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1.
Dental press j. orthod. (Impr.) ; 20(2): 68-75, Mar-Apr/2015. tab, graf
Artículo en Inglés | LILACS | ID: lil-745863

RESUMEN

OBJECTIVE: The aim of this cross sectional study was to assess serum insulin-like growth factor-1 (IGF-1) levels in female and male subjects at various cervical vertebral maturation (CVM) stages. MATERIAL AND METHODS: The study sample consisted of 60 subjects, 30 females and 30 males, in the age range of 8-23 years. For all subjects, serum IGF-1 level was estimated from blood samples by means of chemiluminescence immunoassay (CLIA). CVM was assessed on lateral cephalograms using the method described by Baccetti. Serum IGF-1 level and cervical staging data of 30 female subjects were included and taken from records of a previous study. Data were analyzed by Kruska-Wallis and Mann Whitney test. Bonferroni correction was carried out and alpha value was set at 0.003. RESULTS: Peak value of serum IGF-1 was observed in cervical stages CS3 in females and CS4 in males. Differences between males and females were observed in mean values of IGF-1 at stages CS3, 4 and 5. The highest mean IGF-1 levels in males was observed in CS4 followed by CS5 and third highest in CS3; whereas in females the highest mean IGF-1 levelswas observed in CS3 followed by CS4 and third highest in CS5. Trends of IGF-1 in relation to the cervical stages also differed between males and females. The greatest mean serum IGF-1 value for both sexes was comparable, for females (397 ng/ml) values were slightly higher than in males (394.8 ng/ml). CONCLUSIONS: Males and females showed differences in IGF-1 trends and levels at different cervical stages. .


OBJETIVO: o objetivo do presente estudo transversal foi avaliar os níveis do fator de crescimento semelhante à insulina-1 (IGF-1 sérico) em pacientes de ambos os sexos e em diferentes estágios de maturação das vértebras cervicais (MVC). MÉTODOS: a amostra consistiu de 60 pacientes, sendo 30 do sexo masculino e 30 do sexo feminino, com idades entre 8 e 23 anos. Amostras de sangue foram colhidas de todos os pacientes, cujos níveis de IGF-1 sérico foram avaliados por meio do método de imunoensaio quimioluminescente (CLIA). O estágio de MVC foi avaliado por meio de radiografias cefalométricas de perfil por meio do método descrito por Baccetti. O nível de IGF-1 sérico e o estágio de maturação das vertebras cervicais de 30 pacientes do sexo feminino foram avaliados e os dados retirados dos registros de um estudo prévio. Os dados foram submetidos aos testes de Kruskal-Wallis e de Mann-Whitney. A correção de Bonferroni foi calculada e o valor de alfa foi de 0,003. RESULTADOS: o valor de pico do IGF-1 sérico foi encontrado no estágio CS3, para mulheres, e CS4, para homens. Foram encontradas diferenças entre as médias dos valores de IGF-1 entre homens e mulheres nos estágios CS3, 4 e 5. O valor médio mais alto para os níveis de IGF-1 nos homens foi observado no estágio CS4, seguido do estágio CS5 e CS3. Nas mulheres, o valor médio mais alto foi observado em CS3, seguido do estágio CS4 e CS5. Diferenças também foram encontradas quanto à curva do IGF-1, em relação ao estágio de maturação das vértebras cervicais nos pacientes de ambos os sexos. O valor médio de IGF-1 sérico mais alto foi comparado. As pacientes do sexo feminino apresentaram valores ligeiramente mais altos (397ng/ml) em comparação aos pacientes do sexo masculino (394.8ng/ml). CONCLUSÕES: homens e mulheres apresentam valores de IGF-1 diferentes em estágios de maturação das vértebras cervicais diferentes. .


Asunto(s)
Animales , Ratones , Retículo Endoplásmico/metabolismo , Mediadores de Inflamación/metabolismo , Macrólidos/metabolismo , Mycobacterium ulcerans/patogenicidad , Úlcera de Buruli/metabolismo , Úlcera de Buruli/microbiología , Úlcera de Buruli/patología , Línea Celular , Moléculas de Adhesión Celular , Retículo Endoplásmico/patología , Lipopolisacáridos/toxicidad , Mycobacterium ulcerans/metabolismo , Biosíntesis de Proteínas/efectos de los fármacos , Transporte de Proteínas/efectos de los fármacos , Factor de Necrosis Tumoral alfa
2.
Braz. dent. j ; 22(2): 99-104, 2011. tab
Artículo en Inglés | LILACS | ID: lil-583810

