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See detailProteins in the gas phase
Meyer, Tim; Gabelica, Valérie ULg; Grubmüller, Helmut et al

in Wiley Interdisciplinary Reviews: Computational Molecular Science (in press)

Proteins are complex macromolecules that evolved over billions of years to be active in aqueous solution. Water is a key element that stabilizes their structure, and most structural studies on proteins ... [more ▼]

Proteins are complex macromolecules that evolved over billions of years to be active in aqueous solution. Water is a key element that stabilizes their structure, and most structural studies on proteins have thus been carried out in aqueous environment. However, recent experimental approaches have opened the possibility to gain structural information on proteins from gas-phase measurements. The obtained results revealed significant structural memory in proteins when transferred from water to the gas phase. However, after several years of experimental and theoretical research, the nature of the structural changes induced by vaporization, the exact characteristics of proteins in the gas phase, and the physicochemical forces stabilizing dehydrated proteins are still unclear. We will review here these issues using both experimental and theoretical sources of information. [less ▲]

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See detailProteins of Bovine Herpesvirus Type 4 Released into the Culture Medium of Productively Infected Cells: Identification of a 135k Glycoprotein Involved in Viral Attachment
Dubuisson, J.; Koromyslov, I.; Pastoret, Paul-Pierre ULg et al

in Journal of General Virology (The) (1992), 73((Pt 1)), 189-94

Three bovine herpesvirus type 4 (BHV-4) proteins released into the culture medium of infected cells were identified, with Mr values of 135K, 16K and 14.5K. Among these three proteins, two were ... [more ▼]

Three bovine herpesvirus type 4 (BHV-4) proteins released into the culture medium of infected cells were identified, with Mr values of 135K, 16K and 14.5K. Among these three proteins, two were precipitated by the monoclonal antibodies characterized in this work. One is a glycoprotein of 135K (gp8) which does not seem to be involved in BHV-4 neutralization. Moreover, this 135K glycoprotein adsorbed onto uninfected susceptible cells. The attachment of gp8 to cells was totally inhibited by the prior adsorption of unlabelled viral proteins. Moreover, anti-gp8 monoclonal antibodies were effective in inhibiting the adsorption of gp8. These results indicate that gp8 could be involved in BHV-4 attachment. [less ▲]

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See detailProteins Specified by Bovine Herpesvirus Type 4: Structural Proteins of the Virion and Identification of Two Major Glycoproteins by Using Monoclonal Antibodies
Dubuisson, Jean; Boulanger, Denise; Bublot, Michel et al

in Journal of General Virology (1989), 70 (Pt 7)

Bovine herpesvirus type 4 proteins were identified by PAGE of [35S]methionine- or [3H]glucosamine-labelled purified virions. Thirty-one monoclonal antibodies (MAbs) raised against the V. Test strain were ... [more ▼]

Bovine herpesvirus type 4 proteins were identified by PAGE of [35S]methionine- or [3H]glucosamine-labelled purified virions. Thirty-one monoclonal antibodies (MAbs) raised against the V. Test strain were used to identify 29 proteins, ten of which were glycosylated. All of these glycoproteins belonged to the viral envelope and a 140K non-glycosylated protein appeared to be the major nucleocapsid protein. The MAbs were classified into two groups. The first group precipitated three glycoproteins of Mr 150K, 120K and 51K. The 120K and 51K glycoproteins were linked by disulphide bonds and the 150K glycoprotein was linked to the others by non-covalent bonds. The second group precipitated a different 120K glycoprotein. [less ▲]

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See detailProtelos – unrivalled efficacy in the short-and long-term
Reginster, Jean-Yves ULg

in OsteOpinion (2008), 4

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See detailProtene del latte: le protein del futuro
Paquot, Michel ULg

in Le protein del latte e derivati: verita nutrizionali Masson (1994)

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See detailThe proteolytic activity of MT4-MMP is required for its proangiogenic and pro-metastatic promoting effects
Host, Lorin; Paye, Alexandra ULg; Detry, Benoît ULg et al

in International Journal of Cancer = Journal International du Cancer (2012), 131(7), 1537-1548

MT4-MMP expression in breast adenocarcinoma stimulates tumor growth and metastatic spreading to the lung. However whether these pro-tumorigenic and pro-metastatic effects of MT4-MMP are related to a ... [more ▼]

