References of "Castronovo, Vincenzo"
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See detailRetinoic Acid Induces Three Newly Cloned Hoxa1 Transcripts in Mcf7 Breast Cancer Cells
Chariot, Alain ULg; Moreau, Louis; Senterre, Geoffrey et al

in Biochemical and Biophysical Research Communications (1995), 215(2), 713-20

Coordinated expression of genes involved in development, differentiation and malignant transformation is regulated by transcription factors including homeodomain-containing proteins. However, most of ... [more ▼]

Coordinated expression of genes involved in development, differentiation and malignant transformation is regulated by transcription factors including homeodomain-containing proteins. However, most of their cDNA sequences are still unknown. We report here the molecular characterization of three newly cloned HOXA1 transcripts from human breast cancer cells. In addition, we provide evidence that these alternatively spliced transcripts encode one homeodomain-containing protein and two products lacking the conserved DNA-binding domain. Moreover, we demonstrate that all three HOXA1 transcripts are induced by retinoic acid in MCF7 cells. Taken together, our results suggest that HOXA1 gene may be a key element in the establishment of the breast cancer cell phenotype. [less ▲]

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See detailGalectin-1 Modulates Human Melanoma Cell Adhesion to Laminin
van den Brule, F. A.; Buicu, C.; Baldet, M. et al

in Biochemical and Biophysical Research Communications (1995), 209(2), 760-7

Galectins constitute a gene family of beta-galactoside-specific lectins that show high homology in their carbohydrate-binding site. They have been postulated to be involved in many biological events, but ... [more ▼]

Galectins constitute a gene family of beta-galactoside-specific lectins that show high homology in their carbohydrate-binding site. They have been postulated to be involved in many biological events, but their specific functions are not yet well defined. Galectin-1 is a laminin binding protein that recognizes poly-N-acetyllactosamine chains on this major basement membrane glycoprotein. In this study, we analyzed the possibility that galectin-1 could modulate interactions between human melanoma cells and laminin. We demonstrated that A375 and A2058 cell lines express galectin-1 both intracellularly and on the cell surface. In an in vitro assay, recombinant galectin-1 increased melanoma cell attachment to laminin in a dose-dependent manner. This effect was abolished by lactose. Anti-galectin-1 inhibited adhesion of melanoma cells to laminin in a dose-dependent fashion. However, neither galectin-1 nor anti-galectin-1 antibody affected melanoma cell spreading on laminin in vitro. These data indicate that galectin-1 might participate in melanoma cell adhesion to laminin and therefore could be a modulator of invasion and metastasis. [less ▲]

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See detailSimulation of Human B-Lymphocyte Proliferation by Agm-1470, a Potent Inhibitor of Angiogenesis
Antoine, Nadine ULg; Bours, Vincent ULg; Heinen, Ernst ULg et al

in Journal of the National Cancer Institute (1995), 87(2), 136-9

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See detailIncreased Expression of Osteonectin and Osteopontin, Two Bone Matrix Proteins, in Human Breast Cancer
Bellahcene, Akeila ULg; Castronovo, Vincenzo ULg

in American Journal of Pathology (1995), 146(1), 95-100

Microcalcifications are a common phenomenon associated with breast cancer and are often the only mammographic sign of a malignant breast disease. Although microcalcifications are not restricted to breast ... [more ▼]

