Browsing
     by title


0-9 A B C D E F G H I J K L M N O P Q R S T U V W X Y Z

or enter first few letters:   
OK
Full Text
Peer Reviewed
See detailDifferential elevation of matrix metalloproteinase expression in women exposed to levonorgestrel-releasing intrauterine system for a short or prolonged period of time
Labied, Soraya ULg; Galant, C.; Nisolle, Michelle ULg et al

in Human Reproduction (2009), 24(1), 113-121

BACKGROUND: The levonorgestrel-releasing intrauterine system (LNG-IUS) is an effective contraceptive and has many non-contraceptive health benefits. However, it is commonly associated with irregular ... [more ▼]

BACKGROUND: The levonorgestrel-releasing intrauterine system (LNG-IUS) is an effective contraceptive and has many non-contraceptive health benefits. However, it is commonly associated with irregular endometrial bleeding. Metalloproteinases contribute to extracellular matrix (ECM) remodelling and regulate bleeding during the menstrual cycle. Enhanced metalloproteinase expression participates in the pathogenesis of breakthrough bleeding. Thus the objective of this study was to compare matrix metalloproteinase (MMP) expression in endometrium during luteal phase and in short-term (1 month) and long-term (> or =6 months) LNG-IUS users. METHODS: MMP expression was analysed by semi-quantitative RT-PCR and immunohistochemistry. Gelatinase activity was determined by gelatin zymography. RESULTS: MMP-1, -2, -3, -7, -9 and -12 mRNAs levels were increased, whereas that of MMP-26 was decreased in the endometrium of LNG-IUS users. MMP-1, -2, -3, -7 and -9 were localized by immunohistochemistry in all biopsies in the short-term group but in only 0-27% in the control group. The incidence of positive immunostaining for MMP-2 and -3 decreased significantly in the long-term compared with short-term LNG-IUS users. MMP-26 was localized in all biopsies from the control group but in only 14 and 25% from the short- and long-term LNG-IUS groups, respectively. In both LNG groups, the numbers of macrophages (the major source of MMP-12) was increased. CONCLUSIONS: MMP-1, active MMP-2, MMP-3, MMP-7, MMP-9 and MMP-12 are more prevalent in the short-term LNG-IUS group, suggesting their important contribution to ECM breakdown and transient bleeding. The decrease in the percentage of women expressing MMP-2 and -3 might contribute to the decreased occurrence of unwanted spotting and bleeding in long-term LNG-IUS users. [less ▲]

Detailed reference viewed: 89 (10 ULg)
Full Text
Peer Reviewed
See detailDifferential Equations of Stiffened Panels
Rigo, Philippe ULg

in Dept. of Naval Architecture and Marine Engineering (2001)

Detailed reference viewed: 57 (2 ULg)
Full Text
Peer Reviewed
See detailDifferential Equations of Stiffened Panels and Fourier Series Expansion
Rigo, Philippe ULg; Richir, Thomas

in The Annals of “Dunarea De Jos” University of Galati (2005) (2005)

Detailed reference viewed: 40 (0 ULg)
Full Text
Peer Reviewed
See detailDifferential Equations of Stiffened Panels of Ship Structures & Fourier Series Expansions
Rigo, Philippe ULg

in Ship Technology Research = Schiffstechnik (2005)

Detailed reference viewed: 62 (4 ULg)
Full Text
Peer Reviewed
See detailDifferential expression of alpha1 (IV) and alpha5 (IV) collagen chains in basal-cell carcinoma.
Quatresooz, Pascale ULg; Martalo, Oriane; Pierard, Gérald ULg

in Journal of Cutaneous Pathology (2003), 30(9), 548-52

BACKGROUND: Basement membrane alterations are common in malignancies, and they may indicate tumoral aggressiveness. Distinct patterns of tumoral coverage by collagen IV were reported in nodular and ... [more ▼]

