References of "Castronovo, Vincenzo"
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See detailLe tamoxifene comme premier traitement du cancer du sein chez la femme âgée: un recul de 10 ans
Colin, Claude ULg; Lifrange, Eric ULg; Genicot, F. et al

in Revue Médicale de Liège (1990), 45(11), 533-8

Cinquante-six patientes, âgées de plus de 70 ans, ont été traitées par tamoxifène pour cancer mammaire T1 à T4. Un délai de 3 à 6 mois est nécessaire pour obtenir une régression de l'opacité tumorale dans ... [more ▼]

Cinquante-six patientes, âgées de plus de 70 ans, ont été traitées par tamoxifène pour cancer mammaire T1 à T4. Un délai de 3 à 6 mois est nécessaire pour obtenir une régression de l'opacité tumorale dans 46,4% des cas, une stabilisation dans 30,4% et une augmentation dans 23,2%. Le type de réponse semble indépendant du stade initial de la tumeur. La survie globale à 10 ans n'est pas différente de cette des patientes de même âge qui avaient préféré recourir au traitement loco-régional classique. Par contre, en cas de régression tumorale, la durée de la survie est nettement plus longue et est comparable à celle d'une population témoin de même âge. Les récidives locales sont fréquentes. Elle sont de moins bon pronostic si elles surviennent au cours des trois premières années du traitement. La véritable cause du décès est souvent difficile à préciser chez ces patientes. Une relation directe avec le cancer mammaire n'est observée que dans la moitié des cas. [less ▲]

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See detailSpatiotemporal segregation of endothelial cell integrin and nonintegrin extracellular matrix-binding proteins during adhesion events.
Basson, C. T.; Knowles, W. J.; Bell, L. et al

in Journal of Cell Biology (1990), 110(3), 789-801

Bovine aortic endothelial cell (BAEC) attachments to laminin, fibronectin, and fibrinogen are inhibited by soluble arginine-glycine-aspartate (RGD)-containing peptides, and YGRGDSP activity is responsive ... [more ▼]

Bovine aortic endothelial cell (BAEC) attachments to laminin, fibronectin, and fibrinogen are inhibited by soluble arginine-glycine-aspartate (RGD)-containing peptides, and YGRGDSP activity is responsive to titration of either soluble peptide or matrix protein. To assess the presence of RGD-dependent receptors, immunoprecipitation and immunoblotting studies were conducted and demonstrated integrin beta 1, beta 3, and associated alpha subunits as well as a beta 1 precursor. Immunofluorescence of BAECs plated on laminin, fibronectin, and fibrinogen reveals different matrix-binding specificities of each of these integrin subclasses. By 1 h after plating, organization of beta 1 integrin into fibrillar streaks is influenced by laminin and fibronectin, whereas beta 3 integrin punctate organization is influenced by fibrinogen and the integrin spatial distribution changes with time in culture. In contrast, the nonintegrin laminin-binding protein LB69 only organizes after cell-substrate contact is well established several hours after plating. Migration of BAECs is also mediated by both integrin and nonintegrin matrix-binding proteins. Specifically, BAEC migration on laminin is remarkably sensitive to RGD peptide inhibition, and, in its presence, beta 1 integrin organization dissipates and reorganizes into perinuclear vesicles. However, RGD peptides do not alter LB69 linear organization during migration. Similarly, agents that block LB69--e.g., antibodies to LB69 as well as YIGSR-NH2 peptide--do not inhibit attachment of nonmotile BAECs to laminin. However, both anti-LB69 and YIGSR-NH2 inhibit late adhesive events such as spreading. Accordingly, we propose that integrin and nonintegrin extracellular matrix-binding protein organizations in BAECs are both temporally and spatially segregated during attachment processes. High affinity nonintegrin interaction with matrix may create necessary stable contacts for longterm attachment, while lower affinity integrins may be important for initial cell adhesion as well as for transient contacts of motile BAECs. [less ▲]