Microcalcifications are a common phenomenon associated with breast cancer and are often the only mammographic sign of a malignant breast disease. Although microcalcifications are not restricted to breast cancer and can be also associated with benign lesions, it is noteworthy that they are composed exclusively of hydroxyapatite in breast carcinoma. Hydroxyapatite is the bone-associated phosphocalcic crystal the deposition of which in bone tissue requires the coordinated expression of several molecules such as osteonectin (OSN) and osteopontin (OPN), synthesized by cells of the osteoblastic lineage. In this study, we evaluated the expression of these two bone matrix proteins, using an immunoperoxidase technique and specific antibodies, in 79 breast lesions including 28 benign and 51 cancerous specimens. We found that normal mammary tissue associated with the lesions examined expressed generally undetectable or lightly detectable (0 or 1+) amounts of OSN and OPN (92 and 81%, respectively). Benign breast lesions, including fibroadenoma and fibrocystic dysplasia, were generally weakly stained (0 or 1+) with both anti-OSN and anti-OPN antibodies (96.4 and 60.7%, respectively). Interestingly, the majority of both in situ and invasive breast carcinoma lesions showed a strong expression (2+ or 3+) for OSN or OPN (74.5 and 84.3%, respectively). High expression of these two bone matrix proteins was associated with frequent microcalcification deposition in the lesion. This study is the first extensive study of OSN and OPN expression in mammary cancers. Our data suggest that OSN and OPN could play a role in the formation of ectopic microcalcifications often associated with breast cancer. It is also tempting to speculate that the expression of these two glycoproteins by breast cancer cells play a role in the preferred bone homing of breast metastases. [less ▲]

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See detailTamoxifen and its active metabolite inhibit growth of estrogen receptor-negative MDA-MB-435 cells
Charlier, Corinne ULg; Chariot, Alain ULg; Antoine, Nadine ULg et al

in Biochemical Pharmacology (1995), 49

Tamoxifen (TAM), the non-steroidal anti-estrogen most widely administered to breast cancer patients, acts, at least in part, by competing with estrogen receptors (ER). However, the existence of an ... [more ▼]

Tamoxifen (TAM), the non-steroidal anti-estrogen most widely administered to breast cancer patients, acts, at least in part, by competing with estrogen receptors (ER). However, the existence of an alternative mechanism of action for this drug is supported by the clinical observations that: (a) 30% of patients with ER-negative cancer cells respond to TAM, and (b) 30% of patients with ER-positive cancer cells are not sensitive to this anti-estrogen. In this study, we observed that growth of the human ER-negative breast cancer cell line MDA-MB-435 was inhibited by TAM and 4-hydroxytamoxifen (4OH-TAM) in a concentration-dependent fashion. Both monoclonal enzymoimmunoassay and Dextran Charcoal Coated Scatchard radioimmunoassay analysis demonstrated that this MDA-MB-435 cell line does not express ER. The absence of ER in MDA-MB-435 cells was also demonstrated at the mRNA level by both northern blot hybridization and reverse transcription-polymerase chain reaction techniques. MDA-MB-435 cell proliferation was not affected by 17 beta-estradiol or by the pure anti-estrogen ICI 164384, further demonstrating that the observed effects of TAM and its active metabolite on the proliferation of MDA-MB-435 cells were due to an ER-independent mechanism, yet to be identified. MDA-MB-435 thus appears to be a promising original model for the study of the alternative ER-independent mechanisms of action of TAM. [less ▲]

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See detailExpression of the monomeric 67-kd laminin-binding protein in human lymphomas as defined by MLuC5 monoclonal antibody and paraffin section immunohistochemistry.
Carbone, A.; Gloghini, A.; Colombatti, A. et al

in Human Pathology (1995), 26(5), 541-6

Interactions between cancer cells and laminin, a major component of basement membranes, are mediated through a large variety of cell surface proteins designated as laminin receptors. Among the above ... [more ▼]

