 135-40

We investigated 14 pituitary adenomas (10 silent adenomas; 3 prolactinomas and one GH-secreting tumor) for the presence of hormone gene transcripts (Northern blot) as well as for translation products ... [more ▼]

We investigated 14 pituitary adenomas (10 silent adenomas; 3 prolactinomas and one GH-secreting tumor) for the presence of hormone gene transcripts (Northern blot) as well as for translation products (immunohistochemistry). The GH-secreting tumor was shown to express the genes coding for GH and PRL and to synthesize the corresponding hormones. In the cases of prolactinomas, immunohistochemical data demonstrated the synthesis of prolactin only. In addition to the PRL gene, Northern blot analysis revealed the transcription of the alpha-subunit gene in one case. Hormone genes were found to be expressed in 7 out of the 10 silent tumors, whereas no hormone synthesis was detected in any of these tissues. LH-beta mRNA was found in 3 cases, FSH-beta mRNA in 5 cases and alpha-subunit gene was shown to be expressed in one case. Surprisingly, the level of expression of the FSH-beta gene was higher than in normal tissue. This study confirms that some so called "silent" adenomas are expressing alpha- and/or beta-subunit glycoprotein hormone genes, even if no hormone is synthesized. The therapeutic action of bromocriptine described in some "silent" adenomas cases could be related to that hormone gene expression potentiality. [less ▲]

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See detailPlacental and Pituitary Growth Hormone Secretion During Pregnancy in Acromegalic Women
Beckers, Albert ULg; Stevenaert, Achille ULg; Foidart, Jean-Michel ULg et al

in Journal of Clinical Endocrinology and Metabolism (1990), 71(3), 725-31

It is now well established that during the second half of normal pregnancy, the human placenta secretes its specific GH variant (placental GH) in increasing amounts up to delivery. During the same period ... [more ▼]

It is now well established that during the second half of normal pregnancy, the human placenta secretes its specific GH variant (placental GH) in increasing amounts up to delivery. During the same period, pituitary GH secretion is progressively suppressed. The present study was aimed at clarifying the physiology of GH secretion in pregnant acromegalic women. Two young women remained acromegalic despite transphenoidal removal of their pituitary adenoma. Increased basal levels of GH and insulin-like growth factor-I (IGF-I) as well as paradoxical GH release after TRH injection were noted. Both women became pregnant and delivered term babies without any complication. In both patients, pituitary GH remained elevated during the entire pregnancy, contrary to the situation in normal women. Paradoxical GH release after TRH treatment was also present, whereas no response was observed in five normal control subjects. GH pulsatility studies revealed a highly pulsatile secretory pattern of pituitary GH, in contrast to that in normal woman, whose placental GH is secreted tonically. Tissue placental GH concentrations were within the range of levels in normal placentas. An increase in serum IGF-I in late pregnancy was also similar to that observed in normal pregnancy. These findings confirm that increased IGF-I levels are not pituitary GH dependent in late pregnancy. They add new evidence that adenomatous somatotrophs lack an IGF-I-dependent feedback regulation present in normal somatotrophs. [less ▲]

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See detailIDENTIFICATION OF PLACENTAL HUMAN GROWTH-HORMONE AS THE GROWTH HORMONE-V GENE-EXPRESSION PRODUCT
Frankenne, Francis ULg; Scippo, Marie-Louise ULg; Van Beeumen, Jos et al

in Journal Of Clinical Endocrinology And Metabolism (1990), 71(1), 15-18

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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 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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