16 results on '"Motti, M. L."'
Search Results
2. Low doses interferon-α in the treatment of high-risk cutaneous melanoma
- Author
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Ascierto, P. A., Palmieri, G., Strazzullo, M., Daponte, A., Botti, G., Satriano, S. M. R., Motti, M. L., Mozzillo, N., and Castello, G.
- Published
- 2000
3. Loss of tumour suppressor gene PTEN marks the transition from intratubular germ cell neoplasias (ITGCN) to invasive germ cell tumors
- Author
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DI VIZIO D., CITO L., BOCCIA A., INSABATO L., PETTINATO G., MOTTI M. L., SCHEPIS F., D, AMICO W., FABIANI F., TAVERNISE B., VENUTA S., FUSCO A., VIGLIETTO G., CHIEFFI, Paolo, DI VIZIO, D., Cito, L., Boccia, A., Chieffi, Paolo, Insabato, L., Pettinato, G., Motti, M. L., Schepis, F., D, Amico, W., Fabiani, F., Tavernise, B., Venuta, S., Fusco, A., and Viglietto, G.
- Published
- 2005
4. Critical role of cyclin D3 in TSH-dependent growth of thyreocytes and in hyperproliferative disorders of the thyroid gland
- Author
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MOTTI M. L, BOCCIA A, BELETTI B, BRUNI P, CITO L, MONACO M, CHIAPPETTA G, BALDASSARE G, PALOMBINI L, FUSCO, ALFREDO, VIGLIETTO G., TRONCONE, GIANCARLO, MOTTI M., L, Boccia, A, Beletti, B, Bruni, P, Troncone, Giancarlo, Cito, L, Monaco, M, Chiappetta, G, Baldassare, G, Palombini, L, Fusco, Alfredo, and Viglietto, G.
- Published
- 2003
5. Complex regulation of the cyclin-dependent kinase inhibitor p27kip1 in thyroid cancer cells by the PI3K/AKT pathway: regulation of p27kip1 expression and localization
- Author
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Motti, M. L., Califano, D., Troncone, G., Marco, C., Migliaccio, I., Palmieri, E., Pezzullo, L., Palombini, L., Alfredo Fusco, Viglietto, G., Motti, Ml, Califano, D, Troncone, Giancarlo, DE MARCO, C, Migliaccio, I, Palmieri, E, Pezzullo, L, Palombini, Lucio, Fusco, Alfredo, and Viglietto, G.
- Subjects
Cytoplasm ,Time Factors ,Morpholines ,Blotting, Western ,Cell Cycle Proteins ,Protein Serine-Threonine Kinases ,Transfection ,Phosphatidylinositol 3-Kinases ,Cytosol ,Cell Line, Tumor ,Proto-Oncogene Proteins ,Humans ,Thyroid Neoplasms ,Phosphorylation ,S-Phase Kinase-Associated Proteins ,Reverse Transcriptase Polymerase Chain Reaction ,Tumor Suppressor Proteins ,PTEN Phosphohydrolase ,Flow Cytometry ,Phosphoric Monoester Hydrolases ,Androstadienes ,Enzyme Activation ,Gene Expression Regulation, Neoplastic ,Original Research Paper ,Bromodeoxyuridine ,Microscopy, Fluorescence ,Chromones ,Wortmannin ,Proto-Oncogene Proteins c-akt ,Cyclin-Dependent Kinase Inhibitor p27 - Abstract
Functional inactivation of the tumor suppressor p27(kip1) in human cancer occurs either through loss of expression or through phosphorylation-dependent cytoplasmic sequestration. Here we demonstrate that dysregulation of the PI3K/AKT pathway is important in thyroid carcinogenesis and that p27(kip1) is a key target of the growth-regulatory activity exerted by this pathway in thyroid cancer cells. Using specific PI3K inhibitors (LY294002, wortmannin, and PTEN) and a dominant active AKT construct (myrAKT), we demonstrated that the PI3K/AKT pathway controlled thyroid cell proliferation by regulating the expression and subcellular localization of p27. Results obtained with phospho-specific antibodies and with transfection of nonphosphorylable p27(kip1) mutant constructs demonstrated that PI3K/AKT-dependent regulation of p27(kip1) mislocalization in thyroid cancer cells occurred via phosphorylation of p27(kip1) at T157 and T198 (but not at S10 or T187). Finally, we evaluated whether these results were applicable to human tumors. Analysis of 100 thyroid carcinomas indicated that p27(kip1) phosphorylation at T157/T198 and cytoplasmic mislocalization were preferentially associated with activation of the PI3K/AKT pathway. Thus the PI3/AKT pathway and its effector p27(kip1) play major roles in thyroid carcinogenesis.