RESUMEN

The present study evaluated the progression of osteogenic cell cultures exposed to a novel calcium aluminate cement (CAC+) in comparison with the gold standard mineral trioxide aggregate (MTA). Cells were enzimatically isolated from newborn rat calvarial bone, plated on glass coverslips containing either CAC+ or a control MTA samples in the center, and grown under standard osteogenic conditions. Over the 10-day culture period, roundening of sample edges was clearly noticed only for MTA group. Although both cements supported osteogenic cell adhesion, spreading, and proliferation, CAC+-exposed cultures showed significantly higher values in terms of total cell number at days 3 and 7, and total protein content and alkaline phosphatase activity at day 10. The present in vitro results indicate that the exposure to CAC+ supports a higher differentiation of osteogenic cells compared with the ones exposed to MTA. Further experimental studies should consider CAC+ as a potential alternative to MTA when the repair of mineralized tissues is one of the desired outcomes in endodontic therapy.


O objetivo do presente estudo foi avaliar a progressão de cultura de células osteogênicas expostas a um novo cimento de aluminato de cálcio (CAC+) em comparação ao agregado de trióxido mineral (MTA). As células foram obtidas por digestão enzimática de calvária de ratos recém-nascidos, plaqueadas sobre lamínulas de vidro contendo em sua área central discos de CAC+ ou MTA e crescidas em condições osteogênicas por até 10 dias. Durante a cultura primária, observou-se o arredondamento das bordas das amostras de cimento apenas para MTA. Embora ambos os cimentos tenham permitido a adesão, o espraiamento e a proliferação celulares, as culturas crescidas em contato com CAC+ exibiram valores maiores de número total de células em 3 e 7 dias, e de conteúdo de proteína total e atividade de fosfatase alcalina em 10 dias. Os resultados indicam que a exposição ao CAC+ permite o desenvolvimento de uma proporção maior de células em estágios mais avançados da diferenciação osteoblástica, quando comparado ao MTA. Deve-se considerar em futuros estudos experimentais a utilização do CAC+ como um material alternativo ao MTA especialmente quando um dos objetivos do tratamento endodôntico é o de reparação dos tecidos mineralizados da região periapical.


Asunto(s)
Animales , Ratas , Compuestos de Aluminio/farmacología , Compuestos de Calcio/farmacología , Osteoblastos/efectos de los fármacos , Osteogénesis/efectos de los fármacos , Materiales de Obturación del Conducto Radicular/farmacología , Animales Recién Nacidos , Fosfatasa Alcalina/metabolismo , Células Cultivadas , Adhesión Celular/efectos de los fármacos , Diferenciación Celular/efectos de los fármacos , Proliferación Celular/efectos de los fármacos , Supervivencia Celular/efectos de los fármacos , Combinación de Medicamentos , Ensayo de Materiales , Óxidos/farmacología , Biosíntesis de Proteínas/efectos de los fármacos , Ratas Wistar , Silicatos/farmacología
3.
Indian J Biochem Biophys ; 2010 Apr; 47(2): 67-74
Artículo en Inglés | IMSEAR | ID: sea-135246

RESUMEN

The heme-regulated inhibitor (HRI), a member of the eIF-2 kinase family is crucial for regulating protein synthesis during stress. In addition to heme, stress proteins Hsp90 and Hsp70 are known to regulate HRI. The present study aims to determine the physical association of these Hsps in the regulation of HRI activation during oxidative stress using human K562 cells as a model. Extracts from the stress-induced cells were used for determining HRI kinase activity by measuring eIF-2 phosphorylation, and Hsp-HRI interaction by immunoprecipitation and immunoblot analyses. The results indicate a significant increase in both Hsp70 and Hsp90 expression during AAPH (2, 2’-azobis (2-amidinopropane) dihydrochloride)-induced oxidative stress. Further, their interaction with HRI, which correlates well with its increased HRI kinase activity leads to inhibition of protein synthesis. Thus, we demonstrate that Hsps play an important role in the regulation of initiation of protein synthesis during oxidative stress.


