RESUMO
PURPOSE: To compare quality of life and functional outcomes associated with orthotopic neobladder (ONB) and ileal conduit (IC) after anterior pelvic exenteration for bladder cancer in women, through a multicentric cross-sectional study. METHODS: All women who have undergone an anterior pelvic exenteration associated with ONB or IC for a bladder cancer between January 2004 and December 2014 within the three participating university hospital centers and that were still alive in February 2016 were included. Three distinct auto-administered questionnaires were submitted to the patients: the EORTC QLQ-C30, the EORTC QLQ-BLmi30 and the SF-12. Comparison of response to these questionnaires between women with ONB and those with IC were studied with Mann-Whitney U tests, with a statistically significant P-value set at<0.05. The primary endpoint was the "global health status" sub-score extracted from the EORTC QLQ-C30 questionnaire. The secondary endpoints were the functional sub-scores and symptoms sub-scores obtained with the EORTC QLQ-C30 questionnaire as well as the sub-scores obtained with the EORTC QLQ-BLmi30 and the SF-12 questionnaires. RESULTS: Forty women were included in the study (17 ONB, 23 IC). The primary endpoint was comparable between the ONB and IC women (83.3 vs. 66.7 P=0.22). Similarly, no significant statistical difference could be pointed between the ONB and IC women in terms of secondary endpoints. CONCLUSION: The present study did not report any significance difference in terms of quality of life and functional outcomes between women with ONB and those with IC after pelvic exenteration for bladder cancer. LEVEL OF EVIDENCE: 3.
Assuntos
Qualidade de Vida , Neoplasias da Bexiga Urinária/cirurgia , Derivação Urinária/métodos , Coletores de Urina , Idoso , Idoso de 80 Anos ou mais , Estudos Transversais , Feminino , Humanos , Pessoa de Meia-Idade , Inquéritos e QuestionáriosRESUMO
In higher vertebrates, the glycolytic enzyme enolase (2-phospho-D-glycerate hydrolyase; EC 4.2.1.11) is active as a dimeric protein formed from three subunits--alpha: ubiquitous, beta: muscle specific, and gamma: neuron specific--encoded by different genes. In the present study, we have shown that an antiserum previously produced against the mouse beta beta enolase is also a specific reagent for the muscle specific human enolase. Using this antiserum to study human muscles, we demonstrated novel patterns of the beta subunit microheterogeneity which are distinctive from those observed previously in rodents and which appear to be independent of age, gender and muscular activity. Two variants of the beta subunit differing by their size have been detected: one heavy form of 46 kDa (beta H) and one light form of 45 kDa (beta L). Muscle biopsies expressed either beta H or beta L or beta H + beta L, and all muscles of an individual expressed the same variants. The products of in vitro translation of RNA prepared from human muscle displayed beta subunit variants identical to those of the protein present in the biopsy. Therefore the differences observed between individuals reveal a difference already present at the level of the RNA transcripts. These observations suggest the existence of an yet undescribed polymorphism of the human beta enolase gene which could affect the coding sequence. Comparative immunocytochemical and histochemical analyses of biopsies demonstrated that the beta subunit was expressed in all fast fibres (type II), but not in slow fibres (type I). No difference was observed in the intensity of beta enolase immunolabelling between the various types (IIA, IIAB, IIB) of fast fibres. No significant difference in fibre type composition and histological appearance was visible between muscles presenting either one of the three patterns of microheterogeneity.
Assuntos
Variação Genética/genética , Fibras Musculares Esqueléticas/enzimologia , Músculo Esquelético/enzimologia , Fosfopiruvato Hidratase/genética , Adulto , Idoso , Animais , Pré-Escolar , Feminino , Humanos , Masculino , Camundongos , Pessoa de Meia-Idade , Fibras Musculares Esqueléticas/fisiologia , Músculo Esquelético/fisiologiaRESUMO
cDNA clones corresponding to subunits of neuron-specific (gamma gamma and alpha gamma) and non-neuronal (alpha alpha) enolase isozymes were characterized from two mouse brain cDNA libraries. Our hybridization data revealed a partial homology of the coding sequences of mouse alpha, mouse gamma and rat gamma mRNAs. The noncoding sequences, however, appear to be specific for each mouse mRNA. Although coding for two polypeptides of the same molecular weight, the mRNA for the gamma subunit (2600 bases) is larger than that for the alpha subunit (1900 bases). The noncoding sequences for neuron-specific gamma mRNA (about 1300 bases) are therefore longer than those of the non-nervous tissue specific alpha mRNA (about 600 bases).