BACKGROUND: Basement membrane alterations are common in malignancies, and they may indicate tumoral aggressiveness. Distinct patterns of tumoral coverage by collagen IV were reported in nodular and aggressive basal-cell carcinomas (BCCs). Differential expressions of alpha (IV) collagen chains were also shown on frozen sections. The aim of our work was to document the immunohistochemical expression of alpha1, alpha3, and alpha5 (IV) collagen chains in BCC after routine fixation and processing. METHODS: The patterns of distribution of alpha1 (IV), alpha3 (IV), and alpha5 (IV) collagen chains were studied in 20 formalin-fixed and paraffin-embedded BCCs showing different infiltrative patterns. One trichoblastoma was used as control. RESULTS: In nodular BCCs, the expression of alpha5 (IV) collagen chain was downregulated and uneven. By contrast, alpha1 (IV) collagen chain expression was preserved around these tumors similar to the surrounding skin. However, the alpha1 (IV) collagen chain expression was discontinuous or absent in BCC areas showing an infiltrative pattern of extension. The alpha3 chain was absent both underneath all BCCs and non-neoplastic skin. CONCLUSIONS: The basement membrane alterations around nodular BCCs involved more precisely the alpha5 (IV) collagen chains. Defects in alpha1 (IV) collagen chain expression seemed to be associated with a tumoral invasive and infiltrative pattern. The biological significance of these findings is unclear. [less ▲]

Detailed reference viewed: 16 (5 ULg)
Full Text
Peer Reviewed
See detailDifferential expression of c-fos, Hsp70 and Hsp27 after photothrombotic injury in the rat brain.
Plumier, Jean-Christophe ULg; Armstrong, J. N.; Wood, N. I. et al

in Molecular Brain Research (1997), 45(2), 239-46

In situ hybridization and immunohistochemistry were used to examine the expression of c-fos, Hsp70 and Hsp27 following photothrombotic injury in the right fronto-parietal cortex of the rat. C-fos mRNA and ... [more ▼]

In situ hybridization and immunohistochemistry were used to examine the expression of c-fos, Hsp70 and Hsp27 following photothrombotic injury in the right fronto-parietal cortex of the rat. C-fos mRNA and protein were detected in the entire cerebral cortex on the lesioned side. Hsp70 mRNA accumulation was observed only adjacent and peripheral to the site of the lesion. At 1 h after photothrombotic injury, Hsp70 expression delineates the area of necrosis at 24 h after photothrombotic injury. Hsp27 protein was observed in the ipsilateral cerebral cortex with the exception of the deep layers of the cingulate cortex. In addition, while c-Fos immunoreactivity was localized in cell nuclei, Hsp27 immunoreactivity was detected in the cytoplasm of astrocytes. These results demonstrate that unilateral cortical injury induces changes in gene expression that vary according to cell type and brain region. [less ▲]

Detailed reference viewed: 14 (4 ULg)
Full Text
Peer Reviewed
See detailDifferential Expression of Cellular Prion Protein on Human Blood and Tonsil Lymphocytes
Antoine, Nadine ULg; Cesbron, J. Y.; Coumans, Bernard ULg et al

in Haematologica (2000), 85(5), 475-80

BACKGROUND AND OBJECTIVE: The expression of cellular prion protein (PrPc) on the surface of peripheral lymphocytes has been previously reported, but little is known about its expression on lymphoid cells ... [more ▼]

BACKGROUND AND OBJECTIVE: The expression of cellular prion protein (PrPc) on the surface of peripheral lymphocytes has been previously reported, but little is known about its expression on lymphoid cells from secondary lymph organs. In this report, we compare the surface expression of PrPc on human blood lymphocytes and tonsil lymphocytes. DESIGN AND METHODS: This analysis was performed by cytometry on live lymphocytes isolated from healthy donors or from the tonsils of adults or children. RESULTS: Human peripheral lymphocytes and tonsillar lymphoid cells, but not erythrocytes or granulocytes, express PrPc at their surfaces. Interestingly, we found significantly less PrPc on freshly isolated tonsil lymphocytes, both B and T, than on blood cells. Although tonsil cells bear less PrPc than circulating blood lymphocytes, they are able to express high quantities of PrPc on their surface when placed in culture. However, contrary to previous results, mitogen stimulation does not affect this expression on B- or T-cells. INTERPRETATION AND CONCLUSIONS: We suggest that the PrPc expression by lymphocytes may be modified by interactions occurring during intratissular migration or during cell-to-cell contacts. Whether PrPc plays a role in intracellular communication at this location, as it does in the nervous system, remains an open question. [less ▲]

