References of "Castronovo, Vincenzo"
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See detailHistone deacetylase HDAC8 associates with smooth muscle alpha–actin and is essential for smooth muscle cell contractility
Glénisson, Wendy; Waltregny, David ULg; Tran, Syv Li et al

Conference (2006)

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See detailStudy of the role of histone deacetylases in myofibroblastic differenciation
Glénisson, Wendy; Waltregny, David ULg; Castronovo, Vincenzo ULg

Scientific conference (2006)

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See detailEvaluation of original dual thromboxane A2 modulators as anti-angiogenic agents
Dassesse, Thibaut; de Leval, Xavier; Dogné, Jean-Michel et al

Scientific conference (2006)

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See detailIdentification of accessible proteins expressed in human breast cancer
Castronovo, Vincenzo ULg; Kischel, Philippe; Guillonneau, François et al

Scientific conference (2006)

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See detailHistone deacetylase 7 is involved in the control of angiogenesis by regulating platelet-derived growth factor-β
Mottet, Denis; Bellahcene, Akeila ULg; Deroanne, Christophe et al

Conference (2006)

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See detailRole of tumor-associated lipogenesis in the formation and composition of membrane microdomains
Timmermans, L.; Kischel, Philippe; Beckers, Albert ULg et al

Conference (2006)

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See detailRole of histone deacetylases in myofibroblastic differenciation
Glénisson, Wendy; Waltregny, David ULg; Castronovo, Vincenzo ULg

Conference (2006)

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See detailDéveloppement de modulateurs de la voie du thromboxane A2 en tant qu’agents anti-angiogéniques et anti-métastatiques
De Leval, X.; Dassesse, T.; Dogne, J. M. et al

Poster (2005, May)

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See detailDentin sialophosphoprotein expression correlates with progression markers in human prostate cancer
Chaplet, Michael; Waltregny, David ULg; Detry, Cédric ULg et al

in Journal of Bone and Mineral Research (2005), 20(Suppl. 2), 45

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See detailHistone deacetylase HDAC8 associates with smooth muscle alpha-actin and is essential for smooth muscle cell contractility
Waltregny, David ULg; Glenisson, Wendy; Tran, Syv Li et al

in FASEB Journal (2005), 19(8), 966-968

Although originally characterized as nuclear enzymes controlling the stability of nucleosomes, histone deacetylases (HDACs) may also exert their activity within the cytosol. Recently, we have demonstrated ... [more ▼]

Although originally characterized as nuclear enzymes controlling the stability of nucleosomes, histone deacetylases (HDACs) may also exert their activity within the cytosol. Recently, we have demonstrated that HDAC8, a class I HDAC, is a novel, prominently cytosolic marker of smooth muscle differentiation. As HDAC8 displays a striking stress fiber-like pattern of distribution and is coexpressed in vivo with smooth muscle alpha-actin (alpha-SMA) and smooth muscle myosin heavy chain, we have explored the possible participation of this HDAC in smooth muscle cytoskeleton regulation. Cell fractionation assays performed with primary human smooth muscle cells (HSMCs) showed that HDAC8, in contrast to HDAC1 and HDAC3, was enriched in cytoskeleton-bound protein fractions and insoluble cell pellets, suggesting an association of HDAC8 with the cystoskeleton. Coimmunoprecipitation experiments using HSMCs, NIH-3T3 cells, and human prostate tissue lysates further demonstrated that HDAC8 associates with alpha-SMA but not with beta-actin. HDAC8 silencing through RNA interference strongly reduced the capacity of HSMCs to contract collagen lattices. Mock transfections had no effect on HSMC contractily, and transfections with small interfering RNAs (siRNAs) specific for HDAC6, a cytosolic HDAC that functions as an alpha-tubulin deacetylase, resulted in a weak contraction inhibition. Although mock- and HDAC6 siRNA-transfected HSMCs showed no noticeable morphological changes, HDAC8 siRNA-transfected HSMCs displayed a size reduction with diminished cell spreading after replating. Altogether, our findings indicate that HDAC8 associates with the smooth muscle actin cytoskeleton and may regulate the contractile capacity of smooth muscle cells. [less ▲]