Interactions between cancer cells and laminin, a major component of basement membranes, are mediated through a large variety of cell surface proteins designated as laminin receptors. Among the above proteins, a 67-kd monomeric high affinity laminin receptor (67 LR) has long been suspected to be involved in tumor progression. In this study we wished to establish whether the 67 LR molecule is detectable on tumor cells of Hodgkin's disease (HD) and non-Hodgkin's lymphomas (NHLs), to define its pattern of expression, and to assess the potential utility of 67 LR in differentiating these pathological entities. Morphological and immunohistological studies were performed on 85 specimens of HD and a series of 334 NHL specimens, including anaplastic large cell (ALC) (CD30-positive) lymphomas (73 specimens). For immunohistochemical assessment of the 67 LR we used the monoclonal antibody (MoAb) MLuC5 directed against the 67-kd laminin receptor on paraffin-embedded sections. Reed-Sternberg cells reacted with MLuC5 MoAb in four of 85 (4.7%) HD specimens. Among the NHL specimens, a MLuC5-positive reaction was expressed in 3.3% of B-cell lymphomas. They all belonged to the high grade subtypes. On the other hand, a MLuC5-positive reaction was detected in none of the T-cell lymphomas tested. In contrast to the results obtained with the other NHLs, in 30.2% of ALC (CD30-positive) lymphoma specimens, tumor cells reacted with MLuC5 MoAb. MLuC5-expressing ALC (CD30-positive) lymphoma cells were of either T-cell (six of 17 specimens), B-cell (three of 25 specimens), or undetermined phenotype (10 of 31 specimens). Our investigation has shown that 67 LR as shown by MLuC5 MoAb is detectable only in neoplastic cells of a fraction of ALC (CD30-positive) lymphomas and small subsets of B-cell high grade NHLs and HD. The restricted expression of the 67 LR molecule to ALC (CD30-positive) lymphomas provides a potential tool for the phenotypic separation of this pathological entity from HD and other lymphomas. Whether the detection of the 67 LR expression in these lymphoma subsets may be related to the aggressiveness of the disease remains to be ascertained. [less ▲]

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See detailCancers épithéliaux de l'ovaire. Acquisitions récentes
van den Brule, F. A.; Lambotte, René ULg; Castronovo, Vincenzo ULg

in Journal de Gynécologie, Obstétrique et Biologie de la Reproduction (1995), 24(3), 241-52

Ovarian carcinomas constitute the major cause of the mortality and morbidity in gynaecology. Most ovary carcinomas are epithelial tumours. Our understanding of ovarian cancerogenesis has been hampered by ... [more ▼]

Ovarian carcinomas constitute the major cause of the mortality and morbidity in gynaecology. Most ovary carcinomas are epithelial tumours. Our understanding of ovarian cancerogenesis has been hampered by the lack of a well defined precursor lesion, the lack of knowledge about tumour progression, and by the relative inaccessibility of the ovaries in the abdominal cavity. Recent studies using experimental models allow us to better define the fundamental mechanisms of carcinogenesis from the serous ovarian cells and of invasion of the abdominopelvic cavity by proximity. This review article tries to update on epidemiology, genetic syndromes, biology, screening, and therapy of these epithelial tumours, and about the new directions taken by basic and clinical research. We will present data concerning oncogenes and tumour suppressor genes involved in epithelial ovarian tumours, regulation of tumour cells by growth factors, genes involved in tumour invasion, and mechanisms used by the cancer cell to resist to therapies. Non-epithelial ovarian tumours will not be examined in this manuscript. [less ▲]

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See detailGalectin-3, a Laminin Binding Protein, Fails to Modulate Adhesion of Human Melanoma Cells to Laminin
van den Brule, F. A.; Buicu, C.; Sobel, M. E. et al

in Neoplasma (1995), 42(5), 215-9

Galectin-3 is a laminin binding protein which expression is altered in a variety of human carcinomas including colon, breast and endometrium. In these tumors, we consistently observed a down regulation of ... [more ▼]