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See detailLaminin and fibronectin increase the steady state level of the 67 kD high affinity metastasis-associated laminin receptor mRNA in human cancer cells.
Castronovo, Vincenzo ULg; Sobel, M. E.

in Biochemical and Biophysical Research Communications (1990), 168(3), 1110-7

Among the various known laminin binding proteins, the 67 kD high affinity laminin receptor (LR) is intimately involved during tumor invasion and metastasis. In this study, we report that laminin and ... [more ▼]

Among the various known laminin binding proteins, the 67 kD high affinity laminin receptor (LR) is intimately involved during tumor invasion and metastasis. In this study, we report that laminin and fibronectin, two attachment glycoproteins, significantly increased the total cellular level of 67 kD LR mRNA in two human cancer cell lines, T47D breast carcinoma cells and A2058 melanoma cells. Neither GRGDS nor YIGSR synthetic peptides induced such a stimulatory effect. Since the steady state level of LR mRNA has been shown to control the number of receptors expressed at the cell surface, these results suggest that contact of the cancer cells with laminin and fibronectin in the host matrix may be an important regulatory mechanism by which cancer cells maintain a high number of LR at their cell surface as they progress through the several steps of tumoral invasion and metastasis. [less ▲]

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See detailImmunodetection of the metastasis-associated laminin receptor in human breast cancer cells obtained by fine-needle aspiration biopsy.
Castronovo, Vincenzo ULg; Colin, Claude; Claysmith, A. P. et al

in American Journal of Pathology (1990), 137(6), 1373-81

Fine-needle aspiration biopsy of the breast is a very useful technique for the evaluation of a suspect lesion before surgical removal. Increased expression of the 67-kd laminin receptor has been ... [more ▼]

Fine-needle aspiration biopsy of the breast is a very useful technique for the evaluation of a suspect lesion before surgical removal. Increased expression of the 67-kd laminin receptor has been associated with the metastatic phenotype of cancer cells, particularly in colon and breast cancers. In this study, the expression of laminin receptor was evaluated using the immunoperoxidase technique in 81 breast aspirates (26 benign and 55 neoplastic lesions). Cells obtained from benign samples exhibited a low level of laminin receptor antigen detected by affinity-purified antibody raised against a cDNA-derived laminin receptor peptide. In contrast, 71% of smears obtained from malignant breast lesions contained cells that were strongly stained by the antibody. Heterogeneous expression of the laminin receptor was noted in both breast aspirates and fixed tissue specimens. These data suggest that the immunodetection of laminin receptor in cells obtained by fine-needle aspiration of breast lesions could be a valuable adjunct in the prognostic evaluation of breast lesions. [less ▲]

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See detailPossible Role of Human Natural Anti-Gal Antibodies in the Natural Antitumor Defense System
Castronovo, Vincenzo ULg; Colin, Claude ULg; Parent, B. et al

in Journal of the National Cancer Institute (1989), 81(3), 212-6

Expression of Gal alpha 1-3Gal cell surface residues has been correlated with the metastatic potential of murine tumor cells. We report that Gal alpha 1-3Gal residues are expressed at the cell surface of ... [more ▼]

Expression of Gal alpha 1-3Gal cell surface residues has been correlated with the metastatic potential of murine tumor cells. We report that Gal alpha 1-3Gal residues are expressed at the cell surface of malignant human cancer cells, including four cell lines and 50% of the malignant breast specimens obtained by aspiration biopsy. In contrast, all benign breast biopsies and normal cells were Gal alpha 1-3Gal negative. Affinity-purified anti-alpha-galactosyl IgG (anti-Gal) antibody, which specifically recognizes Gal alpha 1-3Gal residues, significantly inhibited cell attachment in two in vitro assays thought to indicate tumor cell extravasation of the circulatory system during the metastatic process: attachment to perfused human umbilical vein endothelium, and attachment to isolated laminin. Since anti-Gal antibody is a natural component of all human sera, we propose that it may be part of the natural antitumor defense system in humans. [less ▲]