Asunto(s)
Amidinas/química , Amidinas/farmacología , Animales , Activación Enzimática/efectos de los fármacos , Proteínas HSP70 de Choque Térmico/metabolismo , Proteínas HSP90 de Choque Térmico/metabolismo , Hemina/farmacología , Humanos , Interacciones Hidrofóbicas e Hidrofílicas , Espacio Intracelular/efectos de los fármacos , Espacio Intracelular/metabolismo , Células K562 , Estrés Oxidativo/efectos de los fármacos , Fosforilación/efectos de los fármacos , Biosíntesis de Proteínas/efectos de los fármacos , Especies Reactivas de Oxígeno/metabolismo
4.
Artículo en Inglés | IMSEAR | ID: sea-46233

RESUMEN

OBJECTIVES: To seek an interrelationship, if any, between oxidant stress and neurochemical changes in various rat brain regions after arsenic exposure. MATERIALS AND METHODS: This study was carried out at the Department of Biochemistry, Al Arab Medical University, Benghazi, Libya. Seventy five male Spraque-Dawley rats were divided into three groups: CONTROL GROUP: Rats were administered 2 ml of normal saline solution/kg body weight (b.wt.) daily for 20 days by intraperitoneal (i.p.) route. ARSENIC-TREATED GROUP: Rats received elemental arsenic (as sodium arsenate) 2.0 mg/kg b.wt. daily for 20 days by i.p. route. RECOVERY GROUP: Rats received 2.0 mg/kg b.wt. elemental arsenic daily for 20 days by i.p. route and were allowed to recover for 20 days. Rats were sacrificed and brains were dissected into cerebral cortex, corpus striatum, cerebellum and brain stem. Tissue homogenized in respective mediums. And were analyzed for lipid classes, oxidative stress, concentration of proteins, glutathione and ascorbic acid by utilizing standard colorimetric procedures. RESULTS: Arsenic exposure increased the oxidant stress because lipid peroxidation was enhanced. And decreased the contents of lipid classes, proteins, glutathione and the ascorbic acid in various rat brain regions. However, thins-layer chromatography exhibited regional variations in phospholipids classes. CONCLUSION: These results suggested that arsenic-initiated oxidant stress by increasing lipid peroxidation. The losses of lipid classes, ascorbic acid and glutathione may be attributed to peroxidative damage and binding of arsenic with sulfhydryl groups of enzymes. Recovery of animals showed reversibility in most of studied parameters, but gangliosides and cerebrosides over shooted. And speculated "Sphingolipidosis". It is then likely that repeated exposures of humans to arsenic may result in hampering of cell signalling, apoptosis and mutagenesis.


Asunto(s)
Animales , Antioxidantes/metabolismo , Arseniatos/toxicidad , Ácido Ascórbico/metabolismo , Encéfalo/metabolismo , Cromatografía en Capa Delgada , Glutatión/metabolismo , Peroxidación de Lípido , Masculino , Estrés Oxidativo , Biosíntesis de Proteínas/efectos de los fármacos , Ratas , Ratas Sprague-Dawley , Esfingolipidosis/inducido químicamente , Compuestos de Sulfhidrilo/metabolismo
5.
Yonsei Medical Journal ; : 308-316, 2007.
Artículo en Inglés | WPRIM | ID: wpr-180514

RESUMEN

PURPOSE: We recently reported that rosiglitazone (RGTZ), a peroxisome proliferator-activated receptor gamma (PPARgamma) agonist, has a protective effect against cyclosporine (CsA)- induced renal injury. Here we report the effect of RGTZ on peroxisome proliferator-activated receptor gamma (PPARgamma) expression in an experimental model of chronic cyclosporine (CsA) nephropathy. MATERIALS AND METHODS: Chronic CsA nephropathy was induced in Sprague-Dawley rats by administering CsA (15mg/kg per day) for 28 days, and control rats were treated with vehicle (VH group, olive oil 1mL/kg per day) for 28 days. RGTZ (3mg/kg) was concurrently administered via gavage to the CsA and VH groups. Expression of PPARgamma mRNA and protein was evaluated with RT-PCR, immunohistochemistry, and immunoblotting. RESULTS: PPARgamma mRNA expression was similar to the level of PPARgamma protein constitutively expressed in the kidneys of the VH treated rats, with expression in the glomerular epithelial, distal tubular cells, and collecting tubular cells. PPARgamma protein expression in CsA-treated rat kidneys was significantly less than in the VH group. However, concomitant administration of RGTZ restored PPARgamma protein expression in the kidneys of the CsA- reated rats. CONCLUSION: Exogenous administration of RGTZ treatment upregulates PPARgamma expression and that this mechanism may play a role in protecting against CsA-induced renal injury.