Galectin-3 is a laminin binding protein which expression is altered in a variety of human carcinomas including colon, breast and endometrium. In these tumors, we consistently observed a down regulation of galectin-3 expression related to increased aggressiveness. Galectin-3 belongs to a family of galactose-binding lectins and binds laminin through its numerous poly-N-acetyllactosamine chains. To date, the exact role of galectin-3 in the complex interactions between cancer cells and laminin has not been clearly defined. Adhesion of melanoma cells to laminin is a critical event during tumor invasion and metastasis. In this study, we explore the possibility that galectin-3 could modulate attachment of two human melanoma cell lines to laminin. A2058 and A375 melanoma cell expressed galectin-3 on their surface as demonstrated by immunofluorescence, and attached to laminin in an in vitro assay. We demonstrate that neither recombinant galectin-3 nor an affinity purified antigalectin-3 antiserum altered adhesion of A2058 or A375 melanoma cells to laminin. Our data strongly suggest that galectin-3 is not a key element in adhesion of the melanoma cells to laminin. These results are not surprising in light of the observation that galectin-3 expression is down regulated in cancer and that increased adhesion to laminin is a constant feature of invasive cancer cells. [less ▲]

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See detailDepressed Immune Surveillance against Cancer: Role of Deficient T Cell: Extracellular Matrix Interactions
Gorski, A.; Castronovo, Vincenzo ULg; Stepien-Sopniewska, B. et al

in Cell Adhesion and Communication (1994), 2(3), 225-33

Although T cells infiltrate malignant tumors, the local immune response is usually inefficient and tumors escape destruction. While extracellular matrix proteins strongly costimulate T cell responses in ... [more ▼]

Although T cells infiltrate malignant tumors, the local immune response is usually inefficient and tumors escape destruction. While extracellular matrix proteins strongly costimulate T cell responses in normal individuals, our studies indicate that peripheral blood T cells from cancer patients and tumor infiltrating cells respond poorly or are resistant to stimulative signals mediated by collagen I and IV and fibronectin. Moreover, the adhesive properties of cancer T cells are markedly depressed. Those functional deficiencies are paralleled by variable deficits in integrin and non-integrin T cell receptors for extracellular matrix. Immunotherapy with BCG causes a dramatic but transient increase in T cell: ECM interactions. [less ▲]

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See detailExpression of Bone Sialoprotein, a Bone Matrix Protein, in Human Breast Cancer
Bellahcene, Akeila ULg; Merville, Marie-Paule ULg; Castronovo, Vincenzo ULg

in Cancer Research (1994), 54(11), 2823-6

Microcalcifications are often associated with human mammary lesions, particularly with breast carcinomas. To date, the molecular mechanism that leads to the deposition of hydroxyapatite in the mammary ... [more ▼]

Microcalcifications are often associated with human mammary lesions, particularly with breast carcinomas. To date, the molecular mechanism that leads to the deposition of hydroxyapatite in the mammary tissue has not been elucidated. Bone sialoprotein (BSP) is a glycoprotein the expression of which coincides with the appearance of the first hydroxyapatite crystals during bone development. In this study, we report the observation that BSP, a bone matrix protein, is expressed in human mammary cancer cells. Using an immunoperoxidase technique, we studied the expression of BSP in 79 breast lesions, including 28 benign and 51 malignant specimens. Two polyclonal antibodies, one directed against intact human BSP and the other against a synthetic peptide of BSP (residues 277-294), were used and gave identical results. Normal mammary glands expressed undetectable or barely detectable amounts of BSP, and the majority of the benign lesions examined were generally unstained (0) or weakly stained (1+). Most of the breast carcinoma specimens (around 87%) showed a significant increase (P = 0.0001) in BSP expression. Breast carcinomas with microcalcifications had the highest immunoreactivity (2+ or 3+) to BSP antibodies. This is the first demonstration that BSP expression is significantly increased in breast cancer. Expression of BSP by breast cancer cells could play a major role in the deposition of microcalcifications and in the preferred bone homing of breast cancer cells. [less ▲]

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See detailInverse Expression of Two Laminin Binding Proteins, 67lr and Galectin-3, Correlates with the Invasive Phenotype of Trophoblastic Tissue
van den Brule, F. A.; Price, J.; Sobel, M. E. et al

in Biochemical and Biophysical Research Communications (1994), 201(1), 388-93

Tumor invasion of host tissues and trophoblastic penetration of the endometrium share common biological features. Both processes involve the invasion of basement membranes, an event that is initiated by ... [more ▼]