Assuntos
Neurônios/enzimologia , Fosfopiruvato Hidratase/genética , Animais , Clonagem Molecular , DNA/genética , Camundongos , Peso Molecular , Família Multigênica , Hibridização de Ácido Nucleico , Biossíntese de Proteínas , RNA Mensageiro/genéticaRESUMO
A specific event which accompanies the terminal differentiation of most neurons is the isozymic enolase transition from the ?? form to the ?? and ?? adult neuronal forms. It is partly expressed during maturation of a mouse neuroblastoma clonal cell line (NIE-115). We demonstrate, in these cell cultures, that the significant increase in the concentration of ? gene product, expressed as ?? enolase during differentiation, is due to a parallel and similar increase in its synthesis. The capacities of poly (A)(+) RNA from undifferentiated and differentiated cultures to direct the synthesis of ? gene product were compared in a reticulocyte cell-free protein-synthesizing system. This translating capacity is stimulated in the same proportion as the rate of synthesis of ? antigen in differentiating cell cultures. Therefore the increase in the level of ? protein (expressed mostly as ?? enolase) during differentiation results from the increased translating activity or relative amount of ?mRNA.
RESUMO
Using the rabbit reticulocyte cell-free translation system we have estimated during ontogenesis the proportions of in vitro translatable alpha and gamma brain enolase mRNAs, which are two minor mRNA species. No polypeptide precursor to these enzyme subunits appears to be synthesized during translation in vitro. During brain development, the changes in translatable alpha and gamma mRNA content seem to parallel those of the corresponding antigens. The proportion of each of the enolase mRNAs is highest in adult mouse brain. Mechanisms controlling alpha and gamma antigen expression are discussed. In order to prepare the specific cDNA probes, purification of alpha and gamma mRNAs was undertaken.
Assuntos
Encéfalo/enzimologia , Encéfalo/crescimento & desenvolvimento , Fosfopiruvato Hidratase/genética , RNA Mensageiro/genética , RNA Mensageiro/metabolismo , Animais , Antígenos/biossíntese , Antígenos/genética , Encéfalo/imunologia , Sistema Livre de Células , Regulação da Expressão Gênica no Desenvolvimento , Regulação Enzimológica da Expressão Gênica , Técnicas In Vitro , Isoenzimas/biossíntese , Isoenzimas/genética , Isoenzimas/imunologia , Camundongos , Fosfopiruvato Hidratase/biossíntese , Fosfopiruvato Hidratase/imunologia , Biossíntese de Proteínas , Coelhos , Ratos , Ratos Sprague-Dawley , Reticulócitos/metabolismoRESUMO
An analysis of enolase expression during differentiation of neuroblastoma clones in homogeneous culture is presented. The enolases expressed in these neuroblast-like cells are identical to those of mouse brain with respect to the examined properties. Our biochemical investigation has premitted us to demonstrate formally that neuroblastoma cells undergo a transition from the embryonic ?? form to the neuronal ?? form and contain both enolases as well as the ?? hybrid form during maturation. These results suggest that the same phenomenon must exist in vivo for neuroblasts. In neuroblastoma cells, an increase in both ?? and ?? neuron specific enolases is related to cell maturation and expression of the ?? form precedes that of the ?? form during differentiation. Modulation of neuronal enolase activities is similar in the various conditions of differentiation studied and appears not to be necessarily related with morphological differentiation, although concomitant with an arrest of cell division. The evolution of specific neuronal enolases in neuroblastoma cells parallels that observed in vivo, in brain from embryonic day 15 to post-natal day 7. Moreover, at least one treatment (dimethylsulfoxide) causes an important decrease in the high specific ?? activity of these cells as occurs in vivo. This enolase can therefore also be considered as a biochemical marker for neuroblastoma maturation. As observed with other markers and other cell types, neuroblastoma cells in culture express an immature biochemical differentiation of the enolase isozymes.