MT4-MMP expression in breast adenocarcinoma stimulates tumor growth and metastatic spreading to the lung. However whether these pro-tumorigenic and pro-metastatic effects of MT4-MMP are related to a proteolytic action is not known yet. Through site directed mutagenesis MT4-MMP has been inactivated in cancer cells through Glutamic acid 249 substitution by Alanine in the active site. Active MT4-MMP triggered an angiogenic switch at day 7 after tumor implantation and drastically accelerated subcutaneous tumor growth as well as lung colonization in RAG -/- mice. All these effects were abrogated upon MT4-MMP inactivation. In sharp contrast to most MMPs being primarily of stromal origin, we provide evidence that tumor-derived MT4-MMP, but not host-derived MT4-MMP contributes to angiogenesis. A genetic approach using MT4-MMP-deficient mice revealed that the status of MT4-MMP produced by host cells did not affect the angiogenic response. Despite of this tumor intrinsic feature, to exert its tumor promoting effect, MT4-MMP requires a permissive microenvironment. Indeed, tumor-derived MT4-MMP failed to circumvent the lack of an host angio-promoting factor such as lasminogen activator inhibitor (PAI-1). Overall, our study demonstrates the key contribution of MT4-MMP catalytic activity in the tumor compartment, at the interface with host cells. It identifies MT4-MMP as a key intrinsic tumor cell determinant that contributes to the elaboration of a permissive microenvironment for metastatic dissemination [less ▲]

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See detailProteolytic and depilatory activities of actinomycetin
Ghuysen, Jean-Marie ULg

in Comptes Rendus des Séances de la Société de Biologie et de ses Filiales (1954), 148

cf. C.A. 47, 6491c; 49, 422d. Actinomycetin, obtained from Streptomyces albus G, was shown to contain 5 distinct enzymes which attack, resp., heat-killed Escherichia coli, keratin, mucin, casein, and a ... [more ▼]

cf. C.A. 47, 6491c; 49, 422d. Actinomycetin, obtained from Streptomyces albus G, was shown to contain 5 distinct enzymes which attack, resp., heat-killed Escherichia coli, keratin, mucin, casein, and a component of the epidermis the destruction of which results in epidermal desquamation and loosening of the hair. The substrate of this last enzyme is a complex protein component of the skin extractable by urea soln. (with or without KCl) at 25°. Another fraction of the epidermis, extractable under similar conditions at 0°, appears to be sensitive to the keratinolytic enzyme. [on SciFinder(R)] [less ▲]

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See detailProteolytic Breakdown Of Gliadin By Enterococcus Faecalis Isolated From Tunisian Fermented Dough
M'Hir, S.; Aldric, Jean-Marc ULg; El Mejdoub, Thami ULg et al

in World Journal of Microbiology & Biotechnology (2008), 24(12),

The aim of this work was to select strains with proteolytic activity on wheat gliadin, among lactic acid bacteria, previously isolated from Tunisian fermented wheat dough. Hydrolysis of gliadin, as sole ... [more ▼]

The aim of this work was to select strains with proteolytic activity on wheat gliadin, among lactic acid bacteria, previously isolated from Tunisian fermented wheat dough. Hydrolysis of gliadin, as sole nitrogen source, in an agar medium was visualized by a clear zone surrounding colonies. The increase in absorbance due to gliadin breakdown was measured spectrophotometrically using Ophthaldialdehyde (OPA) on Gliadin Glucose Broth medium. Fermented liquid dough inoculated with individual selected Enterococcus faecalis, showed a decrease of the gliadin concentration from 45 g/kg to 18 g/kg determined by sandwich ELISA test (R-7001). Only the enterococci strains show an hydrolysis of gliadin proteins. Strains showing proteolytic activity are gaining more and more importance in cereal based fermented foods and may help to reduce gliadin involved in coeliac disease. [less ▲]

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See detailProteolytic cleavage confers nitric oxide synthase inducing activity upon prolactin
Corbacho, A. M.; Nava, G.; Eiserich, J. P. et al

in Journal of Biological Chemistry (2000), 275(18), 13183-6

Prolactin (PRL), originally associated with milk secretion, is now known to possess a wide variety of biological actions and diverse sites of production beyond the pituitary. Proteolytic cleavage is a ... [more ▼]

Prolactin (PRL), originally associated with milk secretion, is now known to possess a wide variety of biological actions and diverse sites of production beyond the pituitary. Proteolytic cleavage is a common post-translational modification that can either activate precursor proteins or confer upon the peptide fragment unique biological actions not exerted by the parent molecule. Recent studies have demonstrated that the 16-kDa N-terminal proteolytic cleavage product of PRL (16K-PRL) acts as a potent inhibitor of angiogenesis. Despite previous demonstrations of 16K-PRL production in vivo, biological functions beyond its antiangiogenic actions remain unknown. Here we show that 16K-PRL, but not full-length PRL, acts to promote the expression of the inducible isoform of nitric oxide synthase (iNOS) and nitric oxide (*NO) production by pulmonary fibroblasts and alveolar type II cells with potency comparable with the proinflammatory cytokines interleukin-1beta, interferon gamma, and tumor necrosis factor alpha. The differential effect of 16K-PRL versus PRL occurs through a receptor distinct from known PRL receptors. Additionally, pulmonary fibroblasts express the PRL gene and endogenously produce 16K-PRL, suggesting that this pathway may serve both autocrine and paracrine roles in the regulation of *NO production. These results reveal that proteolytic cleavage of PRL confers upon this classical hormone potent iNOS inducing activity, suggesting its role in inflammatory/immune processes. [less ▲]