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See detailAnti-laminin receptor antibody targeting of liposomes with encapsulated doxorubicin to human breast cancer cells in vitro.
Rahman, A.; Panneerselvam, M.; Guirguis, R. et al

in Journal of the National Cancer Institute (1989), 81(23), 1794-800

The tumor cell laminin receptor is a cell-surface protein that binds laminin with high affinity (Kd = 1.0 nM). The putative ligand-binding domain of the laminin receptor has been molecularly cloned and ... [more ▼]

The tumor cell laminin receptor is a cell-surface protein that binds laminin with high affinity (Kd = 1.0 nM). The putative ligand-binding domain of the laminin receptor has been molecularly cloned and sequenced. In the present study, we used the predicted amino acid sequence of the laminin receptor to generate synthetic peptide antigens and produced immunoglobulin M (IgM) anti-laminin receptor monoclonal antibodies. The disulfide bond group of the IgM molecule was used to couple the antibodies to the surface of liposomes encapsulating doxorubicin. The anti-laminin receptor monoclonal antibodies coupled to the liposomes bound avidly to the surface of MDA-MB-435S (MDA-435) human breast carcinoma cells, which have high numbers of laminin receptors. These antibody-coupled liposomes exhibited a low degree of binding to Hs 578Bst (Hs 578) normal human breast epithelial cells, which express a low number of laminin receptors. Excess liposomes competed for the binding of unbound laminin to the tumor cell surface, and excess laminin competed for binding with the liposomes. Antibody-coupled liposomes encapsulating doxorubicin were specifically more efficient in inhibiting colony formation by MDA-435 cells in vitro than unbound doxorubicin or liposomes without anti-laminin receptor monoclonal antibodies. Unbound doxorubicin inhibited thymidine uptake by 10%-20% in both Hs 578 and MDA-435 cells, whereas the antibody-coupled liposomes encapsulating doxorubicin inhibited thymidine uptake by 90% in MDA-435 cells but only 15% in Hs 578 cells. Thus, use of anti-laminin receptor monoclonal antibodies coupled with liposomes encapsulating doxorubicin represents a new strategy for selective targeting of doxorubicin to carcinoma cells with exposed laminin receptors. [less ▲]

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See detailModulation of laminin receptor expression by estrogen and progestins in human breast cancer cell lines.
Castronovo, Vincenzo ULg; Taraboletti, G.; Liotta, L. A. et al

in Journal of the National Cancer Institute (1989), 81(10), 781-8

The effects of estradiol and two synthetic progestins (ORG2058 and R5020) on the expression of the high-affinity, metastasis-associated laminin receptor in two human breast carcinoma cell lines were ... [more ▼]

The effects of estradiol and two synthetic progestins (ORG2058 and R5020) on the expression of the high-affinity, metastasis-associated laminin receptor in two human breast carcinoma cell lines were examined. The T47D cell line contains estrogen and progesterone receptors, but the MDA-MB 231 cell line lacks both receptors. Treatment of T47D cells with 10(-9) M estradiol alone results in a three-fold increase (P less than or equal to .05) in the steady-state level of laminin receptor mRNA determined by RNA blot analysis as well as in cell-surface, laminin receptor expression that is evaluated by immunofluorescence. No effects of estradiol on the receptor-negative MDA-MB 231 cells were observed. Untreated and steroid-treated MDA-MB 231 cells had higher levels of laminin receptor mRNA than did untreated or estradiol-treated T47D cells. A more dramatic increase (five-fold; P less than or equal to .005) of mRNA and cell-surface expression in T47D cells was observed after treatment with estradiol plus 10(-8) M progestin or with progestin alone. Estradiol treatment also increased chemotaxis and haptotaxis of T47D cells but not of MDA-MB 231 cells to laminin; it had no effect on the attachment of these latter cells to laminin. Interestingly, treatment with estradiol plus progestin or progestin alone significantly increased the attachment of T47D cells to laminin but did not have an effect on either haptotaxis or chemotaxis to laminin. These results suggest that the various cell-laminin interactions are mediated by different mechanisms. The augmentation of laminin receptor mRNA by estrogen and progesterone treatment in hormone receptor-positive cells, but not in cells that lack these receptors, may relate functionally to the difference in the clinical aggressiveness between classes of breast cancers. [less ▲]

