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1.
Indian J Exp Biol ; 2014 Jun; 52(6): 579-588
Artículo en Inglés | IMSEAR | ID: sea-153736

RESUMEN

The interaction of a newly synthesized antitumor complex cis-dichloro-1,2-propylenediamine-N,N,N',N'-tetraacetato ruthenium (III) (RAP) with DNA was investigated in vitro through a number of techniques including comet assay, immunoprecipitation, and immunolocalization of certain nucleolar proteins (the upstream binding factor (UBF) and fibrillarin) involved in DNA transcription, rRNA processing, and ribosomal assembly. The results showed that RAP binds to the DNA of two cell lines (H4 and Hs-683) causing a delay in cell proliferation rate leading to a number of cellular modifications. These modifications include DNA-damage assessed by the single cell gel electrophoresis method (comet assay) and variation in the expression of nucleolar proteins; UBF was more abundant in RAP treated cells, this was explained by the high affinity of this protein to DNA modified by RAP. On the other hand, fibrillarin was found in less quantities in RAP treated cells which was explained by a de-regulation of the ribosomal machinery caused by RAP.


Asunto(s)
Antineoplásicos/farmacología , Línea Celular Tumoral , Daño del ADN , Evaluación Preclínica de Medicamentos , Humanos , Proteínas Nucleares/metabolismo , Compuestos Organometálicos/farmacología , Transporte de Proteínas/efectos de los fármacos , Procesamiento Postranscripcional del ARN/efectos de los fármacos , Distribución Tisular/efectos de los fármacos , Transcripción Genética/efectos de los fármacos
2.
Indian J Biochem Biophys ; 1990 Dec; 27(6): 438-42
Artículo en Inglés | IMSEAR | ID: sea-26451

RESUMEN

The EGF-receptor is a proto-oncogene encoded membrane protein related to the verb-B oncogene product of avian erythroblastosis virus. Here we report studies on expression and maturation characteristics of this receptor. The expression of intact 170 kDa EGF-receptor as well as a 100 kDa homologue that contains only the external domain is enhanced by the ligand EGF. EGF acts at transcriptional and post-transcriptional levels. To dissociate these pre-translational effects and the effects of EGF on receptor polypeptide synthesis from those on receptor export, pulse-chase experiments were conducted. These studies indicate that EGF stimulates post-translational transport and processing of the receptor, and this stimulation can occur in the absence of new protein synthesis. Other studies show that EGF accelerates at least two slow events in receptor maturation--the deoxynojirimycin-sensitive processing in endoplasmic reticulum (ER) and the swainsonine-sensitive processing in golgi, suggesting that EGF may influence one or more of the rate determining steps that control receptor export from ER. Overall the results demonstrate that EGF controls EGF-receptor expression at multiple levels, viz. at transcriptional, pre-translational and post-translational pathways of receptor biosynthesis.


Asunto(s)
Northern Blotting , Factor de Crecimiento Epidérmico/farmacología , Regulación de la Expresión Génica/efectos de los fármacos , Aparato de Golgi/efectos de los fármacos , Humanos , Cinética , Proteínas de la Membrana/metabolismo , Proteínas Oncogénicas/metabolismo , Pruebas de Precipitina , Procesamiento Proteico-Postraduccional/efectos de los fármacos , Procesamiento Postranscripcional del ARN/efectos de los fármacos , Receptores ErbB/biosíntesis , Células Tumorales Cultivadas
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