- Published
- 2005
6. Retinoic acid induces neuronal differentiation of embryonal carcinoma cells by reducing proteasome-dependent proteolysis of the cyclin-dependent inhibitor p27
- Author
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Baldassarre, G., Boccia, A., Bruni, P., Sandomenico, C., Maria Vittoria BARONE, Pepe, S., Angrisano, T., Belletti, B., Motti, M. L., Fusco, A., Viglietto, G., G., Baldassarre, A., Boccia, P., Bruni, C., Sandomenico, M. V., Barone, S., Pepe, Angrisano, Tiziana, B., Belletti, M. L., Motti, Fusco, Alfredo, G., Viglietto, Barone, MARIA VITTORIA, Pepe, Stefano, and G. V. i. g. l. i. e. t. t., O.
- Subjects
Neurons ,Proteasome Endopeptidase Complex ,Tumor Suppressor Proteins ,p27 ,Antineoplastic Agents ,Cell Cycle Proteins ,Cell Differentiation ,Tretinoin ,NTERA-2 clone D1 cell line ,Cyclin-Dependent Kinases ,Gene Expression Regulation, Neoplastic ,Cysteine Endopeptidases ,Multienzyme Complexes ,Carcinoma, Embryonal ,Tumor Cells, Cultured ,retinoic acid ,Humans ,Microtubule-Associated Proteins ,neuronal differentiation ,Cyclin-Dependent Kinase Inhibitor p27 - Abstract
Retinoic acid (RA) treatment of embryonal carcinoma cell line NTERA-2 clone D1 (NT2/D1) induces growth arrest and terminal differentiation along the neuronal pathway. In the present study, we provide a functional link between RA and p27 function in the control of neuronal differentiation in NT2/D1 cells. We report that RA enhances p27 expression, which results in increased association with cyclin E/cyclin-dependent kinase 2 complexes and suppression of their activity; however, antisense clones, which have greatly reduced RA-dependent p27 inducibility (NT2-p27AS), continue to synthesize DNA and are unable to differentiate properly in response to RA as determined by lack of neurite outgrowth and by the failure to modify surface antigens. As to the mechanism involved in RA-dependent p27 up-regulation, our data support the concept that RA reduces p27 protein degradation through the ubiquitin/proteasome-dependent pathway. Taken together, these findings demonstrate that in embryonal carcinoma cells, p27 expression is required for growth arrest and proper neuronal differentiation.
- Published
- 2000
7. Use of nutritional supplements among south Italian students of physical training and sport university
- Author
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Mazzeo, F., Motti, M. L., Messina, G., Monda, V., Ascione, A., Domenico Tafuri, Palmieri, F., Messina, A., Monda, M., Mazzeo, F, Motti, Ml, Messina, G, Monda, Marcellino, Ascione, A, Tafuri, D, Palmieri, F, Messina, A, and Monda, M.
- Subjects
education
8. Clinical significance of PCR-positive mRNA markers in peripheral blood and regional nodes of malignant melanoma patients. Melanoma Cooperative Group
- Author
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Palmieri, G., Pirastu, M., Strazzullo, M., Ascierto, P. A., Satriano, S. M., Motti, M. L., Gerardo Botti, Mozzillo, N., Castello, G., Cossu, A., Lissia, A., and Tanda, F.
9. Loss of the tumor suppressor gene PTEN marks the transition from intratubular germ cell neoplasias (ITGCN) to invasive germ cell tumors
- Author
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Alfredo Fusco, Wanda D'Amico, Barbara Tavernise, Luigi Insabato, Filippo Schepis, Guido Pettinato, Dolores Di Vizio, Maria Letizia Motti, Paolo Chieffi, Fernanda Fabiani, Letizia Cito, Salvatore Venuta, Angelo Boccia, Giuseppe Viglietto, Di Vizio, D., Cito, L., Boccia, A., Chieffi, P., Insabato, Luigi, Pettinato, Guido, Motti, M. L., Schepis, F., D'Amico, W., Fabiani, F., Tavernise, B., Venuta, S., Fusco, Alfredo, and Viglietto, G.