Tumor invasion of host tissues and trophoblastic penetration of the endometrium share common biological features. Both processes involve the invasion of basement membranes, an event that is initiated by adhesion of cancer or trophoblast cells to basement membrane components and particularly to laminin. Adhesion to this latter glycoprotein is mediated through a variety of cell surface receptors. We have previously shown that the 67 kD Laminin Receptor (67LR) and a 31 kD Human Laminin Binding Protein, recently renamed galectin-3, are inversely modulated as the invasive phenotype of cancer cells progresses, with up regulation of the former, and down regulation of the latter, respectively. In this study, we examined the expression of these two proteins in 27 human trophoblastic specimens at different gestational ages using Northern and Western blot techniques. Expression of the 67LR increased from 7 weeks to a maximum at 12 weeks, when invasion is maximal, and then decreased. Expression of galectin-3 was inversely modulated by the gestational age, with a minimum expression at 12 weeks. Our data demonstrate that invasive trophoblast displays the same pattern of laminin binding proteins expression than invasive cancer cells, and further demonstrates that invasion of the extracellular matrix by trophoblast and cancer cells share common molecular mechanisms. [less ▲]

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See detailLa protéine P53, protectrice de l'intégrité du génome: rôle dans la genèse des cancers
Bellahcene, Akeila ULg; Merville, Marie-Paule ULg; Gielen Jacques et al

in Revue Médicale de Liège (1994), 49(5), 274-84

L'homéostasie des tissus de l'organisme est le résultat d'un équilibre dynamique stable entre des facteurs de régulation positifs et négatifs. Ceux-ci contrôlent la prolifération des cellules et ... [more ▼]

L'homéostasie des tissus de l'organisme est le résultat d'un équilibre dynamique stable entre des facteurs de régulation positifs et négatifs. Ceux-ci contrôlent la prolifération des cellules et déterminent leur appartenance tissulaire. Des données récentes indiquent que l'apparition des cancers résulte du déséquilibre de cet état dynamique soit part l'activation de facteurs positifs désignés sous le terme d'oncogènes, soit par l'inactivation de facteurs négatifs qui sont regroupés dans la famille des gènes suppresseurs de tumeurs. Le gène codant pour la protéine p53 est un membre particulièrement important de cette dernière famille. En effet, son inactivation, par mutation et/ou délétion, est l'une des altérations génétiques la plus fréquemment détectée dans les cancers. La fonction principale attribuée à la protéine p53 consiste à préserver le génome des altérations susceptibles d'entraîner, entre autres, la cellule dans un processus de transformation maligne. C'est en permettant la réparation des altérations du DNA survenues lors de sa réplication avant la mitose ou provoquées par des agents extérieurs, que la protéine p53 semble exercer ses fonctions. Des altérations du gène p53 entraînant des perturbations de la fonction de la protéine p53 ont été identifiées au niveau de la plupart des lésions tumorales malignes. A ce titre, cette protéine semble jouer un rôle déterminant au niveau de la genèse des cancers. Aussi le gène p53 fait-il l'objet de recherches intensives qui devraient déboucher sur la mise au point de nouveaux moyens de détection et d'évaluation pronostique des cancers. D'autre part, des expériences visant à restaurer la fonction de la protéine p53 au niveau des cellules cancéreuses ouvrent de nouvelles et séduisantes perspectives thérapeutiques. [less ▲]

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See detailAgm-1470, a Potent Angiogenesis Inhibitor, Prevents the Entry of Normal but Not Transformed Endothelial Cells into the G1 Phase of the Cell Cycle
Antoine, Nadine ULg; Greimers, Roland ULg; De Roanne, C. et al

in Cancer Research (1994), 54(8), 2073-6

AGM-1470 is a potent angiogenesis inhibitor that is very effective in inhibiting endothelial cell proliferation in both in vitro and in vivo models and that prevents tumor growth in vivo. Although this ... [more ▼]