Asunto(s)
Ratas , Masculino , Animales , Transcripción Genética/efectos de los fármacos , Tiazolidinedionas/farmacología , Ratas Sprague-Dawley , ARN Mensajero/genética , Biosíntesis de Proteínas/efectos de los fármacos , PPAR gamma/genética , Enfermedades Renales/genética , Regulación de la Expresión Génica/efectos de los fármacos , Modelos Animales de Enfermedad , Ciclosporina/toxicidad
6.
Experimental & Molecular Medicine ; : 677-685, 2006.
Artículo en Inglés | WPRIM | ID: wpr-106417

RESUMEN

The early growth response-1 gene (egr-1) encodes a zinc-finger transcription factor Egr-1 and is rapidly inducible by a variety of extracellular stimuli. Anisomycin (ANX), a protein synthesis inhibitor, stimulates mitogen-activated protein kinase (MAPK) pathways and thereby causes a rapid induction of immediate-early response genes. We found that anisomycin treatment of U87MG glioma cells resulted in a marked, time-dependent increase in levels of Egr-1 protein. The results of Northern blot analysis and reporter gene assay of egr-1 gene promoter (Pegr-1) activity indicate that the ANX- induced increase in Egr-1 occurs at the transcriptional level. Deletion of the serum response element (SRE) in the 5'-flanking region of egr-1 gene abolished ANX-induced Pegr-1 activity. ANX induced the phosphorylation of the ERK1/2, JNK, and p38 MAPKs in a time-dependent manner and also induced transactivation of Gal4-Elk-1, suggesting that Elk-1 is involved in SRE-mediated egr-1 transcription. Transient transfection of dominant-negative constructs of MAPK pathways blocked ANX-induced Pegr-1 activity. Furthermore, pretreatment with specific MAPK pathway inhibitors, including the MEK inhibitor U0126, the JNK inhibitor SP600125, and the p38 kinase inhibitor SB202190, completely inhibited ANX-inducible expression of Egr-1. Taken together, these results suggest that all three MAPK pathways play a crucial role in ANX-induced transcriptional activation of Pegr-1 through SRE-mediated transactivation of Elk


Asunto(s)
Humanos , Proteínas Quinasas p38 Activadas por Mitógenos/genética , Proteína Elk-1 con Dominio ets/genética , Activación Transcripcional/efectos de los fármacos , Elemento de Respuesta al Suero , Inhibidores de Proteínas Quinasas/farmacología , Biosíntesis de Proteínas/efectos de los fármacos , Regiones Promotoras Genéticas/genética , Sistema de Señalización de MAP Quinasas/efectos de los fármacos , Proteínas Quinasas JNK Activadas por Mitógenos/genética , Quinasas MAP Reguladas por Señal Extracelular/genética , Proteína 1 de la Respuesta de Crecimiento Precoz/genética , Línea Celular Tumoral , Anisomicina/farmacología
7.
Experimental & Molecular Medicine ; : 265-272, 2006.
Artículo en Inglés | WPRIM | ID: wpr-96564

RESUMEN

Phosphoinositide-specific phospholipase C-gamma1 (PLC-gamma1) has two pleckstrin homology (PH) domains: an amino-terminal domain (PH1) and a split PH domain (PH2). Here, we show that overlay assay of bovine brain tubulin pool with glutathione-S-transferase (GST)-PLC-gamma1 PH domain fusion proteins, followed by matrix-assisted laser-desorption ionization-time of flight mass spectrometry (MALDI-TOF MS), identified 68-kDa neurofilament light chain (NF-L) as a binding protein of amino-terminal PH domain of PLC-gamma1. NF-L is known as a component of neuronal intermediate filaments, which are responsible for supporting the structure of myelinated axons in neuron. PLC-gamma1 and NF-L colocalized in the neurite in PC12 cells upon nerve growth factor stimulation. In vitro binding assay and immunoprecipitation analysis also showed a specific interaction of both proteins in differentiated PC12 cells. The phosphatidylinositol 4, 5-bisphosphate [PI(4,5)P2] hydrolyzing activity of PLC-gamma1 was slightly decreased in the presence of purified NF-L in vitro, suggesting that NF-L inhibits PLC-gamma1. Our results suggest that PLC-gamma1-associated NF-L sequesters the phospholipid from the PH domain of PLC-gamma1.