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See detailHistone deacetylase HDAC8 associates with smooth muscle alpha–actin and is essential for smooth muscle cell contractility
Glénisson, Wendy; Waltregny, David ULg; Tran, Syv Li et al

Conference (2005)

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See detailExpression of dentin sialophosphoprotein in human prostate cancer and its correlation with tumor aggressiveness
Waltregny, David ULg; Chaplet, Michael; Detry, Cédric et al

Conference (2005)

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See detailDentin sialophosphoprotein expression correlates with progression markers in human prostate cancer
Chaplet, Michael; Waltregny, David ULg; Detry, Cédric et al

Conference (2005)

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See detailZoledronic acid up-regulates bone sialoprotein expression in osteoblastic cells through Rho GTPase inhibition
Chaplet, Michaël; Deroanne, Christophe ULg; Fisher, Larry W. et al

in Biochemical Journal (2004), 384(Pt 3), 591-598

Clinical practice reveals that osteoporotic women treated with BPs (bisphosphonates) show an increased bone mass density and a reduced risk of fractures. However, the mechanisms leading to these ... [more ▼]

Clinical practice reveals that osteoporotic women treated with BPs (bisphosphonates) show an increased bone mass density and a reduced risk of fractures. However, the mechanisms leading to these beneficial effects of BPs are still poorly understood. We hypothesized that ZOL (zoledronic acid), a potent third-generation BP, may induce the expression of proteins associated with the bone-forming potential of osteoblastic cells such as BSP (bone sialoprotein). Expression of BSP gene is up-regulated by hormones that promote bone formation and has been associated with de novo bone mineralization. Using real-time reverse transcriptase-PCR and Western-blot analysis, we demonstrated that ZOL increased BSP expression in Saos-2 osteoblast-like cells. Nuclear run-on and mRNA decay assays showed no effect at the transcriptional level but a stabilization of BSP transcripts in ZOL-treated cells. ZOL effect on BSP expression occurred through an interference with the mevalonate pathway since it was reversed by either mevalonate pathway intermediates or a Rho GTPase activator. We showed that ZOL impaired membrane localization of RhoA in Saos-2 cells indicating reduced prenylation of this protein. By the use of small interfering RNAs directed to RhoA and Rac1, we identified both Rho GTPases as negative regulators of BSP expression in Saos-2 cells. Our study demonstrates that ZOL induces BSP expression in osteoblast-like cells through inactivation of Rho GTPases and provides a potential mechanism to explain the favourable effects of ZOL treatment on bone mass and integrity. [less ▲]

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See detailLignées de carcinome prostatique et apoptose: état de la question
Califice, Stéphane ULg; Waltregny, David ULg; Castronovo, Vincenzo ULg et al

in Revue Médicale de Liège (2004), 59(12), 704-10

Prostate cancer is a major pathology in industrialized countries. Tumor growth usually results from increased cell proliferation, conjugated with an inhibition of programmed cell death (apoptosis). In ... [more ▼]

Prostate cancer is a major pathology in industrialized countries. Tumor growth usually results from increased cell proliferation, conjugated with an inhibition of programmed cell death (apoptosis). In this paper, after a short description of the apoptotic mechanisms and their methods of investigation, we review the present knowledge of the implication of different molecular actors in the regulation of apoptosis in prostate cancer cells. This review notably summarizes the present knowledge of the (de)regulation of the effects of androgens, p53, Bcl-2, Bcl-xL, Bax, Akt, PTEN, Par-4, clusterine, caspases and NF-kappaB in prostate adenocarcinoma cell lines and provides an appraisal of their therapeutic potential. A better knowledge of the apoptotic pathways in these cells could indeed allow the development of new selective and effective anti-cancer strategies. [less ▲]

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See detailGalectin-3 and Cancer (Review)
Califice, Stéphane; Castronovo, Vincenzo ULg; van den Brûle, Fréderic

in International Journal of Oncology (2004), 25(4), 983-92

Galectin-3 is a pleiotropic carbohydrate-binding protein involved in a variety of normal and pathological biological processes. Its carbohydrate-binding properties constitute the basis for cell-cell and ... [more ▼]

