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1.
West China Journal of Stomatology ; (6): 510-517, 2021.
Article in English | WPRIM | ID: wpr-921367

ABSTRACT

OBJECTIVES@#This study aims to investigate the effect of RhoE expression on the migration and invasion of tongue squamous cell carcinoma (TSCC).@*METHODS@#Forty-eight TSCC cases were selected from the Maxillofacial Surgery Center of Qingdao Municipal Hospital from 2017 to 2019. The expression of RhoE in the specimens (TSCC and adjacent tissues) was detected by immunohistochemistry, and RhoE mRNA and protein were extracted to further detect the expression of RhoE. SCC-4 and CAL-27 cells were selected for @*RESULTS@#The expression level of RhoE in TSCC was significantly lower than that in adjacent tissues (@*CONCLUSIONS@#RhoE expression is low in TSCC. Over expression RhoE in TSCC can significantly decrease its migration and invasion abilities. Hence, RhoE may play an important role in regulating the metastasis and invasion of TSCC and provide a new target for gene therapy.


Subject(s)
Humans , Carcinoma, Squamous Cell , Cell Line, Tumor , Matrix Metalloproteinase 2 , Neoplasm Invasiveness , Tongue , Tongue Neoplasms , rho GTP-Binding Proteins/genetics , rho-Associated Kinases
2.
Mem. Inst. Oswaldo Cruz ; 101(supl.1): 323-326, Oct. 2006. graf, ilus
Article in English | LILACS | ID: lil-441267

ABSTRACT

In a previous study, the Schistosoma mansoni Rho1 protein was able to complement Rho1 null mutant Saccharomyces cerevisiae cells at restrictive temperatures and under osmotic stress (low calcium concentration) better than the human homologue (RhoA). It is known that under osmotic stress, the S. cerevisiae Rho1 triggers two distinct pathways: activation of the membrane 1,3-beta-glucan synthase enzymatic complex and activation of the protein kinase C1 signal transduction pathway, promoting the transcription of response genes. In the present work the SmRho1 protein and its mutants smrho1E97P, smrho1L101T, and smrho1E97P, L101T were used to try to clarify the basis for the differential complementation of Rho1 knockout yeast strain by the human and S. mansoni genes. Experiments of functional complementation in the presence of caffeine and in the presence of the osmotic regulator sorbitol were conducted. SmRho1 and its mutants showed a differential complementation of the yeast cells in the presence of caffeine, since smrho1E97P and smrho1E97P, L101T mutants showed a delay in the growth when compared to the yeast complemented with the wild type SmRho1. However, in the presence of sorbitol and caffeine the wild type SmRho1 and mutants showed a similar complementation phenotype, as they allowed yeast growth in all caffeine concentrations tested.


Subject(s)
Animals , Humans , Caffeine/pharmacology , Protein Kinase C/genetics , Saccharomyces cerevisiae Proteins/genetics , Saccharomyces cerevisiae/genetics , Schistosoma mansoni/genetics , rho GTP-Binding Proteins/genetics , Genes, Helminth , Mutation , Saccharomyces cerevisiae Proteins/metabolism , Saccharomyces cerevisiae/drug effects , Saccharomyces cerevisiae/metabolism , Schistosoma mansoni/metabolism , Signal Transduction/genetics , rho GTP-Binding Proteins/metabolism
3.
Experimental & Molecular Medicine ; : 358-366, 2004.
Article in English | WPRIM | ID: wpr-119640

ABSTRACT

The rearrangement of the actin cytoskeleton has been shown to play a critical role in the development of transformation and malignant phenotype of cancer cells. Rho family GTPases regulate the arrangement of the actin cytoskeleton. By wound-healing assay, we have found that NIH 3T3 fibroblast cells move towards the wound- gaps by extending filopodial and lamellipdial structures at the leading edge of the moving cells. We have inactivated the function of Rho GTPases of v-Ras transformed NIH 3T3 cells by overexpressing Rho GTPase-activating (RhoGAP) domain of RhoGAP of p190. We have observed that inactivation of Rho, Rac and Cdc42 GTPases by overexpressing RHG causes inhibition of: (i) polymerization of actin to form filaments, (ii) formation of lamellipodia, filopodia and stress fibres, (iii) cell motility, (iv) cell spreading and (v) cell-to-cell adhesions. These results further strengthen the current knowledge on the role of Rho, Rac and Cdc42 GTPases in the regulation of the rearrangement of actin cytoskeleton. Our results, for the first time, demonstrate that RhoGAP domain of RhoGAP could be used to study the molecular mechanism of Ras-mediated signalling in growth, differentiation and carcinogenesis.


Subject(s)
Animals , Mice , Biological Assay , Cell Line, Transformed , Cell Movement/physiology , Cell Transformation, Neoplastic/ultrastructure , Actin Cytoskeleton/metabolism , NIH 3T3 Cells , Wound Healing , rho GTP-Binding Proteins/genetics
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