Base de dados : MEDLINE
Pesquisa : D08.811.277.040.330.300.400.700.200 [Categoria DeCS]
Referências encontradas : 4738 [refinar]
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[PMID]:29337059
[Au] Autor:Lin L; Li M; Lin L; Xu X; Jiang G; Wu L
[Ad] Endereço:Department of Thoracic Surgery, Shanghai Pulmonary Hospital, Tongji University School of Medicine, Shanghai 200433, China; Tongji University School of Medicine, Shanghai 200092, China.
[Ti] Título:FPPS mediates TGF-ß1-induced non-small cell lung cancer cell invasion and the EMT process via the RhoA/Rock1 pathway.
[So] Source:Biochem Biophys Res Commun;496(2):536-541, 2018 02 05.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Farnesyl pyrophosphate synthase (FPPS), a key enzyme in the mevalonate pathway, was recently shown to play a role in cancer progression. However, its role in non-small cell lung cancer (NSCLC) metastasis and the underlying mechanism remain unclear. In this study, FPPS expression was significantly correlated with TNM stage, and metastasis. Inhibition or knockdown of FPPS blocked TGF-ß1-induced cell invasion and epithelial-to-mesenchymal transition (EMT) process. FPPS expression of FPPS was induced by TGF-ß1 and FPPS promoted cell invasion and EMT via the RhoA/Rock1 pathway. In conclusion, FPPS mediates TGF-ß1-induced lung cancer cell invasion and EMT via the RhoA/Rock1 pathway. These findings suggest new treatment strategies to reduce mortality associated with metastasis in patients with NSCLC.
[Mh] Termos MeSH primário: Carcinoma Pulmonar de Células não Pequenas/metabolismo
Transição Epitelial-Mesenquimal
Geraniltranstransferase/metabolismo
Neoplasias Pulmonares/metabolismo
Fator de Crescimento Transformador beta1/metabolismo
Quinases Associadas a rho/metabolismo
Proteína rhoA de Ligação ao GTP/metabolismo
[Mh] Termos MeSH secundário: Idoso
Carcinoma Pulmonar de Células não Pequenas/genética
Carcinoma Pulmonar de Células não Pequenas/patologia
Linhagem Celular Tumoral
Feminino
Regulação Neoplásica da Expressão Gênica
Geraniltranstransferase/análise
Geraniltranstransferase/genética
Seres Humanos
Pulmão/metabolismo
Pulmão/patologia
Neoplasias Pulmonares/genética
Neoplasias Pulmonares/patologia
Masculino
Meia-Idade
Invasividade Neoplásica/genética
Invasividade Neoplásica/patologia
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Transforming Growth Factor beta1); EC 2.5.1.10 (Geranyltranstransferase); EC 2.7.11.1 (ROCK1 protein, human); EC 2.7.11.1 (rho-Associated Kinases); EC 3.6.5.2 (rhoA GTP-Binding Protein)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180117
[St] Status:MEDLINE


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[PMID]:29373579
[Au] Autor:Schrade K; Tröger J; Eldahshan A; Zühlke K; Abdul Azeez KR; Elkins JM; Neuenschwander M; Oder A; Elkewedi M; Jaksch S; Andrae K; Li J; Fernandes J; Müller PM; Grunwald S; Marino SF; Vukicevic T; Eichhorst J; Wiesner B; Weber M; Kapiloff M; Rocks O; Daumke O; Wieland T; Knapp S; von Kries JP; Klussmann E
[Ad] Endereço:Max Delbrück Center for Molecular Medicine Berlin (MDC), Berlin, Germany.
[Ti] Título:An AKAP-Lbc-RhoA interaction inhibitor promotes the translocation of aquaporin-2 to the plasma membrane of renal collecting duct principal cells.
[So] Source:PLoS One;13(1):e0191423, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Stimulation of renal collecting duct principal cells with antidiuretic hormone (arginine-vasopressin, AVP) results in inhibition of the small GTPase RhoA and the enrichment of the water channel aquaporin-2 (AQP2) in the plasma membrane. The membrane insertion facilitates water reabsorption from primary urine and fine-tuning of body water homeostasis. Rho guanine nucleotide exchange factors (GEFs) interact with RhoA, catalyze the exchange of GDP for GTP and thereby activate the GTPase. However, GEFs involved in the control of AQP2 in renal principal cells are unknown. The A-kinase anchoring protein, AKAP-Lbc, possesses GEF activity, specifically activates RhoA, and is expressed in primary renal inner medullary collecting duct principal (IMCD) cells. Through screening of 18,431 small molecules and synthesis of a focused library around one of the hits, we identified an inhibitor of the interaction of AKAP-Lbc and RhoA. This molecule, Scaff10-8, bound to RhoA, inhibited the AKAP-Lbc-mediated RhoA activation but did not interfere with RhoA activation through other GEFs or activities of other members of the Rho family of small GTPases, Rac1 and Cdc42. Scaff10-8 promoted the redistribution of AQP2 from intracellular vesicles to the periphery of IMCD cells. Thus, our data demonstrate an involvement of AKAP-Lbc-mediated RhoA activation in the control of AQP2 trafficking.