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See detailEvidence for a precursor of the high-affinity metastasis-associated murine laminin receptor.
Rao, C. N.; Castronovo, Vincenzo ULg; Schmitt, M. C. et al

in Biochemistry (1989), 28(18), 7476-86

The high-affinity cellular receptor for the basement membrane component laminin is differentially expressed during tumor invasion and metastasis. A cDNA clone encoding the murine laminin receptor was ... [more ▼]

The high-affinity cellular receptor for the basement membrane component laminin is differentially expressed during tumor invasion and metastasis. A cDNA clone encoding the murine laminin receptor was isolated and identified on the basis of sequence homology to the human laminin receptor [Wewer et al. (1986) Proc. Natl. Acad. Sci. U.S.A. 83, 7137-7141]. Primer extension experiments demonstrated that the clone contained the complete 5' sequence of the murine laminin receptor mRNA. RNA blot data demonstrated a single-sized laminin receptor mRNA, approximately 1400 bases long, in human, mouse, and rat. The nascent laminin receptor predicted from the cDNA sequence is 295 amino acids long, with a molecular weight of 33,000, and contains one intradisulfide bridge, a short putative transmembrane domain, and an extracellular carboxy-terminal region which has abundant glutamic acid residues and multiple repeat sequences. The precursor of the laminin receptor is apparently smaller than the 67-kilodalton protein isolated from tissue. The apparent molecular weight on SDS-polyacrylamide gels of the rabbit reticulocyte cell-free translation product of selectively hybridized laminin receptor mRNA is 37,000. Antisera to three different domains of the cDNA-predicted receptor were used to study the relationship between the 37- and 67-kilodalton polypeptides. Antisera to cDNA-deduced synthetic peptides of the receptor immunoprecipitated a 37-kilodalton band both from cell-free translation products and from pulse-labeled cell extracts. On immunoblots of cell extracts, one antisynthetic peptide antiserum recognized only the 67-kilodalton receptor, while another antiserum identified both 37- and 67-kilodalton polypeptides, suggesting a precursor-product relationship between the two polypeptides. [less ▲]

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See detailReactivity of human anti-alpha-galactosyl IgG antibody with alpha(1-->3)-linked galactosyl epitopes exposed on basement membranes and on glomerular epithelial cells: an in vitro and in vivo study in the mouse.
Vecchi, M. L.; Davin, J. C.; Castronovo, Vincenzo ULg et al

in Clinical & Experimental Immunology (1989), 78(2), 271-7

Anti-alpha-galactosyl antibody (a-Gal Ab) is a human natural antibody belonging to the IgG class, found in high titres in all normal sera regardless of blood group, and specifically recognizing alpha (1 ... [more ▼]

Anti-alpha-galactosyl antibody (a-Gal Ab) is a human natural antibody belonging to the IgG class, found in high titres in all normal sera regardless of blood group, and specifically recognizing alpha (1-->3)-linked galactosyl residues. We have observed by radioimmunoassay, ELISA, passive haemagglutination and immunofluorescence blocking studies that affinity-purified a-Gal Ab reacted with mouse laminin, but not with the other mouse basement membrane proteins tested; it was able to fix complement in vitro. When injected intravenously into mice, the a-Gal Ab was found to mainly accumulate in kidneys, liver, spleen and lungs. No acute respiratory distress syndrome was observed shortly after the i.v. injection of 100 or 200 microg of antibodies. These doses of a-Gal Ab were also unable to induce acute glomerular injury. However, in primary cultures, the a-Gal Ab (100 or 200 microg per ml of medium) was shown to impair the attachment of mouse glomerular epithelial cells to mouse laminin and to elicit complement-dependent cell damage. The data indicate that the a-Gal Ab can interact in vitro and/or in vivo with alpha (1-->3)-linked galactosyl residues exposed on murine laminin or on murine cultured glomerular epithelial cells. Although this antibody fails to be pathogenic when administered at low doses in the intact animal, similar doses can alter some metabolic properties of these cells in vitro. [less ▲]