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See detailProteome alteration induced by hTERT transfection of human fibroblast cells
Mazzucchelli, Gabriel ULg; Gabelica, Valérie ULg; Smargiasso, Nicolas ULg et al

in Proteome Science (2008), 6(1), 12

Background: Telomerase confers cellular immortality by elongating telomeres, thereby circumventing the Hayflick limit. Extended-life-span cells have been generated by transfection with the human ... [more ▼]

Background: Telomerase confers cellular immortality by elongating telomeres, thereby circumventing the Hayflick limit. Extended-life-span cells have been generated by transfection with the human telomerase reverse transcriptase (hTERT) gene. hTERT transfected cell lines may be of outstanding interest to monitor the effect of drugs targeting the telomerase activity. The incidence of hTERT gene transfection at the proteome level is a prerequisite to that purpose. The effect of the transfection has been studied on the proteome of human fibroblast (W138). Cytosolic and nuclear fractions of W138 cells, empty vector transfected W138 (W138-HPV) and hTERT W138 cells were submitted to a 2D-DIGE (Two-Dimensional Differential In-Gel Electrophoresis) analysis. Only spots that had a similar abundance in W138 and W138-HPV, but were differentially expressed in W138 hTERT were selected for MS identification. This method directly points to the proteins linked with the hTERT expression. Number of false positive differentially expressed proteins has been excluded by using control W138-HPV cells. The proteome alteration induced by hTERT W138 transfection should be taken into account in subsequent use of the cell line for anti-telomerase drugs evaluation. Results: 2D-DIGE experiment shows that 57 spots out of 2246 are significantly differentially expressed in the cytosolic fraction due to hTERT transfection, and 38 were confidently identified. In the nuclear fraction, 44 spots out of 2172 were selected in the differential proteome analysis, and 14 were identified. The results show that, in addition to elongating telomeres, hTERT gene transfection has other physiological roles, among which an enhanced ER capacity and a potent cell protection against apoptosis. Conclusion: We show that the methodology reduces the complexity of the proteome analysis and highlights proteins implicated in other processes than telomere elongation. hTERT induced proteome changes suggest that telomerase expression enhances natural cell repair mechanisms and stress resistance probably required for long term resistance of immortalized cells. Thus, hTERT transfected cells can not be only consider as an immortal equivalent to parental cells but also as cells which are over-resistant to stresses. These findings are the prerequisite for any larger proteomics aiming to evaluate anti-telomerase drugs proteome alteration and thus therapeutics induced cell reactions. [less ▲]

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See detailProteome analysis of the bovine milk fat globule: Enhancement of membrane purification
Vanderghem, Caroline ULg; Blecker, Christophe ULg; Danthine, Sabine ULg et al

in International Dairy Journal (2008), 18(9), 885-893

A simple and rapid procedure was cl developed for the extraction of the milk fat globule membrane from milk removes the large majority of the skim milk proteins for proteome analysis. In order to improve ... [more ▼]

A simple and rapid procedure was cl developed for the extraction of the milk fat globule membrane from milk removes the large majority of the skim milk proteins for proteome analysis. In order to improve the extraction and the solubilization of the hydrophobic membrane proteins for subsequent two-dimensional gel electrophoresis, four detergents (3-[(3-cholamidopropyl)dimethylammoniol-1-propanesulfonate, amidosulfobetaine-14, sodium lauroyl sarcosinate and sodium deoxycholate) were tested in the sample preparation, associated with a sonication step. Zwitterionic detergents were shown to be efficient in recovering integral and peripheral proteins from membrane material. Spots were identified by matrix-assisted laser desorption/ionization tandem-time-of-flight (MALDI-TOF/TOF). The advantages of MALDI-TOF/TOF (speed, easiness of analysis, good sensitivity and high mass accuracy) were demonstrated on the milk fat globule membrane proteome investigation. Identified proteins are implicated in a wide range of functions including fat secretion and transport, protein trafficking and regulation. (C) 2008 Elsevier Ltd. All rights reserved. [less ▲]