- Subjects
Male ,PTEN ,Cancer Research ,Animals ,Breast Neoplasms ,Cell Line ,Tumor ,Cell Transformation ,Neoplastic ,Chromosomes ,Human ,Pair 10 ,Female ,Flow Cytometry ,Genes ,Tumor Suppressor ,Germinoma ,Humans ,In Situ Hybridization ,Loss of Heterozygosity ,Mice ,PTEN Phosphohydrolase ,Phosphoric Monoester Hydrolases ,RNA ,Messenger ,Testicular Neoplasms ,Testis ,Tumor Suppressor Proteins ,endocrine system diseases ,Genes, Tumor Suppressor ,Cell Transformation, Neoplastic ,Teratoma ,Tumor suppressor gene ,Biology ,Embryonal carcinoma ,Cell Line, Tumor ,Genetics ,medicine ,RNA, Messenger ,Molecular Biology ,PI3K/AKT/mTOR pathway ,ITGCN ,Chromosomes, Human, Pair 10 ,germ cell tumor ,Seminoma ,medicine.disease ,Cancer research ,biology.protein ,Germ cell tumors ,p27kip1 - Abstract
PTEN/MMAC1/TEP1: (hereafter PTEN) is a tumor suppressor gene (located at 10q23) that is frequently mutated or deleted in sporadic human tumors. PTEN encodes a multifunctional phosphatase, which negatively regulates cell growth, migration and survival via the phosphatidylinositol 3'-kinase/AKT signalling pathway. Accordingly, Pten+/- mice develop various types of tumors including teratocarcinomas and teratomas. We have investigated PTEN expression in 60 bioptic specimens of germ cell tumors (32 seminomas, 22 embryonal carcinomas and six teratomas) and 22 intratubular germ cell neoplasias (ITGCN) adjacent to the tumors for PTEN protein and mRNA expression. In total, 10 testicular biopsies were used as controls. In the testis, PTEN was abundantly expressed in germ cells whereas it was virtually absent from 56% of seminomas as well as from 86% of embryonal carcinomas and virtually all teratomas. On the contrary, ITGCN intensely expressed PTEN, indicating that loss of PTEN expression is not an early event in testicular tumor development. The loss of PTEN expression occurs mainly at the RNA level as determined by in situ hybridization of cellular mRNA (17/22) but also it may involve some kind of post-transcriptional mechanisms in the remaining 25% of cases. Analysis of microsatellites D10S551, D10S541 and D10S1765 in GCTs (n=22) showed LOH at the PTEN locus at 10q23 in at least 36% of GCTs (three embryonal carcinoma, three seminoma, two teratoma); one seminoma and one embryonal (9%) carcinoma presented an inactivating mutation in the PTEN gene (2/22). Finally, we demonstrated that the phosphatidylinositol 3'-kinase/AKT pathway, which is regulated by the PTEN phosphatase, is crucial in regulating the proliferation of the NT2/D1 embryonal carcinoma cells, and that the cyclin-dependent kinase inhibitor p27(kip1) is a key downstream target of this pathway.
- Published
- 2005
10. Regulation of p27Kip1 protein levels contributes to mitogenic effects of the RET/PTC kinase in thyroid carcinoma cells
- Author
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Rosa Marina Melillo, Donata Vitagliano, Maria Letizia Motti, Anderson J. Ryan, Massimo Santoro, Giuseppe Viglietto, Alfredo Fusco, Francesca Carlomagno, Jerome M. Hershman, Marina N. Nikiforova, Yuri E. Nikiforov, Vitagliano, D., Carlomagno, Francesca, Motti, M. L., Viglietto, G., Nikiforov, Y. E., Nikiforova, M. N., Hershman, J. M., Ryan, A. J., Fusco, Alfredo, Melillo, ROSA MARINA, and Santoro, Massimo
- Subjects
MAPK/ERK pathway ,Proteasome Endopeptidase Complex ,endocrine system ,Cancer Research ,Oncogene Proteins, Fusion ,endocrine system diseases ,MAP Kinase Signaling System ,Cell Cycle Proteins ,Biology ,Piperidines ,Multienzyme Complexes ,Cell Line, Tumor ,Cyclin D ,Cyclins ,Proto-Oncogene Proteins ,Cyclin E ,medicine ,Humans ,Thyroid Neoplasms ,c-Raf ,Enzyme Inhibitors ,Protein kinase A ,Thyroid cancer ,Cyclin ,Gene Rearrangement ,Kinase ,Tumor Suppressor Proteins ,Proto-Oncogene Proteins c-ret ,Cyclin-dependent kinase 2 ,Receptor Protein-Tyrosine Kinases ,Protein-Tyrosine Kinases ,medicine.disease ,Up-Regulation ,Cysteine Endopeptidases ,Pyrimidines ,Oncology ,Quinazolines ,biology.protein ,Cancer research ,Pyrazoles ,Cyclin-Dependent Kinase Inhibitor p27 - Abstract
We show that treatment of a panel of thyroid carcinoma cell lines naturally harboring the RET/PTC1 oncogene, with the RET kinase inhibitors PP1 and ZD6474, results in reversible G1 arrest. This is accompanied by interruption of Shc and mitogen-activated protein kinase (MAPK) phosphorylation, reduced levels of G1 cyclins, and increased levels of the cyclin-dependent kinase inhibitor p27Kip1 because of a reduced protein turnover. MAP/extracellular signal-regulated kinase 1/2 inhibition by U0126 caused G1 cyclins down-regulation and p27Kip1 up-regulation as well. Forced expression of RET/PTC in normal thyroid follicular cells caused a MAPK- and proteasome-dependent down-regulation of p27Kip1. Reduction of p27Kip1 protein levels by antisense oligonucleotides abrogated the G1 arrest induced by RET/PTC blockade. Therefore, in thyroid cancer, RET/PTC-mediated MAPK activation contributes to p27Kip1 deregulation. This pathway is implicated in cell cycle progression and in response to small molecule kinase inhibitors.