Detailed reference viewed: 36 (4 ULg)
Full Text
Peer Reviewed
See detailDifferential expression of galectin 3 and galectin 1 in colorectal cancer progression.
Sanjuan, X.; Fernandez, P. L.; Castells, A. et al

in Gastroenterology (1997), 113(6), 1906-15

BACKGROUND & AIMS: Galectins are beta-galactoside-binding proteins possibly involved in tumor progression. The aim of this study was to determine the pattern of galectin 3 and galectin 1 expression and ... [more ▼]

BACKGROUND & AIMS: Galectins are beta-galactoside-binding proteins possibly involved in tumor progression. The aim of this study was to determine the pattern of galectin 3 and galectin 1 expression and involvement in colorectal cancer progression. METHODS: Galectin 3 expression was examined immunohistochemically in 39 samples of normal mucosae, 25 adenomas, 87 carcinomas, and 39 lymph node metastases. Galectin 1 was analyzed in 25 samples of mucosae, 15 adenomas, 25 carcinomas, and 11 metastases. Western blot analysis was also performed. RESULTS: All normal mucosae showed strong nuclear galectin 3 expression, which was down-regulated in the neoplastic progression, because only 60% of adenomas, 48% of carcinomas, and 44% of metastases were strongly positive (P < 0.0001). Cytoplasmic expression was down-regulated in adenomas (16%) but increased again in carcinomas (64%) (P < 0.0001). Galectin 1 expression was mainly detected in stromal cells and correlated with tumor progression from normal mucosae to adenomas and carcinomas (P < 0.0001). CONCLUSIONS: Galectin 3 expression is down-regulated in the initial stages of neoplastic progression, whereas a dissociated cytoplasmic expression increases in later phases of tumor progression. Galectin 1 in colorectal mucosa is predominantly a stromal product whose overexpression is associated with the neoplastic progression of colorectal cancer. [less ▲]

Detailed reference viewed: 13 (4 ULg)
Full Text
Peer Reviewed
See detailDifferential expression of galectin-1 and galectin-3 during first trimester human embryogenesis.
van den Brûle, Frédéric; Fernandez, Pedro L.; Buicu, Crina et al

in Developmental Dynamics : An Official Publication of the American Association of Anatomists (1997), 209(4), 399-405

Development of complex organisms requires specific temporospatial differentiation and expression of the correct phenotype through activation of a variety of genes. Galectins are mammalian lectins able to ... [more ▼]

Development of complex organisms requires specific temporospatial differentiation and expression of the correct phenotype through activation of a variety of genes. Galectins are mammalian lectins able to interact with various extracellular matrix glycoconjugates and have been implicated in several biological events including cell attachment, differentiation, apoptosis, embryogenesis, and cancer invasion and metastasis. In this study, we have examined the expression of galectin-1 and galectin-3 during human first trimester embryogenesis using immunohistochemistry and Western blotting. Variable amounts of galectin-1 and galectin-3 were detected in all tissue protein extracts. Galectin-1 expression was demonstrated in the connective tissue and derived tissues such as smooth and striated muscle cells, and in some epithelia, such as in the basal layers of the skin after 14 weeks and in the epithelial cells of the gonads. Galectin-3 was detected mainly in epithelia, such as the skin, epithelial lining of the digestive and respiratory tract, and urothelium and excretory tubes of the kidney, but also in the myocardial cells, in the peripheral and preossifying hypertrophic chondrocytes, and in the notochord and in the liver. Our study constitutes the first demonstration of galectin-1 and galectin-3 during human embryogenesis. The differential expression of these two lectins suggests that they could participate in the complex processes of tissue differentiation. [less ▲]