[Mh] Termos MeSH primário: Proteínas de Ancoragem à Quinase A/metabolismo
Aquaporina 2/metabolismo
Membrana Celular/metabolismo
Túbulos Renais Coletores/citologia
Antígenos de Histocompatibilidade Menor/metabolismo
Proteínas Proto-Oncogênicas/metabolismo
Bibliotecas de Moléculas Pequenas/farmacologia
Proteína rhoA de Ligação ao GTP/metabolismo
[Mh] Termos MeSH secundário: Membrana Celular/efeitos dos fármacos
Células HEK293
Seres Humanos
Ligação Proteica/efeitos dos fármacos
Transporte Proteico/efeitos dos fármacos
Bibliotecas de Moléculas Pequenas/química
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (A Kinase Anchor Proteins); 0 (AKAP13 protein, human); 0 (Aquaporin 2); 0 (Minor Histocompatibility Antigens); 0 (Proto-Oncogene Proteins); 0 (Small Molecule Libraries); EC 3.6.5.2 (rhoA GTP-Binding Protein)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180127
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191423


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[PMID]:29307655
[Au] Autor:Chang X; Li H; Li Y; He Q; Yao J; Duan T; Wang K
[Ad] Endereço:Clinical and Translational Research Center, Shanghai First Maternity and Infant Hospital, Tongji University School of Medicine, Shanghai, 200040, PR China.
[Ti] Título:RhoA/MLC signaling pathway is involved in Δ9-tetrahydrocannabinol-impaired placental angiogenesis.
[So] Source:Toxicol Lett;285:148-155, 2018 Mar 15.
[Is] ISSN:1879-3169
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Cannabis is a widely used illicit drug and its abuse during pregnancy has been related to adverse reproductive outcomes. In addition, placental angiogenesis is considered to be responsible for the transport of nutrients critical for placental development and fetal growth. The purpose of this study is to determine the effects of Δ9-tetrahydrocannabinol (THC), the major component of cannabis, on placental angiogenesis, involving endothelial cell (EC) proliferation, migration and tube formation. Here, we observe dramatic alterations in placental vascular network of cannabis users correlated with an impaired HUVE cell proliferation, migration and tube formation after treated with THC. Mechanistically, the activity of RhoA/MLC is involved in the THC-impaired EC migration and angiogenesis. To further analyze the role of cannabis in mice placental and embryonic development, we inject pregnant mice with THC daily. This treatment results in an altered placental microvasculature, accompanied by the decreased expression of CD31 and activity of RhoA/MLC. Taken together, these findings identify THC plays a pivotal role in impairing placental angiogenesis potentially via RhoA/MLC signaling nexus.
[Mh] Termos MeSH primário: Dronabinol/toxicidade
Cadeias Leves de Miosina/metabolismo
Neovascularização Fisiológica/efeitos dos fármacos
Placenta/efeitos dos fármacos
Proteína rhoA de Ligação ao GTP/metabolismo
[Mh] Termos MeSH secundário: Animais
Movimento Celular/efeitos dos fármacos
Proliferação Celular/efeitos dos fármacos
Feminino
Células Endoteliais da Veia Umbilical Humana
Seres Humanos
Camundongos Endogâmicos C57BL
Microvasos/efeitos dos fármacos
Microvasos/metabolismo
Placenta/irrigação sanguínea
Placenta/metabolismo
Gravidez
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Myosin Light Chains); 7J8897W37S (Dronabinol); EC 3.6.5.2 (rhoA GTP-Binding Protein)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180219
[Lr] Data última revisão:
180219
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180109
[St] Status:MEDLINE


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[PMID]:29247652
[Au] Autor:Miyamoto S; Nagamura Y; Nakabo A; Okabe A; Yanagihara K; Fukami K; Sakai R; Yamaguchi H
[Ad] Endereço:Department of Cancer Cell Research, Sasaki Institute, Sasaki Foundation, 2-2 Kandasurugadai, Chiyoda-ku, Tokyo 101-0062, Japan.
[Ti] Título:Aberrant alternative splicing of RHOA is associated with loss of its expression and activity in diffuse-type gastric carcinoma cells.
[So] Source:Biochem Biophys Res Commun;495(2):1942-1947, 2018 01 08.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:RhoA is a member of Rho family small GTPases that regulates diverse cellular functions. Recent large-scale sequencing studies have identified recurrent somatic mutations of RHOA in diffuse-type gastric carcinoma (DGC), indicating that RHOA is a driver of DGC. In this study, we investigated the possible abnormalities of RHOA in a panel of gastric carcinoma (GC) cell lines. Pulldown assay and immunoblot analysis showed that the activity and expression of RhoA were detectable in all GC cell lines tested, except for two DGC cell lines, HSC-59 and GSU. RHOA coding region sequencing revealed that aberrant alternative splicing of RHOA occurred in these cell lines. Quantitative real-time PCR analysis showed that the expression of wild-type RHOA was nearly undetectable, whereas splicing variants were almost exclusively expressed in HSC-59 and GSU cell lines. However, the expression levels of RHOA splicing variants were very low and the corresponding proteins were not detected by immunoblotting. Moreover, the splicing isoforms of RhoA protein were neither efficiently expressed nor activated even if ectopically expressed in cells. These results indicate that aberrant alternative splicing of RHOA results in the loss of its activity and expression in DGC cells.