- Published
- 2004
11. Akt-dependent T198 phosphorylation of cyclin-dependent kinase inhibitor p27kip1in breast cancer
- Author
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Giuseppe Viglietto, Daniela Califano, Maria Letizia Motti, Alfredo Fusco, Carmela De Marco, Motti, M. L., DE MARCO, Carmela, Califano, D., Fusco, Alfredo, and Viglietto, G.
- Subjects
Threonine ,Molecular Sequence Data ,Breast Neoplasms ,Cell Cycle Proteins ,Protein Serine-Threonine Kinases ,Biology ,Kidney ,Cell Line ,Phosphates ,chemistry.chemical_compound ,Cyclin-dependent kinase ,Cell Line, Tumor ,Proto-Oncogene Proteins ,Humans ,LY294002 ,Protein phosphorylation ,Amino Acid Sequence ,Breast ,Phosphorylation ,skin and connective tissue diseases ,Molecular Biology ,Protein kinase B ,PI3K/AKT/mTOR pathway ,Kinase ,Tumor Suppressor Proteins ,Epithelial Cells ,Cell Biology ,Transfection ,Enzyme Activation ,chemistry ,biology.protein ,Cancer research ,Proto-Oncogene Proteins c-akt ,Cyclin-Dependent Kinase Inhibitor p27 ,Developmental Biology - Abstract
The localization of the cyclin-dependent kinase inhibitor p27(kip1) is dependent on the phosphorylation of one of three key amino acid residues: S10, T157 and T198. However, it was unclear whether endogenous p27(kip1) is phosphorylated at T198 in the living cell. In the present work we describe the generation and characterization of a polyclonal antibody able to recognize recombinant, transfected as well as endogenous T198-phosphorylated p27(kip1). Using this antibody, we demonstrate that: (1) endogenous p27(kip1) is phosphorylated at T198 in 4 breast cancer cells lines (MCF7, MDA-MB231, MDA- MB436 and MDA-MB468); (2) T198 phosphorylation is increased in breast cancer cells compared with normal mammary epithelial cells (HMEC); (3) T198-phosphorylated p27(kip1) is exclusively cytoplasmic; (4) T198 phosphorylation is dependent on the activity of the PI3K-PKB/Akt pathway, being it drastically reduced by the pharmacological PI3K inhibitor LY294002 or stimulated by the constitutive activation of PKB/Akt. Finally, in primary human breast carcinomas, cytoplasmic accumulation of T198-phosphorylated p27(kip1) parallels Akt activation. We conclude that in breast cancer cells p27(kip1) is phosphorylated at T198 in a PI3K/Akt dependent manner and that this phosphorylation may contribute to p27(kip1) cytoplasmic mislocalization observed in breast cancer.
12. Characterization of 2 novel and 2 recurring BRCA1 germline mutations in breast and/or ovarian carcinoma patients from the area of Naples.