Detailed reference viewed: 61 (23 ULg)
Full Text
Peer Reviewed
See detailDifferential Expression of Genes and DNA Methylation associated with Prenatal Protein Undernutrition by Albumen Removal in an avian model
Willems, E.; Guerrero-Bosagna, C.; Decuypere, E. et al

in Scientific Reports (2016), 6

Previously, long-term effects on body weight and reproductive performance have been demonstrated in the chicken model of prenatal protein undernutrition by albumen removal. Introduction of such persistent ... [more ▼]

Previously, long-term effects on body weight and reproductive performance have been demonstrated in the chicken model of prenatal protein undernutrition by albumen removal. Introduction of such persistent alterations in phenotype suggests stable changes in gene expression. Therefore, a genomewide screening of the hepatic transcriptome by RNA-Seq was performed in adult hens. The albumendeprived hens were created by partial removal of the albumen from eggs and replacement with saline early during embryonic development. Results were compared to sham-manipulated hens and non-manipulated hens. Grouping of the differentially expressed (DE) genes according to biological functions revealed the involvement of processes such as 'embryonic and organismal development' and 'reproductive system development and function'. Molecular pathways that were altered were 'amino acid metabolism', 'carbohydrate metabolism' and 'protein synthesis'. Three key central genes interacting with many DE genes were identified: UBC, NR3C1, and ELAVL1. The DNA methylation of 9 DE genes and 3 key central genes was examined by MeDIP-qPCR. The DNA methylation of a fragment (UBC-3) of the UBC gene was increased in the albumen-deprived hens compared to the nonmanipulated hens. In conclusion, these results demonstrated that prenatal protein undernutrition by albumen removal leads to long-term alterations of the hepatic transcriptome in the chicken. [less ▲]

Detailed reference viewed: 6 (1 ULg)
Full Text
Peer Reviewed
See detailDifferential expression of plasminogen activator inhibitor-1, tumor necrosis factor-alpha, TNF-alpha converting enzyme and ADAMTS family members in murine fat territories
Vörös, Gabor; Maquoi, Erik ULg; Collen, Désiré et al

in Biochimica et Biophysica Acta-Gene Structure and Expression (2003), 1625(1), 36-42

ur objective was to investigate expression of A disintegrin and metalloproteinase (ADAM) and ADAM proteins with a thrombospondin (TS) motif (ADAMTS) family members in adipose tissue of lean and obese mice ... [more ▼]

ur objective was to investigate expression of A disintegrin and metalloproteinase (ADAM) and ADAM proteins with a thrombospondin (TS) motif (ADAMTS) family members in adipose tissue of lean and obese mice. Five-week-old male mice were kept on standard chow (SFD) or on high fat diet (HFD) for 15 weeks, and subcutaneous (SC) and gonadal (GON) adipose tissue, as well as mature adipocytes and stromal–vascular (S–V) cells were harvested. mRNA levels of plasminogen activator inhibitor-1 (PAI-1), tumor necrosis factor-α (TNF-α), ADAM-17 (TACE or TNF-α converting enzyme), ADAMTS-1 and ADAMTS-8 were quantified in isolated adipose tissues and cell fractions, and during differentiation of murine preadipocytes. The HFD resulted in a significantly enhanced weight of isolated SC and GON fat pads, and in enhanced blood levels of glucose, cholesterol and PAI-1. ADAM-17, TNF-α, PAI-1, ADAMTS-1 and ADAMTS-8 mRNA were detected in both SC and GON adipose tissue of lean mice (SFD). In SC adipose tissue of obese mice (HFD), the expression of ADAM-17 and PAI-1 was enhanced and that of ADAMTS-1 reduced, whereas in GON adipose tissue expression of TNF-α was enhanced and that of ADAMTS-8 reduced. In lean and obese mice, expression of ADAM-17, ADAMTS-1 and ADAMTS-8 was higher in the S–V cell fraction than in mature adipocytes. During differentiation of murine 3T3-F442A preadipocytes, expression of ADAM-17 and ADAMTS-1 remained virtually unaltered, whereas that of ADAMTS-8 decreased as adipocytes matured. Several ADAM and ADAMTS family members are expressed in adipose tissue and during differentiation of preadipocytes. Modulation of their expression upon development of obesity is adipose tissue-dependent. [less ▲]

