Your browser doesn't support javascript.
loading
Mostrar: 20 | 50 | 100
Resultados 1 - 5 de 5
Filtrar
1.
Oncogene ; 25(11): 1594-601, 2006 Mar 13.
Artículo en Inglés | MEDLINE | ID: mdl-16550159

RESUMEN

Identifying genes involved in the development of cancer is crucial to fully understanding cancer biology, for developing novel therapeutics for cancer treatment and for providing methods for cancer prevention and early diagnosis. The use of polymorphic markers, in particular single nucleotide polymorphisms (SNPs), promises to provide a comprehensive tool for analysing the human genome and identifying those genes and genomic regions contributing to the cancer phenotype. This review summarizes the various analytical methodologies in which SNPs are used and presents examples of how each of these methodologies have been used to locate genes and genomic regions of interest for various cancer types. Additionally many of the current SNP-analysing technologies will be reviewed with particular attention paid to the advantages and disadvantages of each and how each technology can be applied to the analysis of the genome for identifying cancer-related genes.


Asunto(s)
Marcadores Genéticos , Neoplasias/genética , Polimorfismo de Nucleótido Simple , Ligamiento Genético , Predisposición Genética a la Enfermedad , Genotipo , Humanos
2.
Mol Cell Biol ; 14(2): 1171-8, 1994 Feb.
Artículo en Inglés | MEDLINE | ID: mdl-8289798

RESUMEN

The mdm2 oncogene, which is often amplified in mammalian tumors, produces a number of transcripts that encode distinct protein forms. Previous studies demonstrating that overexpression of the mdm2 gene can activate its transforming potential, and can inhibit the transcriptional activation function of p53, prompted us to begin to explore possible functional differences among the various mdm2 products. Utilizing a transient transfection assay, we have evaluated four naturally occurring murine mdm2 forms for their ability to inhibit p53-mediated transcriptional activation of reporter genes regulated by p53 response elements. Three of these mdm2 forms were found to physically associate with the wild-type p53 protein and to possess the ability to inhibit its transactivation function. A fourth form failed to exhibit either of these functions. This last mdm2 form lacks the N-terminal protein domain that is present in the other three splice forms examined, pointing to this region as one that is critical for complex formation with the p53 protein. Identifying such differences among mdm2 proteins provides important clues for dissecting their functional domains, and emphasizes that defining the individual properties of these products will be critical in elucidating the overall growth control function of the mdm2 gene.


Asunto(s)
Proteínas de Neoplasias/metabolismo , Proteínas Nucleares , Proteínas Proto-Oncogénicas , Proteína p53 Supresora de Tumor/metabolismo , Empalme Alternativo , Animales , Carcinoma de Pulmón de Células no Pequeñas , Línea Celular , Cloranfenicol O-Acetiltransferasa/biosíntesis , Cloranfenicol O-Acetiltransferasa/metabolismo , Eliminación de Gen , Humanos , Luciferasas/biosíntesis , Luciferasas/metabolismo , Neoplasias Pulmonares , Ratones , Proteínas de Neoplasias/biosíntesis , Oncogenes , Proteínas Proto-Oncogénicas c-mdm2 , ARN Mensajero/metabolismo , Transcripción Genética , Transfección , Células Tumorales Cultivadas
4.
Genomics ; 19(3): 407-16, 1994 Feb.
Artículo en Inglés | MEDLINE | ID: mdl-8188282

RESUMEN

The mouse dilute gene encodes a novel type of non-muscle myosin that structurally combines elements from both nonmuscle myosin type I and nonmuscle myosin type II. Phenotypically, mutations in the mouse dilute gene result not only in the lightening of coat color, but also in the onset of severe neurological defects shortly after birth. This may indicate that the mouse dilute gene is important in maintaining the normal neuronal function in the mouse. We report the isolation and sequencing of "myoxin" (MYH12), the human homologue of the mouse dilute gene, and its assignment to human chromosome 15.


Asunto(s)
Cromosomas Humanos Par 15 , Proteínas de Filamentos Intermediarios/genética , Ratones/genética , Cadenas Pesadas de Miosina , Miosina Tipo V , Miosinas/clasificación , Proteínas del Tejido Nervioso/genética , Secuencia de Aminoácidos , Animales , Secuencia de Bases , Pollos/genética , Mapeo Cromosómico , Clonación Molecular , Epilepsia/genética , Color del Cabello/genética , Humanos , Síndromes de Inmunodeficiencia/genética , Proteínas de Filamentos Intermediarios/inmunología , Ratones Mutantes Neurológicos/genética , Datos de Secuencia Molecular , Familia de Multigenes , Miosinas/genética , Proteínas del Tejido Nervioso/inmunología , Trastornos de la Pigmentación/genética , Proteínas Proto-Oncogénicas p21(ras)/genética , Proteínas Proto-Oncogénicas p21(ras)/inmunología , Alineación de Secuencia , Homología de Secuencia , Síndrome
5.
J Cell Physiol ; 126(3): 333-40, 1986 Mar.
Artículo en Inglés | MEDLINE | ID: mdl-3949887

RESUMEN

ST2-3T3, a spontaneously transformed BALB/c-3T3 cell line which does not require platelet-derived growth factor (PDGF) for growth, was fused to THO2, a PDGF-responsive non-transformed BALB/c-3T3 cell line, in order to learn whether transformation is expressed coordinately with PDGF independence. Hybrid cells were selected and grown in medium containing both HAT (hypoxanthine-aminopterin-thymidine) and ouabain; unfused cells of each parental type were killed in HAT-ouabain medium. Five independently isolated ST2-3T3xTHO2 hybrid cell lines were established and characterized for both transformation and PDGF responsiveness. All five were transformed, having a disorganized growth pattern and achieving a final cell density similar to that of ST2-3T3 cells. Two of these lines did not respond to a brief treatment with PDGF: the mitogen neither induced the synthesis of a PDGF-modulated lysosomal protein (termed MEP), nor stimulated the cells to enter the S phase; one line responded to PDGF by synthesizing both MEP and DNA, whereas two others synthesized MEP but not DNA. In contrast, four independently isolated cell lines obtained by fusing PDGF-responsive non-transformed BALB/c-3TC cells to the THO2 line were all PDGF-responsive for both MEP and DNA synthesis and were not transformed. It appears that PDGF independence is not required for the transformation of BALB/c-3T3 cells.


Asunto(s)
Transformación Celular Viral/efectos de los fármacos , Factor de Crecimiento Derivado de Plaquetas/farmacología , Proteínas , Animales , División Celular/efectos de los fármacos , Línea Celular , Separación Celular , Medios de Cultivo , Replicación del ADN/efectos de los fármacos , Citometría de Flujo , Células Híbridas/efectos de los fármacos , Ratones , Ratones Endogámicos BALB C , Biosíntesis de Proteínas
SELECCIÓN DE REFERENCIAS
DETALLE DE LA BÚSQUEDA