Galectin-3 is a pleiotropic carbohydrate-binding protein involved in a variety of normal and pathological biological processes. Its carbohydrate-binding properties constitute the basis for cell-cell and cell-matrix interactions and cancer progression. Modulation of galectin-3 expression in cancer cells has indeed been reported. These observations lead to the recognition of galectin-3 as a diagnostic/prognostic marker for specific cancer types, such as thyroid and prostate. This review discusses the expression and cellular localization of galectin-3 in cancer cells, as well as its numerous functions in cancer cell biology, including cell-cell adhesion, cell-matrix interactions, growth regulation, apoptosis, angiogenesis and mRNA splicing. [less ▲]

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See detailDual activities of galectin-3 in human prostate cancer: tumor suppression of nuclear galectin-3 vs tumor promotion of cytoplasmic galectin-3
Castronovo, Vincenzo ULg; Bracke, M.; van den Brule, F. et al

in Oncogene (2004), 23(45), 7527-7536

Galectin-3, a multifunctional lectin, is involved during cancer progression. Previous observations showed that both cytosolic expression and nuclear exclusion of galectin-3 in human prostate cancer cells ... [more ▼]

Galectin-3, a multifunctional lectin, is involved during cancer progression. Previous observations showed that both cytosolic expression and nuclear exclusion of galectin-3 in human prostate cancer cells were associated to progression of the disease. In this study, we examined the biological roles of galectin-3 when expressed either in the nucleus or in the cytosol. LNCaP, a galectin-3-negative human prostate cancer cell line, was used to generate transfectants expressing galectin-3 either in the nucleus or in the cytosol. No changes in cell morphology, proliferation, attachment to laminin-1 or androgen dependency were observed. Cytoplasmic galectin-3 induced significantly increased Matrigel invasion, anchorage-independent growth and in vivo tumor growth and angiogenesis, and decreased inducible apoptosis. Surprisingly, nuclear galectin-3 affected these parameters in an opposite fashion with an overall antitumoral activity. Thus, our study demonstrates that galectin-3 exerts opposite biological activities according to its cellular localization: nuclear galectin-3 plays antitumor functions and cytoplasmic galectin-3 promotes tumor progression. [less ▲]

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See detailExpression of histone deacetylase 8, a class I histone deacetylase, is restricted to cells showing smooth muscle differentiation in normal human tissues
Waltregny, David ULg; de Leval, Laurence ULg; Glenisson, Wendy et al

in American Journal of Pathology (2004), 165(2), 553-564

Histone deacetylases (HDACs) were originally identified as nuclear enzymes involved in gene transcription regulation. Until recently, it was thought that their activity was restricted within the nucleus ... [more ▼]

Histone deacetylases (HDACs) were originally identified as nuclear enzymes involved in gene transcription regulation. Until recently, it was thought that their activity was restricted within the nucleus, with histones as unique substrates. The demonstration that specific HDACs deacetylate nonhistone proteins, such as p53 and alpha-tubulin, broadened the field of activity of these enzymes. HDAC8, a class I HDAC, is considered to be ubiquitously expressed, as suggested by results of Northern blots performed on tissue RNA extracts, and transfection experiments using various cell lines have indicated that this enzyme may display a prominent nuclear localization. Using immunohistochemistry, we unexpectedly found that, in normal human tissues, HDAC8 is exclusively expressed by cells showing smooth muscle differentiation, including visceral and vascular smooth muscle cells, myoepithelial cells, and myofibroblasts, and is mainly detected in their cytosol. These findings were confirmed in vitro by nucleo-cytoplasmic fractionation and immunoblot experiments performed on human primary smooth muscle cells, and by the cytosolic detection of epitope-tagged HDAC8 overexpressed in fibroblasts. Immunocytochemistry strongly suggested a cytoskeleton-like distribution of the enzyme. Further double-immunofluorescence staining experiments coupled with confocal microscopy analysis showed that epitope-tagged HDAC8 overexpressed in murine fibroblasts formed cytoplasmic stress fiber-like structures that co-localized with the smooth muscle cytoskeleton protein smooth muscle alpha-actin. Our works represent the first demonstration of the restricted expression of a class I HDAC to a specific cell type and indicate that HDAC8, besides being a novel marker of smooth muscle differentiation, may play a role in the biology of these contractile cells. [less ▲]

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