RESUMO
The male albino rat testis and liver showed tissue modification upon exposure to phenobarbitol (PB), 24 mg/100 g of body weight, for about 3 weeks and upon staining of their sections with hematoxylin and eosin. In this procedure, the control liver showed normal hepatocytes with centrally placed nuclei, and the PB-treated hepatocyte showed degeneration of cytoplasm and nucleus, necrosis and fragmentation of nucleus, and pushing of nucleus to periphery. The control rat testis showed epithelial layer having broad seminiferous tubules, spermatids, mature spermatozoa, and lumen of seminiferous tubules, and the PB-treated rat testis showed degenerative and necrotic changes in seminiferous tubules and clumping of seminiferous tubules. These changes almost returned to normal conditions in rat liver and testis upon the oral administration of an antioxidant that is present in Azadirachta seed-kernel extract (ASKE, 100 mg/kg body weight). In the case of enzymes, glutathione transferase and glutathione peroxidase were induced upon PB or ASKE treatment and the combination of both the treatments. The lipid peroxides were reduced in all the three cases in both liver and testis. The histological studies and enzymatic analysis revealed that the potential role of ASKE in the protection of the testis and liver tissues from PB-induced damage.
Assuntos
Azadirachta , Hepatócitos/efeitos dos fármacos , Fenobarbital/efeitos adversos , Fitoterapia/métodos , Extratos Vegetais/farmacologia , Substâncias Protetoras/farmacologia , Túbulos Seminíferos/efeitos dos fármacos , Testículo/efeitos dos fármacos , Administração Oral , Animais , Modelos Animais de Doenças , Relação Dose-Resposta a Droga , Peroxidação de Lipídeos/efeitos dos fármacos , Masculino , Ratos , Ratos WistarRESUMO
RNA helicases play important roles in cellular processes such as pre-mRNA splicing, rRNA processing, ribosomal biogenesis, and translation. A full-length DEAD box RNA helicase cDNA (CfrHlc113) was isolated from the spruce budworm, Choristoneura fumiferana. CfrHlc113 contained the eight functional motifs, which are highly conserved in the DEAD box RNA helicase family, and an arginine-serine-aspartate (RSD) domain at its N-terminal end. CfrHlc113 was highly homologous to Rattus norvegicus HEL117 and human prp5 genes, both of which are suggested to be involved in RNA splicing. The results of Northern and Western blotting showed that expression of the CfrHlc113 gene was low or undetectable in eggs, larvae, pupae, and adults. High levels of expression were, however, detected in the three in vitro cultured cell lines, CF-203, CF-124T, and CF-70, which were developed from the midgut, ovaries, and neonate larvae, respectively. Immunocytochemistry revealed that CfrHlc113 protein was present exclusively in the nuclei of these cell lines.
Assuntos
Lepidópteros/enzimologia , RNA Helicases/genética , Motivos de Aminoácidos , Sequência de Aminoácidos , Animais , Sequência de Bases , Northern Blotting , Western Blotting , Clonagem Molecular , Feminino , Imunofluorescência , Lepidópteros/genética , Dados de Sequência Molecular , Filogenia , RNA Helicases/química , RNA Mensageiro/química , RNA Mensageiro/genética , Proteínas Recombinantes/genética , Reação em Cadeia da Polimerase Via Transcriptase Reversa , Alinhamento de SequênciaRESUMO
A spruce budworm (Choristoneura fumiferana) transferrin cDNA (CfTf) was isolated and cloned from a cDNA library that was constructed using mRNA from fifth to sixth instar larvae. CfTf cDNA encoded a predicted protein of 681 amino acids with a molecular mass of approximately 76 kDa. CfTf shared 72% and 74% identities at the amino acid level with transferrins of Manduca sexta and Bombyx mori, respectively. Like other transferrins, CfTf retains most of the N-terminal, iron-binding amino acid residues. Northern blot analyses indicated that CfTf mRNA was present at high levels after ecdysis, but that the expression level was low prior to ecdysis at the fourth-sixth instar stages. The highest level of CfTf expression was detected in the fat body. Relatively low levels of expression were detected in the epidermis and no expression was found in the midgut. Expression of CfTf mRNA could be induced by bacteria but not fungi. Expression of CfTf mRNA was suppressed by iron load.