Detailed reference viewed: 19 (0 ULg)
Full Text
Peer Reviewed
See detailDifferential expression of proteins in response to ceramide-mediated stress signal in colon cancer cells by 2-D gel electrophoresis and MALDI-TOF-MS.
Fillet, Marianne ULg; Cren-Olive, Cécile; Renert, A.-F. et al

in Journal of Proteome Research (2005), 4(3), 870-80

Comparative cancer cell proteome analysis is a strategy to study the implication of ceramides in the transmission of stress signals. To better understand the mechanisms by which ceramide regulate some ... [more ▼]

Comparative cancer cell proteome analysis is a strategy to study the implication of ceramides in the transmission of stress signals. To better understand the mechanisms by which ceramide regulate some physiological or pathological events and the response to the pharmacological treatment of cancer, we performed a differential analysis of the proteome of HCT-116 (human colon carcinoma) cells in response to these substances. We first established the first 2-dimensional map of the HCT-116 proteome. Then, HCT116 cell proteome treated or not with C6-ceramide have been compared using two-dimensional electrophoresis, matrix-assisted laser desorption/ionization-mass spectrometry and bioinformatic (genomic databases). 2-DE gel analysis revealed more than fourty proteins that were differentially expressed in control cells and cells treated with ceramide. Among them, we confirmed the differential expression of proteins involved in apoptosis and cell adhesion. [less ▲]

Detailed reference viewed: 22 (1 ULg)
Full Text
Peer Reviewed
See detailDifferential Expression of the 67-Kd Laminin Receptor and 31-Kd Human Laminin-Binding Protein in Human Ovarian Carcinomas
van den Brule, F. A.; Berchuck, A.; Bast, R. C. et al

in European Journal of Cancer (1994), 30A(8), 1096-9

The expression of the 67-kD laminin receptor (67LR) and the 31-kD human laminin-binding protein (HLBP31), two proteins involved in cancer cell laminin interaction, was evaluated on 30 ovarian cancer ... [more ▼]

The expression of the 67-kD laminin receptor (67LR) and the 31-kD human laminin-binding protein (HLBP31), two proteins involved in cancer cell laminin interaction, was evaluated on 30 ovarian cancer specimens. Expression of the 67LR was increased (up to 2.5-fold, in 87% of the patients), while HLBP31 expression was downregulated in cancer cells compared with the normal tissue, as detected by northern blotting and immunohistochemistry. The immunohistochemical study demonstrated that the 67LR was significantly overexpressed (P < 0.05) in the group of patients whose cytoreductive surgery was suboptimal, and those with poor clinical outcome. No correlation was observed between HLBP31 expression and clinicopathological features. Increased expression of the 67LR appears to correlate with the invasive phenotype of ovarian cancer cells and suggests a role of the latter in ovarian cancer invasion. [less ▲]

Detailed reference viewed: 13 (0 ULg)
Full Text
Peer Reviewed
See detailDifferential expression of the GTL2 gene within the callipyge region of ovine chromosome 18.
Bidwell, C. A.; Shay, T. L.; Georges, Michel ULg et al

in Animal Genetics (2001), 32(5), 248-56

The inheritance pattern of the skeletal muscle hypertrophy phenotype caused by the callipyge gene has been characterized as polar overdominance. We hypothesized that this trait may be caused by a gain or ... [more ▼]

The inheritance pattern of the skeletal muscle hypertrophy phenotype caused by the callipyge gene has been characterized as polar overdominance. We hypothesized that this trait may be caused by a gain or loss of gene expression because of the reversible nature of the phenotype in paternal vs. maternal inheritance. Suppression subtraction cDNA probes were made from skeletal muscle mRNA of normal (NN) and callipyge (C(Pat)N(Mat)) animals and hybridized to Southern blots containing bacterial artificial chromosomes (BACs) that comprise a physical contig of the callipyge region. The CN-NN probes hybridized to two ovine and seven bovine BACs. Sequence analysis of fragments within those BACs indicated short regions of similarity to mouse gene trap locus (gtl2). Northern blots analysis of RNA from hypertrophy-responsive muscles show a population of GTL2 mRNA centred around 2.4 kb that were abundantly expressed in 14-day prenatal NN and C(Pat)N(Mat) lambs but were down-regulated in day 14 and day 56 postnatal NN lambs. The expression of GTL2 remained elevated in 14- and 56-day-old C(Pat)N(Mat) lambs as well as in 56-day-old N(Pat)C(Mat) and CC lambs. Expression of GTL2 in the supraspinatus, which does not undergo hypertrophy, was very low for all genotypes and ages. Isolation of cDNA sequences show extensive alternative splicing and a lack of codon bias suggesting that GTL2 does not encode a protein. The mutation of the callipyge allele has altered postnatal expression of GTL2 in muscles that undergo hypertrophy and will help identify mechanisms involved in growth, genomic imprinting and polar overdominance. [less ▲]