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See detailInteractions of invasive cells with native and modified extracellular matrix in vitro.
Bracke, M.; Castronovo, Vincenzo ULg; De Bruyne, G. et al

in Advances in Experimental Medicine and Biology (1988), 233

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See detailFlavonoids inhibit malignant tumor invasion in vitro.
Bracke, M. E.; De Pestel, G.; Castronovo, Vincenzo ULg et al

in Progress in Clinical & Biological Research (1988), 280

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See detailInteractions of invasive cells with native and modified extracellular matrix in vitro.
Bracke, M.; Castronovo, Vincenzo ULg; De Bruyne, G. et al

in Advances in Experimental Medicine and Biology (1988), 233

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See detailPerfusion of Human Umbilical Veins. A New Approach to Study the Interactions of Circulating Malignant Cells with Vascular Wall and Their Modulations
Castronovo, Vincenzo ULg; Parent, B.; Foidart, Jean-Michel ULg et al

in Invasion & Metastasis (1988), 8(6), 332-50

Interactions of malignant or non-malignant human and rodent cells with the vascular wall were studied using perfused human umbilical cord veins. The integrity of perfused endothelium was confirmed by ... [more ▼]

Interactions of malignant or non-malignant human and rodent cells with the vascular wall were studied using perfused human umbilical cord veins. The integrity of perfused endothelium was confirmed by morphological and functional criteria. Highly malignant cells in vivo adhered to the endothelial cells, as shown by scanning electron microscopy. The specific attachment of radiolabelled malignant cells to the whole vein was already maximal within 30-60 min and remained stable for perfusion flow rates ranging between 10 and 60 ml/min. It increased proportionally to the number of cells infused and could be modulated by human platelets, human fibronectin and rabbit anti-laminin antibodies. In contrast, the binding of human or rodent non-malignant cells in vivo, of human red blood cells and of human platelets to the endothelial cells was negligible under similar experimental conditions. This perfusion system therefore represents a new model for elucidating some mechanisms involved in tumour cell arrest in vivo. [less ▲]

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See detailInteractions of invasive cells with native and modified extracellular matrix in vitro.
Bracke, M.; Castronovo, Vincenzo ULg; De Bruyne, G. et al

in In Prodi, G.; Liotta, L. A.; Lollini, P. L. (Eds.) et al Cancer Metastasis : Biological and Biochemical Mechanisms and Clinical Aspects. (1988)

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See detailThe anti-invasive flavonoid (+)-catechin binds to laminin and abrogates the effect of laminin on cell morphology and adhesion
Bracke, M. E.; Castronovo, Vincenzo ULg; Van Cauwenberge, R. M. et al

in Experimental Cell Research (1987), 173(1), 193-205

To study the effect of the flavonoid (+)-catechin on cell-matrix interactions two cell types with a different morphology on and adhesion to laminin were used. MO4 virally transformed fetal mouse cells ... [more ▼]

To study the effect of the flavonoid (+)-catechin on cell-matrix interactions two cell types with a different morphology on and adhesion to laminin were used. MO4 virally transformed fetal mouse cells adhere and spread when cultured on top of laminin-coated coverslips or on human amnion basement membrane. M5076 mouse reticulum cell sarcoma cells poorly adhere to these substrates and remain round. Both cell types are invasive in confronting cultures with embryonic chick heart fragments. (+)-Catechin binds to laminin in a pH-dependent way. Pretreatment of laminin-coated coverslips or amnion basement membrane with 0.5 mM (+)-catechin abrogates the effect of laminin on cell morphology and adhesion. MO4 cells do not adhere to the pretreated substrates and remain round, while M5076 cells now adhere and spread. (+)-Catechin inhibits the invasion of MO4 cells but not of M5076 cells into embryonic chick heart in vitro. We speculate that the anti-invasive activity of the flavonoid to MO4 cells is the result of its interference with MO4 cell adhesion to laminin. Invasion of M5076 cells does not imply adhesion to and spreading on laminin. [less ▲]