Asunto(s)
Ratas , Animales , Espectrometría de Masa por Láser de Matriz Asistida de Ionización Desorción , Mapeo de Interacción de Proteínas , Biosíntesis de Proteínas/efectos de los fármacos , Unión Proteica/efectos de los fármacos , Fosfoproteínas/química , Fosfolipasa C gamma/antagonistas & inhibidores , Fosfatidilinositol 4,5-Difosfato/metabolismo , Péptidos/química , Células PC12 , Proteínas de Neurofilamentos/química , Factor de Crecimiento Nervioso/farmacología , Peso Molecular , Datos de Secuencia Molecular , Microtúbulos/metabolismo , Microscopía Fluorescente , Isoenzimas/metabolismo , Glutatión Transferasa/metabolismo , Far-Western Blotting , Proteínas Sanguíneas/química , Sitios de Unión , Secuencia de Aminoácidos
8.
Experimental & Molecular Medicine ; : 310-319, 2006.
Artículo en Inglés | WPRIM | ID: wpr-51258

RESUMEN

Myristoylated alanine-rich C kinase substrate (MARCKS) is a widely distributed protein kinase C (PKC) substrate and has been implicated in actin cytoskeletal rearrangement in response to extracellular stimuli. Although MARCKS was extensively examined in various cell culture systems, the physiological function of MARCKS in the central nervous system has not been clearly understood. We investigated alterations of cellular distribution and phosphorylation of MARCKS in the hippocampus following kainic acid (KA)-induced seizures. KA (25 mg/kg, i.p.) was administered to eight to nine week-old C57BL/6 mice. Behavioral seizure activity was observed for 2 h after the onset of seizures and was terminated with diazepam (8 mg/kg, i.p.). The animals were sacrificed and analyzed at various points in time after the initiation of seizure activity. Using double-labeling immunofluorescence analysis, we demonstrated that the expression and phosphorylation of MARCKS was dramatically upregulated specifically in microglial cells after KA-induced seizures, but not in other types of glial cells. PKC alpha, beta I, beta II and delta, from various PKC isoforms examined, also were markedly upregulated, specifically in microglial cells. Moreover, immunoreactivities of phosphorylated MARCKS were co-localized in the activated microglia with those of the above isoforms of PKC. Taken together, our in vivo data suggest that MARCKS is closely linked to microglial activation processes, which are important in pathological conditions, such as neuroinflammation and neurodegeneration.


Asunto(s)
Ratones , Animales , Regulación hacia Arriba/efectos de los fármacos , Factores de Tiempo , Convulsiones/inducido químicamente , Proteína Quinasa C-delta/análisis , Proteína Quinasa C-alfa/análisis , Proteína Quinasa C/análisis , Biosíntesis de Proteínas/efectos de los fármacos , Fosforilación/efectos de los fármacos , Microscopía Confocal , Microglía/citología , Ratones Endogámicos C57BL , Proteínas de la Membrana/análisis , Ácido Kaínico/toxicidad , Isoenzimas/análisis , Péptidos y Proteínas de Señalización Intracelular/análisis , Inmunohistoquímica
9.
Indian J Physiol Pharmacol ; 2005 Apr; 49(2): 139-47
Artículo en Inglés | IMSEAR | ID: sea-107021

RESUMEN

Successful blastocyst implantation depends upon the synchronous dialogue between age- and stage-matched embryo and adequately primed maternal endometrium. Endometrial signals present in the uterine lumen influence the growth and the viability of preimplantation stage embryo. Thus, uterine secretion of embryotoxic cytokines may affect the preimplantation stage embryo. Our previous study in the rhesus monkey has indicated that tumor necrosis factor-alpha (TNF-alpha) is one such candidate present in the uterine lumen, which may act as an embryotoxic agent. In the present study, the effect of TNF-alpha on de novo protein synthesis by mouse morulae (n = 100) and blastocysts (n = 100) in vitro was investigated by 2D-polyacrylamide gel electrophoresis. A total of 35 and 40 protein spots were detected in lysates of control morulae and blastocysts, respectively. Exposure of embryos to TNF-alpha (50 ng/ml) reduced the number of protein spots to 15 and 17 compared to that of control morulae and blastocysts. Seven spots in morula and 13 protein spots in blastocyst flourograms showed quantitative changes in their expressions with exposure to TNF-alpha. Morulae and blastocysts exposed to TNF-alpha expressed 8 and 17 protein spots, respectively, that were not seen in control embryos. It appears from the present study that exposure of preimplantation stage embryos to TNF-alpha affects their protein synthesis both quantitatively and qualitatively.