Detailed reference viewed: 6 (1 ULg)
Full Text
Peer Reviewed
See detailDifferential expression of two somatostatin genes during zebrafish embryonic development
Devos, Nathalie; Deflorian, Gianluca; Biemar, Frédéric et al

in Mechanisms of Development (2002), 115(1-2), 133-7

We have identified the cDNAs of two new zebrafish preprosomatostatins, PPSS1 and PPSS3, in addition to the previously cloned PPSS2 (Argenton et al., 1999). PPSS1 is the orthologue of mammalian PPSSs, with ... [more ▼]

We have identified the cDNAs of two new zebrafish preprosomatostatins, PPSS1 and PPSS3, in addition to the previously cloned PPSS2 (Argenton et al., 1999). PPSS1 is the orthologue of mammalian PPSSs, with a conserved C-terminal SS-14 sequence, PPSS2 is a divergent SS precursor and PPSS3 is a cortistatin-like prohormone. Using whole-mount in situ hybridisation, we have analysed the expression of PPSS1 and PPSS2 in zebrafish embryos up to 5 days post fertilisation. PPSS1 was expressed in the developing pancreas and central nervous system (CNS), whereas PPSS2 expression was exclusively pancreatic. In the CNS, PPSS1 was detected in several areas, in particular in the vagal motor nucleus and in cells that pioneer the tract of the postoptic commissure. PPSS1 was also expressed transiently in the telencephalon and spinal motor neurons. In all areas but the telencephalon PPSS1 was coexpressed with islet-1. [less ▲]

Detailed reference viewed: 36 (6 ULg)
Full Text
Peer Reviewed
See detailDifferential expression of vascular endothelial growth factor and its receptors in hematopoietic and fatty bone marrow: evidence that neuropilin-1 is produced by fat cells.
Belaid, Zakia ULg; Hubint, Frederique; Humblet, Chantal ULg et al

in Haematologica (2005), 90(3), 400-1

Vascular endothelial growth factor (VEGF), its receptors (VEGFR-1, VEGFR-2) and neuropillin-1 (NRP-1) are expressed at variable levels in bone marrow. NRP-1expression is higher in fatty bone marrow than ... [more ▼]

Vascular endothelial growth factor (VEGF), its receptors (VEGFR-1, VEGFR-2) and neuropillin-1 (NRP-1) are expressed at variable levels in bone marrow. NRP-1expression is higher in fatty bone marrow than in hematopoietic marrow. Adipocytes are responsible for NRP-1 expression suggesting that they may play a role in hematopoiesis by producing NRP-1 or that NRP-1 may regulate adipocyte activity. [less ▲]

Detailed reference viewed: 44 (6 ULg)
Full Text
Peer Reviewed
See detailDifferential expression of Vegfr-2 and its soluble form in preeclampsia.
Munaut, Carine ULg; LORQUET, Sophie ULg; Pequeux, Christel ULg et al

in PLoS ONE (2012), 7(3), 33475

Background: Several studies have suggested that the main features of preeclampsia (PE) are consequences of endothelial dysfunction related to excess circulating anti-angiogenic factors, most notably ... [more ▼]