AGM-1470 is a potent angiogenesis inhibitor that is very effective in inhibiting endothelial cell proliferation in both in vitro and in vivo models and that prevents tumor growth in vivo. Although this molecule appears to be a most promising anticancer drug, its mechanism of action has not yet been elucidated. In this study, we examined the effects of AGM-1470 on the cell cycle of normal and transformed endothelial cells. We showed that AGM-1470, at picomolar concentrations, specifically inhibits the proliferation of both bovine aortic endothelial cells and human umbilical vein endothelial cells. AGM-1470 was ineffective in significantly inhibiting the proliferation of Ea.hy926 cells, a hybrid cell line obtained by the fusion of human umbilical vein endothelial cells with a human carcinoma cell line, or cEnd.1 cells, a polyoma middle T oncogene-transformed endothelioma cell line derived from mouse embryo. Using a double labeling technique with anti-Ki67 antibodies and propidium iodide, we demonstrated, with flow cytometry analysis, that AGM-1470 specifically prevents the entry of endothelial cells into the G1 phase of the cell cycle. We also showed that AGM-1470 was ineffective in inhibiting endothelial cell migration toward laminin or capillary-like tube formation inside a type I collagen matrix induced by phorbol esters. Our data strongly suggest that AGM-1470 is a molecule that specifically inhibits a cell cycle control pathway active in normal cells but which could be bypassed or altered in transformed cells. [less ▲]

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See detailThe Nf-Kappa B Transcription Factor and Cancer: High Expression of Nf-Kappa B- and I Kappa B-Related Proteins in Tumor Cell Lines
Bours, Vincent ULg; Dejardin, Emmanuel ULg; Goujon-Letawe, F. et al

in Biochemical Pharmacology (1994), 47(1), 145-9

NF-kappa B is a pleiotropic transcription factor which controls the expression of many genes and viruses. To date, there is good evidence, but no definitive proof, for its role in tumor formation and ... [more ▼]

NF-kappa B is a pleiotropic transcription factor which controls the expression of many genes and viruses. To date, there is good evidence, but no definitive proof, for its role in tumor formation and development of metastasis. To investigate the possibility that members of the NF-kappa B family could participate in the molecular control of the transformed and invasive phenotype, we examined the expression of these proteins in a variety of human tumor cell lines. The expression of p50, p65, p52 and I kappa B was quantified at the protein level using western immunoblot and mobility shift assay and at the RNA level by northern blot. We observed high expression of the NF-kappa B inhibitor I kappa B in the ovarian carcinoma cell line OVCAR-3 together with constitutive nuclear NF-kappa B activity. We also studied the colon carcinoma cell line HT-29 and its metastatic counterpart HTM-29 and we observed specific expression of the p52 NF-kappa B-related protein in the metastatic cells. Our data confirm that NF-kappa B could be involved in the genesis of a variety of cancers including solid tumors and provide us with interesting models to explore the exact role of these transcription factors in cancer. [less ▲]

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See detailHomeobox Genes: Potential Candidates for the Transcriptional Control of the Transformed and Invasive Phenotype
Castronovo, Vincenzo ULg; Kusaka, Masami; Chariot, Alain ULg et al

in Biochemical Pharmacology (1994), 47(1), 137-43

The transformation of a cell and the acquisition of the invasive and metastatic phenotype result from the activation of a group of complex cellular processes rather than from the effect of a single gene ... [more ▼]

