RESUMO
Objective To investigate the RADIL mRNA expression in pancreatic carcinoma and to evaluate its clinical significance.Methods Fluoesecent quantitative PCR (FQ-PCR) was used to detect the RADIL mRNA expression in 40 patients with pancreatic carcinoma and adjacent tissue and in 5 healthy adult with normal pancreatic tissue and to observe its relationship with clinicopathologic parameters.Results RADIL mRNA was expressed in pancreatic carcinoma and adjacent tissue, as well as normal pancreatic tissue, and the relative expression was 2.263 ± 3.826, 5.425 ± 8.858 and 8.559 ± 4.214, respectively.There was statistically significant difference among the three groups (P ＜0.05 ).RADIL mRNA expression was closely related with the metastasis and differentiation grade ( r = -0.312 and -0.294, P ＜ 0.05 ), however, it was not significantly related to tumor site, tumor size, CA19-9, TNM staging, sex and age.Conclusions RADIL gene may have an inhibitory effect on the pancreatic cancer.
RESUMO
Low molecular weight GTP-binding proteins are molecular switches that are believed to play pivotal roles in cell growth, differentiation, cytoskeletal organization, and vesicular trafficking. Rab proteins are key players in the regulation of vesicular transport, while Rho family members control actin-dependent cell functions, i.e. the regulation of cytoskeletal organization in response to extracelluar growth factors and in dendritic neuron development. In this study, we have examined the regulation of small GTP-binding proteins that are implicated in neurosecretion and differentiation of neuron during ageing processes. Comparison of small GTP-binding proteins from the synaptosome and crude synaptic vesicles (LP2 membranes) of 2 months and 20 months old rat brain respectively showed no difference in the level of Rab family proteins (Rab3A and Rab5A). However, Rho family proteins such as RhoA and Cdc42 were elevated in LP2 membranes of the aged brain. The dissociation of Rab3A by Ca2+/calmodulin (CaM) from SV membranes was not changed during aging. Ca2+/CaM stimulated phosphorylation of the 22 and 55-kDa proteins in SV membranes from the aged rat brain, and inhibited phosporylation of 30-kDa proteins. GTPgammaS inhibited phosphorylation of the 100-kDa proteins and stimulated phosphorylation of the 70 kDa in LP2 membranes from both the young and aged rat brains, whereas GDPbetaS caused just the opposite reaction. These results suggest that protein phosphorylation and regulation of Rho family GTPases in rat brain appears to be altered during ageing processes.
Assuntos
Bovinos , Ratos , Envelhecimento , Animais , Encéfalo/metabolismo , Cálcio/farmacologia , Estudo Comparativo , Proteínas de Ligação ao GTP/metabolismo , Guanosina 5'-O-(3-Tiotrifosfato)/metabolismo , Peso Molecular , Fosforilação/efeitos dos fármacos , Ratos Sprague-Dawley , Membranas Sinápticas/metabolismo , Sinaptossomos/metabolismo , Proteína cdc42 de Ligação ao GTP/biossíntese , Proteína rab3A de Ligação ao GTP/metabolismo , Proteínas rab5 de Ligação ao GTP/metabolismo , Proteína rhoA de Ligação ao GTP/biossínteseRESUMO
Low molecular weight GTP-binding proteins are molecular switches that are believed to play pivotal roles in cell growth, differentiation, cytoskeletal organization, and vesicular trafficking. Rab proteins are key players in the regulation of vesicular transport, while Rho family members control actin-dependent cell functions, i.e. the regulation of cytoskeletal organization in response to extracelluar growth factors and in dendritic neuron development. In this study, we have examined the regulation of small GTP-binding proteins that are implicated in neurosecretion and differentiation of neuron during ageing processes. Comparison of small GTP-binding proteins from the synaptosome and crude synaptic vesicles (LP2 membranes) of 2 months and 20 months old rat brain respectively showed no difference in the level of Rab family proteins (Rab3A and Rab5A). However, Rho family proteins such as RhoA and Cdc42 were elevated in LP2 membranes of the aged brain. The dissociation of Rab3A by Ca2+/calmodulin (CaM) from SV membranes was not changed during aging. Ca2+/CaM stimulated phosphorylation of the 22 and 55-kDa proteins in SV membranes from the aged rat brain, and inhibited phosporylation of 30-kDa proteins. GTPgammaS inhibited phosphorylation of the 100-kDa proteins and stimulated phosphorylation of the 70 kDa in LP2 membranes from both the young and aged rat brains, whereas GDPbetaS caused just the opposite reaction. These results suggest that protein phosphorylation and regulation of Rho family GTPases in rat brain appears to be altered during ageing processes.