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See detailInteractions between fibroblasts and a reconstituted basement membrane matrix
Emonard, H.; Calle, A.; Grimaud, J. A. et al

in Journal of Investigative Dermatology (1987), 89

A gel-like reconstituted basement membrane matrix containing type IV collagen, laminin, entactin, nidogen, and heparan sulfate proteoglycan was used to examine the interactions between normal calf skin ... [more ▼]

A gel-like reconstituted basement membrane matrix containing type IV collagen, laminin, entactin, nidogen, and heparan sulfate proteoglycan was used to examine the interactions between normal calf skin fibroblasts and basement membranes. Within 6 h after seeding, fibroblasts initiated a migration that resulted in the formation of a cellular network after 1 day of culture on top of the gel. Electron microscopy revealed that fibroblasts were able to remodel the basement membrane matrix by penetrating into the gel (from day 3), depositing fibronectin and collagen fibers, and retracting this extracellular matrix. Fibroblasts cultured on the Engelbreth-Holm-Swarm reconstituted basement membrane matrix displayed ultrastructural features characterized by a poor synthetic apparatus (rough endoplasmic reticulum and Golgi vesicles), a large cytoskeleton, and intracytoplasmic vesicles containing laminin. Thus the reconstituted basement membrane matrix is remodeled by skin fibroblasts, and reciprocally their ultrastructural morphologic features are affected by this matrix. [less ▲]

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See detailHuman Anti-Alpha-Galactosyl Igg Reduces the Lung Colonization by Murine Mo4 Cells
Castronovo, Vincenzo ULg; Foidart, Jean-Michel ULg; Li Vecchi, M. et al

in Invasion & Metastasis (1987), 7(6), 325-45

The lung colonization of MO4 cells, a highly malignant murine cell line, is strongly reduced in syngeneic C3H/He mice by a prior incubation with anti-alpha-galactosyl antibody (alpha-Gal Ab), a natural ... [more ▼]

The lung colonization of MO4 cells, a highly malignant murine cell line, is strongly reduced in syngeneic C3H/He mice by a prior incubation with anti-alpha-galactosyl antibody (alpha-Gal Ab), a natural IgG antibody present in high titers in all normal human sera and specifically recognizing Gal alpha(1----3) structures (alpha-D-galactopyranosyl; alpha-D-Galp). The protective effect is due to a binding of alpha-Gal Ab to alpha-D-Galp end groups of MO4 cells, inducing both an increase in their sequestration into the liver and the spleen and a decrease in their sequestration into the lung. The F(ab')2 fragments of this antibody also exhibit a protective effect by inhibiting the homing of MO4 cells into the lung, without modifying their accumulation into the spleen and the liver. Since both the antibody and the alpha-galactosidase pretreatments of MO4 cells block their subsequent attachment to murine laminin in vitro, we suggest that, in this model, the lung colonization may be dependent on the alpha-D-Galp end groups exposed on the surface of MO4 cells. [less ▲]

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See detailFlavonoids : tools for the study of tumor invasion in vitro.
Bracke, M. E.; Van Cauwenberge, Jean-Rémy ULg; Mareel, M. M. et al

in Plant Flavonoids in Biology and Medicine: Biochemical, Pharmacological and Structure-Activity Relationships. (1986)

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See detailFibronectin mediates the retraction of type I collagen fibers by breast cancer cells.
Castronovo, Vincenzo ULg; Paye, M.; Courtois, R. et al

in Evaluation du Risque de Cancer Mammaire. Chimiothérapie Première ? (1985)

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