Asunto(s)
Animales , Blastocisto/citología , Electroforesis en Gel Bidimensional , Femenino , Ratones , Mórula/citología , Técnicas de Cultivo de Órganos , Embarazo , Biosíntesis de Proteínas/efectos de los fármacos , Apoyo a la Investigación como Asunto , Factor de Necrosis Tumoral alfa/metabolismo
10.
Indian Pediatr ; 2004 Nov; 41(11): 1129-32
Artículo en Inglés | IMSEAR | ID: sea-12921

RESUMEN

Linezolid is an oxazolidinone antibacterial agent that acts by inhibiting the initiation of bacterial protein synthesis. Linezolid has a wide spectrum of activity against gram-positive organisms including methicillin resistant staphylococci, penicillin resistant pneumococci and vancomycin resistant enterococcus faecalis and E. faecium. Linezolid has a good bio-availability orally and could be switched from parenteral to oral therapy while treating serious infections. Linezolid is well tolerated in children.


Asunto(s)
Acetamidas/efectos adversos , Adulto , Antibacterianos/efectos adversos , Niño , Infecciones por Bacterias Grampositivas/tratamiento farmacológico , Humanos , Oxazolidinonas/efectos adversos , Biosíntesis de Proteínas/efectos de los fármacos , Inhibidores de la Síntesis de la Proteína/efectos adversos
11.
J Biosci ; 2001 Jun; 26(2): 225-31
Artículo en Inglés | IMSEAR | ID: sea-110866

RESUMEN

Leishmania donovani requires an exogenous source of heme for growth and transformation. In in vitro culture of the free-living promastigotes, exogenously added hemin enhances cell proliferation. In this investigation, the question of the function of heme with particular reference to protein synthesis and cell proliferation has been addressed. The results of in vitro cell culture experiments demonstrated that hemin (10 microM) alone is suitable for supporting optimum level of protein synthesis, and thereby cell proliferation of promastigotes to an extent that it can replace fetal bovine serum. However, in situ labelling experiments along with Western blots revealed that high concentration of hemin (50 microM) reduced the level of protein synthesis in general and of beta-tubulin in particular with a concomitant induction of hsp90, and induced consequent morphological changes that are observed during in situ transformation of promastigotes in mammalian macrophages. These results therefore suggest that sudden exposure to high concentration of heme in mammalian macrophages may be one of the key factors that trigger promastigote to amastigote transformation in L. donovani. Furthermore, hemin with its dual characteristic could be used as a tool to understand molecular mechanism of cell proliferation and transformation in these parasites.


Asunto(s)
Animales , División Celular/efectos de los fármacos , Relación Dosis-Respuesta a Droga , Proteínas HSP90 de Choque Térmico/biosíntesis , Hemina/farmacología , Immunoblotting , Leishmania donovani/citología , Biosíntesis de Proteínas/efectos de los fármacos , Proteínas Protozoarias/biosíntesis , Tubulina (Proteína)/biosíntesis
12.
Journal of Korean Medical Science ; : 189-192, 1992.
Artículo en Inglés | WPRIM | ID: wpr-191175

RESUMEN

The intracellular mechanism by which interferon-gamma induces the expression of class II major histocompatibility complex (MHC) antigen in nonlymphoid cells is not clear. The effect of recombinant rat interferon-gamma (IFN-gamma), and cycloheximide on the expression of class II MHC gene was studied using the techniques of immunocytochemical staining and northern blot analysis. IFN-gamma induced de novo transcription of class II MHC gene and class II MHC antigen expression on the cell surface. Cycloheximide did not inhibit IFN-gamma-induced class II MHC antigen expression in a dose-dependent manner indicating translational blockade. These results suggest that IFN-gamma induces class II MHC antigen expression via de novo transcription of class II MHC gene leading to synthesis of new class II MHC molecule.


Asunto(s)
Animales , Ratas , Línea Celular , Cicloheximida/farmacología , Regulación de la Expresión Génica/efectos de los fármacos , Genes MHC Clase II , Interferón gamma/farmacología , Biosíntesis de Proteínas/efectos de los fármacos , Transcripción Genética/efectos de los fármacos
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