- Author
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Curci A, Capasso I, Romano A, Bruni P, Motti ML, Pignata S, D'Aiuto G, Casamassimi A, D'Urso M, Fusco A, and Viglietto G
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- Adult, Age Factors, Aged, Family Health, Female, Humans, Italy, Male, Middle Aged, Pedigree, Polymorphism, Single-Stranded Conformational, Sequence Analysis, DNA, Breast Neoplasms genetics, Genes, BRCA1, Mutation, Ovarian Neoplasms genetics
- Abstract
We have analyzed 18 families with high incidence of breast cancer or breast and ovarian cancer for the presence of BRCA1 mutations. We identified 4 mutations in the BRCA1 gene in 4 unrelated probands who belong to families with at least 1 case of breast and 1 case of ovarian cancer. Two of the mutations reported in this study are novel (GAA(1172)-->TAA in family Naples 14, GAA(1765)-->TAA in family Naples 20) whereas the others are already present in the Breast Cancer Information Core Electronic Database (http://nchgr.nih.gov/ Intramural research/Lab transfer/Bic/) (5382insC in family Naples 18 and 2080delA in family Naples 19). Conversely, no mutation in the BRCA1 gene was detected in 14 families characterized by 2 or more cases of breast cancer only, even if bilateral and with early-onset. These results indicate that germline mutations in the BRCA1 gene highly predispose for a cancer syndrome that involves the presence of both breast and ovarian cancer.
- Published
- 2002
- Full Text
- View/download PDF
13. Detection of occult melanoma cells in paraffin-embedded histologically negative sentinel lymph nodes using a reverse transcriptase polymerase chain reaction assay.
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Palmieri G, Ascierto PA, Cossu A, Mozzillo N, Motti ML, Satriano SM, Botti G, Caracò C, Celentano E, Satriano RA, Lissia A, Tanda F, Pirastu M, and Castello G
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- Biomarkers, Tumor analysis, DNA, Neoplasm analysis, False Negative Reactions, Humans, Lymphatic Metastasis diagnosis, Melanoma pathology, Paraffin Embedding, Prognosis, Sensitivity and Specificity, Skin Neoplasms pathology, Specimen Handling, Melanoma diagnosis, Reverse Transcriptase Polymerase Chain Reaction standards, Sentinel Lymph Node Biopsy, Skin Neoplasms diagnosis
- Abstract
Purpose: Detection of occult metastasis before the development of clinical disease could allow more accurate staging, appropriate follow-up procedures, and adjuvant therapies in patients with malignant melanoma (MM). The sentinel lymph node (SLN) has been proposed as a reliable predictor of metastatic disease in the lymphatic basin draining the primary melanoma. In this study, we screened both paraffin-embedded SLNs and peripheral-blood (PB) samples from MM patients at various stage of disease using a multimarker reverse transcriptase polymerase chain reaction (RT-PCR) assay. The prognostic significance of the presence of PCR-positive markers was also evaluated., Patients and Methods: Total RNA was obtained from paraffin-embedded SLN sections and PB samples of 75 MM patients. RT-PCR was performed using tyrosinase and MelanA/MART1 as melanoma-associated markers. Radiolabeled PCR products were analyzed on denaturing polyacrylamide gels., Results: Good sensitivity of the RT-PCR assay on archival tissues was demonstrated after comparison of RT-PCR results on frozen and paraffin-embedded SLNs from 16 MM patients. Significant correlation between the disease stage and marker expression in both PB and SLN samples was observed; the highest value was for patients who were positive for both markers in SLN (P =.006). Progression of disease was significantly associated with the total number of PCR-positive markers in both PB (P =.034) and SLN (P =.001) samples., Conclusion: Although sensitivity is lowered by the use of paraffin-embedded specimens, our data indicate that RT-PCR analysis of serial sections from archival SLNs may be helpful in improving detection of occult micrometastases, thus improving staging of patients with melanoma.
- Published
- 2001
- Full Text
- View/download PDF
14. Clinical significance of PCR-positive mRNA markers in peripheral blood and regional nodes of malignant melanoma patients. Melanoma Cooperative Group.