Background: Several studies have suggested that the main features of preeclampsia (PE) are consequences of endothelial dysfunction related to excess circulating anti-angiogenic factors, most notably, soluble sVEGFR-1 (also known as sFlt-1) and soluble endoglin (sEng), as well as to decreased PlGF. Recently, soluble VEGF type 2 receptor (sVEGFR-2) has emerged as a crucial regulator of lymphangiogenesis. To date, however, there is a paucity of information on the changes of VEGFR-2 that occur during the clinical onset of PE. Therefore, the aim of our study was to characterize the plasma levels of VEGFR-2 in PE patients and to perform VEGFR-2 immunolocalization in placenta. METHODOLOGY/PRINCIPAL FINDINGS: By ELISA, we observed that the VEGFR-2 plasma levels were reduced during PE compared with normal gestational age matched pregnancies, whereas the VEGFR-1 and Eng plasma levels were increased. The dramatic drop in the VEGFR-1 levels shortly after delivery confirmed its placental origin. In contrast, the plasma levels of Eng and VEGFR-2 decreased only moderately during the early postpartum period. An RT-PCR analysis showed that the relative levels of VEGFR-1, sVEGFR-1 and Eng mRNA were increased in the placentas of women with severe PE. The relative levels of VEGFR-2 mRNA as well as expressing cells, were similar in both groups. We also made the novel finding that a recently described alternatively spliced VEGFR-2 mRNA variant was present at lower relative levels in the preeclamptic placentas. CONCLUSIONS/SIGNIFICANCE: Our results indicate that the plasma levels of anti-angiogenic factors, particularly VEGFR-1 and VEGFR-2, behave in different ways after delivery. The rapid decrease in plasma VEGFR-1 levels appears to be a consequence of the delivery of the placenta. The persistent circulating levels of VEGFR-2 suggest a maternal endothelial origin of this peptide. The decreased VEGFR-2 plasma levels in preeclamptic women may serve as a marker of endothelial dysfunction. [less ▲]

Detailed reference viewed: 80 (7 ULg)
Full Text
Peer Reviewed
See detailDifferential Functionalities of Amphiphilic Peptide Segments of the Cell-Septation Penicillin-Binding Protein 3 of Escherichia Coli
Marrec-Fairley, Monique; Piette, André ULg; Gallet, Xavier et al

in Molecular Microbiology (2000), 37(5), 1019-1031

The class B M1-V577 penicillin-binding protein (PBP) 3 of Escherichia coli consists of a M1-L39 membrane anchor (bearing a cytosolic tail) that is linked via a G40-S70 intervening peptide to an R71-I236 ... [more ▼]

The class B M1-V577 penicillin-binding protein (PBP) 3 of Escherichia coli consists of a M1-L39 membrane anchor (bearing a cytosolic tail) that is linked via a G40-S70 intervening peptide to an R71-I236 non-catalytic module (containing the conserved motifs 1-3) itself linked via motif 4 to a D237-V577 catalytic module (containing the conserved motifs 5-7 of the penicilloyl serine transferases superfamily). It has been proposed that during cell septation the peptidoglycan crosslinking activity of the acyl transferase module of PBP3 is regulated by the associated M1-I236 polypeptide itself in interaction with other components of the divisome. The fold adopted by the R71-V577 polypeptide of PBP3 has been modelled by reference to the corresponding R76-S634 polypeptide of the class B Streptococcus pneumoniae PBP2x. Based on these data and the results of site-directed mutagenesis of motifs 1-3 and of peptide segments of high amphiphilicity (identified from hydrophobic moment plots), the M1-I236 polypeptide of PBP3 appears to be precisely designed to work in the way proposed. The membrane anchor and the G40-S70 sequence (containing the G57-Q66 peptide segment) upstream from the non-catalytic module have the information ensuring that PBP3 undergoes proper insertion within the divisome at the cell septation site. Motif 1 and the I74-L82 overlapping peptide segment, motif 2 and the H160-G172 overlapping peptide segment, and the G188-D197 motif 3 are located at or close to the intermodule junction. They contain the information ensuring that PBP3 folds correctly and the acyl transferase catalytic centre adopts the active configuration. The E206-V217 peptide segment is exposed at the surface of the non-catalytic module. It has the information ensuring that PBP3 fulfils its cell septation activity within the fully complemented divisome. [less ▲]

Detailed reference viewed: 84 (23 ULg)