The transformation of a cell and the acquisition of the invasive and metastatic phenotype result from the activation of a group of complex cellular processes rather than from the effect of a single gene product. It is likely that the coordination of the multiple genes involved in malignancy is under the control of a few genes that act as master genes or orchestrator genes. The latter probably code for transcription factors that control the genetic program for tumor invasion and metastasis. Homeobox genes are a family of transcription factors that contain a 183 bp highly conserved nucleotide sequence coding for a 61 amino acid domain that binds specifically to DNA. First discovered in Drosophila as genes controlling segmentation and segment identity, homeobox genes have since been identified in many other species including nematodes, frog, mouse and human. There is strong support for the suggestion that homeobox genes play a key role in development and differentiation. In humans, there are 38 homeobox genes organized in four clusters that are localized on chromosomes 2, 7, 12 and 17. The specific functions of each of these genes are generally unknown. Alterations in expression of several homeobox genes have been reported in a variety of malignant lesions, suggesting that they could play a role in the development of cancer. Using reverse transcriptase reaction coupled with polymerase chain reaction and degenerate oligonucleotides corresponding to the 5' and 3' ends of the highly conserved homeodomain, we amplified 130 bp cDNA fragments from the human breast cancer cell line MCF7 that were subsequently cloned into pBluescript vector. Sequencing of the clones, resulted in the identification of the homeodomains of four different human homeobox genes: HOXB6, HOXA1, HOXA10 and HOXC6. Further studies should determine the specific role of these four homeobox genes in the development and progression of human breast cancer and potentially determine if they might be good targets for gene therapy. [less ▲]

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See detailGalectins: a family of animal beta-galactoside-binding lectins.
Barondes, S. H.; Castronovo, Vincenzo ULg; Cooper, D. N. et al

in Cell (1994), 76(4), 597-8

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See detailCell localization and redistribution of the 67 kD laminin receptor and alpha 6 beta 1 integrin subunits in response to laminin stimulation: an immunogold electron microscopy study.
Romanov, V.; Sobel, M. E.; pinto da Silva, P. et al

in Cell Adhesion and Communication (1994), 2(3), 201-9

The 67 kDa laminin receptor (67LR), one of several cell surface laminin-binding proteins, is involved in the interactions between cancer cells and laminin during tumor invasion and metastasis. A 37 kDa ... [more ▼]

The 67 kDa laminin receptor (67LR), one of several cell surface laminin-binding proteins, is involved in the interactions between cancer cells and laminin during tumor invasion and metastasis. A 37 kDa polypeptide (37LRP), previously identified as the 67LR precursor, is abundantly present in the cytoplasm and has been implicated in polysome formation. To better understand the cellular localization of the 67LR and its precursor, transmission electron microscopic studies of human melanoma A2058 cells were carried out using immunogold labeling and a variety of antibodies: (a) affinity purified antibodies directed against 37LRP cDNA-derived synthetic peptides; (b) anti-67LR monoclonal antibodies raised against intact human small cell lung carcinoma cells; and (c) monoclonal antibodies against the subunits of the integrin laminin receptor, alpha 6 beta 1. Double-labeling immunocyto-chemistry revealed that anti-67LR monoclonal antibodies as well as anti-37 LRP antibodies recognized antigens that were localized in the cytoplasm in electron dense structures. As expected, cell membrane labeling was also observed. Surprisingly, alpha 6 and beta 1 integrin subunits were detected in the same cytoplasmic structures positive for the 67LR and the 37LRP. After addition of soluble laminin to A2058 cells in suspension, the number of labeled cytoplasmic structures increased especially in the vicinity of the plasma membrane, and were exported onto the cell surface. Neither fibronectin nor BSA induced such an effect. The data demonstrate that the 67 LR and the 37 LRP antibodies detect colocalized antigens that are in cytoplasmic structures with alpha 6 beta 1 integrin.(ABSTRACT TRUNCATED AT 250 WORDS) [less ▲]

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See detailTamoxifen activates the cell-cell adhesion function of E-Cadherin in MCF-7/6 human mammary carcinoma cells
Bracke, M.; Charlier, Corinne ULg; Bruyneel, E. et al

Poster (1994)

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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 ▲]

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See detailTamoxifen restores the E-cadherin function in human breast cancer MCF-7/6 cells and suppresses their invasive phenotype
Bracke, M. E.; Charlier, Corinne ULg; Bruyneel, E. A. et al

in Cancer Research (1994), 54

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