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See detailProteome variations of the Myzus persicae aphid according to host plant change.
Francis, Frédéric ULg; GERKENS, P.; Harmel, Nicolas ULg et al

in Insect Biochemistry and Molecular Biology (2006), 36(3), 219-227

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See detailProteomic analyses of serous and endometrioid epithelial ovarian cancers - cases studies - molecular insights of a possible histological etiology of serous ovarian cancer.
Longuespée, Rémi ULg; Gagnon, Hugo; Boyon, Charlotte et al

in Proteomics. Clinical Applications (2013), 7(5-6), 337-54

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See detailProteomic analysis of human pancreas cancers for the identification of targetable biomarkers
Castronovo, Vincenzo ULg; Wang, Ying Hong; Musmeci, Davide et al

(2010)

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See detailProteomic analysis of ovine muscle hypertrophy.
Hamelin, M.; Sayd, T.; Chambon, C. et al

in Journal of Animal Science (2006), 84(12), 3266-76

Two-dimensional electrophoresis was used to investigate the effects of a QTL for muscle hypertrophy on sarcoplasmic protein expression in ovine muscles. In the Belgian Texel breed, the QTL for muscle ... [more ▼]

Two-dimensional electrophoresis was used to investigate the effects of a QTL for muscle hypertrophy on sarcoplasmic protein expression in ovine muscles. In the Belgian Texel breed, the QTL for muscle hypertrophy is localized in the myostatin-encoding gene. Based on microsatellite markers flanking the myostatin gene, we compared the hypertrophied genotype with the normal genotype. The average age of the sheep was 3 mo. Among the 4 muscles studied, in the hypertrophied genotype only the vastus medialis was normal, whereas the semimembranosus, tensor fasciae latae, and LM were hypertrophied. In the hypertrophied genotype, these muscles showed upregulation of enzymes involved in glycolytic metabolism together with oxidative metabolism in LM. Certain chaperone proteins, including glutathione S-transferase-Pi, heat shock protein-27, and heat shock cognate-70, were also more highly expressed, probably due to increased use of energetic pathways. Expression of the iron transport protein transferrin was increased. Alpha-1-antitrypsin was the only protein showing a similar pattern of expression (i.e., less expressed) in all 4 muscles of the hypertrophied genotype. It is suggested that transferrin and alpha-1-antitrypsin may interact to reinforce myogenic proliferative signaling. [less ▲]

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See detailProteomic analysis of telomerase inhibition by telomere specific ligands
Mazzucchelli, Gabriel ULg; Gabelica, Valérie ULg; Smargiasso, Nicolas ULg et al

in Anticancer Research (2008), 28(5c), 3257-3258

Telomeres consist of protein complexes and repeated ‘TTAGGG’ double strand DNA sequences ended by a 3’ single strand DNA of the same sequence. Progressive telomere shortening is observed in vitro upon ... [more ▼]

Telomeres consist of protein complexes and repeated ‘TTAGGG’ double strand DNA sequences ended by a 3’ single strand DNA of the same sequence. Progressive telomere shortening is observed in vitro upon cell divisions and with ageing in vivo. At a critical telomere length, shortened telomeres trigger a permanent growth arrest known as replicative senescence. Telomerase is an RNA-dependent DNA polymerase that extends telomeres by adding ‘TTAGGG’ repeats. It consists of a functional RNA component (hTR) which serves as template and a catalytic protein (hTERT) with reverse transcriptase activity. The expression of hTERT alone is sufficient for the immortalisation of cells. Telomerase is highly expressed in tumor cells but at very low level in most somatic cells. These observations make the telomerase an attractive target for anticancer strategies. One of these strategies relies on the use of drug candidates able to stabilize the particular telomere G-quadruplex DNA structures. The stabilization of these structures makes the telomere inaccessible for telomerase and thus inhibits telomerase activity. The effect of the hTERT transfection was first studied on the proteome of human WI38 fibroblast cells (1). Then, the proteome alteration response of hTERT transfected WI38 cells induced by the treatment of two G-quadruplexes ligands, telomestatin and TMPyP4, was analyzed. Both compounds can inhibit telomerase but have different selectivity for the different G-quadruplexes structures. Proteome analysis of the treated cells reveals that TMPyP4 induces much more protein expression alterations than telomestatin probably due to its poor selectivity. TMPyP4 induces especially a drastic down expression of the hnRNPs, a modulation of the proteasome pathway, an apparent decrease of the translation and an over expression of several molecular chaperones. Telomestatin induces in particular an over expression of the protein BCL2A1 which is involved in drug resistance of cancer cells and a probable increase of the translation. Both treatments have a common effect particularly on the molecular chaperone CCT (down expression), HSP90 alpha (over expression) and hnRNP D (down expression). The protein HSP90 alpha is also over expressed in hTERT transfected cells compared to parental cells. This protein is already a promising anticancer target protein due to its central role in oncogenesis and in telomerase activity regulation. 1 Mazzucchelli et al: Proteome Science 6: 12, 2008. [less ▲]

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