- Author
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Palmieri G, Pirastu M, Strazzullo M, Ascierto PA, Satriano SM, Motti ML, Botti G, Mozzillo N, Castello G, Cossu A, Lissia A, and Tanda F
- Subjects
- Biomarkers, Tumor genetics, Blotting, Southern, Disease Progression, Follow-Up Studies, Humans, Neoplasm Proteins genetics, Neoplasm Staging, Reverse Transcriptase Polymerase Chain Reaction, Biomarkers, Tumor blood, Lymph Nodes pathology, Melanoma blood, Neoplasm Proteins blood, Neoplastic Cells, Circulating, RNA, Messenger analysis, Skin Neoplasms blood
- Abstract
Reverse-transcriptase polymerase chain reaction (RT-PCR) with multiple markers has been demonstrated to be highly sensitive in detecting metastatic cells in peripheral blood of malignant melanoma (MM) patients, and the circulating MM cells to be significantly correlated with disease stages. We further evaluated the presence of specific PCR-positive mRNA markers in peripheral blood as well as in regional nodes as an expression of tumor progression. Peripheral blood samples from 317 MM patients with either localized (n = 219) or metastatic (n = 98) disease were processed to obtain total cellular RNA. RT-PCR was performed using tyrosinase (TYR), p97, and MelanA/MART1 as mRNA markers. PCR products were analyzed by gel electrophoresis and Southern blot hybridization. In addition, paraffin-embedded samples of histologically proven tumor-negative lymph nodes from the subset of patients with localized disease were analyzed by RT-PCR, using radiolabeled primers for TYR and MelanA/MART1. The presence of mRNA markers was significantly correlated with tumor burden with a good correlation between risk of recurrence (evaluated in stage I-III patients) and increasing number of PCR-positive markers (p = 0.0002). Currently, for each patient, PCR results obtained at different times during follow-up are being analyzed, and any variation in the number of PCR-positive markers is being correlated to the clinical status. Molecular screening of histologically negative nodes for the presence of metastatic MM cells is also under evaluation. Preliminary assessment of a subset of MM patients with higher risk of recurrence will require longer follow-up in order to define the role of RT-PCR in monitoring these patients.
- Published
- 2001
- Full Text
- View/download PDF
15. Retinoic acid induces neuronal differentiation of embryonal carcinoma cells by reducing proteasome-dependent proteolysis of the cyclin-dependent inhibitor p27.
- Author
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Baldassarre G, Boccia A, Bruni P, Sandomenico C, Barone MV, Pepe S, Angrisano T, Belletti B, Motti ML, Fusco A, and Viglietto G
- Subjects
- Antineoplastic Agents therapeutic use, Carcinoma, Embryonal genetics, Carcinoma, Embryonal metabolism, Cell Differentiation drug effects, Cyclin-Dependent Kinase Inhibitor p27, Cyclin-Dependent Kinases antagonists & inhibitors, Cysteine Endopeptidases genetics, Cysteine Endopeptidases metabolism, Gene Expression Regulation, Neoplastic drug effects, Humans, Microtubule-Associated Proteins genetics, Microtubule-Associated Proteins metabolism, Multienzyme Complexes genetics, Multienzyme Complexes metabolism, Neurons metabolism, Proteasome Endopeptidase Complex, Tretinoin therapeutic use, Tumor Cells, Cultured, Antineoplastic Agents pharmacology, Carcinoma, Embryonal drug therapy, Carcinoma, Embryonal pathology, Cell Cycle Proteins, Neurons pathology, Tretinoin pharmacology, Tumor Suppressor Proteins
- Abstract
Retinoic acid (RA) treatment of embryonal carcinoma cell line NTERA-2 clone D1 (NT2/D1) induces growth arrest and terminal differentiation along the neuronal pathway. In the present study, we provide a functional link between RA and p27 function in the control of neuronal differentiation in NT2/D1 cells. We report that RA enhances p27 expression, which results in increased association with cyclin E/cyclin-dependent kinase 2 complexes and suppression of their activity; however, antisense clones, which have greatly reduced RA-dependent p27 inducibility (NT2-p27AS), continue to synthesize DNA and are unable to differentiate properly in response to RA as determined by lack of neurite outgrowth and by the failure to modify surface antigens. As to the mechanism involved in RA-dependent p27 upregulation, our data support the concept that RA reduces p27 protein degradation through the ubiquitin/proteasome-dependent pathway. Taken together, these findings demonstrate that in embryonal carcinoma cells, p27 expression is required for growth arrest and proper neuronal differentiation.
- Published
- 2000
16. Low doses interferon-alpha in the treatment of high-risk cutaneous melanoma. Melanoma Cooperative Group.
- Author
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Ascierto PA, Palmieri G, Strazzullo M, Daponte A, Botti G, Satriano SM, Motti ML, and Mozzillo N
- Subjects
- Adult, Disease-Free Survival, Humans, Lymphatic Metastasis, Male, Melanoma secondary, Risk Factors, Skin Neoplasms pathology, Antineoplastic Agents therapeutic use, Interferon-alpha therapeutic use, Melanoma drug therapy, Skin Neoplasms drug therapy
- Published
- 2000
- Full Text
- View/download PDF
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