[Mh] Termos MeSH primário: Processamento Alternativo/genética
Regulação Neoplásica da Expressão Gênica/genética
Isoformas de Proteínas/genética
Neoplasias Gástricas/enzimologia
Neoplasias Gástricas/genética
Proteína rhoA de Ligação ao GTP/genética
[Mh] Termos MeSH secundário: Linhagem Celular Tumoral
Ativação Enzimática/genética
Seres Humanos
Mutação/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Protein Isoforms); 124671-05-2 (RHOA protein, human); EC 3.6.5.2 (rhoA GTP-Binding Protein)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180214
[Lr] Data última revisão:
180214
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171217
[St] Status:MEDLINE


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[PMID]:28743511
[Au] Autor:Yang L; Tang L; Dai F; Meng G; Yin R; Xu X; Yao W
[Ad] Endereço:School of pharmacy, Nantong University, 19 QiXiu Road, Nantong 226001, China.
[Ti] Título:Raf-1/CK2 and RhoA/ROCK signaling promote TNF-α-mediated endothelial apoptosis via regulating vimentin cytoskeleton.
[So] Source:Toxicology;389:74-84, 2017 08 15.
[Is] ISSN:1879-3185
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:Both RhoA/ROCK and Raf-1/CK2 pathway play essential roles in cell proliferation, apoptosis, differentiation, and multiple other common cellular functions. We previously reported that vimentin is responsible for TNF-α-induced cell apoptosis. Herein, we investigated the regulation of RhoA/ROCK and Raf-1/CK2 signaling on vimentin filaments and endothelial apoptosis mediated by TNF-α. Treatment with TNF-α significantly induced the activation of RhoA and ROCK, and the expression of ROCK1. RhoA deficiency could obviously inhibit ROCK activation and ROCK1 expression induced by TNF-α. Both RhoA deficiency and ROCK activity inhibition (Y-27632) greatly inhibited endothelial apoptosis and preserved cell viability in TNF-α-induced human umbilical vein endothelial cells (HUVECs). Also vimentin phosphorylation and the remodeling of vimentin or phospho-vimentin induced by TNF-α were obviously attenuated by RhoA suppression and ROCK inhibition. TNF-α-mediated vimentin cleavage was significantly inhibited by RhoA suppression and ROCK inhibition through decreasing the activation of caspase3 and 8. Furthermore, TNF-α treatment greatly enhanced the activation of Raf-1. Suppression of Raf-1 or CK2 by its inhibitor (GW5074 or TBB) blocked vimentin phosphorylation, remodeling and endothelial apoptosis, and preserved cell viability in TNF-α-induced HUVECs. However, Raf-1 inhibition showed no significant effect on TNF-α-induced ROCK expression and activation, suggesting that the regulation of Raf-1/CK2 signaling on vimentin was independent of ROCK. Taken together, these results indicate that both RhoA/ROCK and Raf-1/CK2 pathway are responsible for TNF-α-mediated endothelial cytotoxicity via regulating vimentin cytoskeleton.
[Mh] Termos MeSH primário: Apoptose/efeitos dos fármacos
Caseína Quinase II/metabolismo
Citoesqueleto/efeitos dos fármacos
Células Endoteliais da Veia Umbilical Humana/efeitos dos fármacos
Proteínas Proto-Oncogênicas c-raf/metabolismo
Fator de Necrose Tumoral alfa/toxicidade
Vimentina/metabolismo
Quinases Associadas a rho/metabolismo
Proteína rhoA de Ligação ao GTP/metabolismo
[Mh] Termos MeSH secundário: Caseína Quinase II/antagonistas & inibidores
Sobrevivência Celular/efeitos dos fármacos
Células Cultivadas
Citoesqueleto/enzimologia
Citoesqueleto/patologia
Células Endoteliais da Veia Umbilical Humana/enzimologia
Células Endoteliais da Veia Umbilical Humana/patologia
Seres Humanos
Fosforilação
Inibidores de Proteínas Quinases/farmacologia
Proteínas Proto-Oncogênicas c-raf/antagonistas & inibidores
Interferência de RNA
Transdução de Sinais/efeitos dos fármacos
Transfecção
Proteína cdc42 de Ligação ao GTP/genética
Proteína cdc42 de Ligação ao GTP/metabolismo
Quinases Associadas a rho/antagonistas & inibidores
Proteína rhoA de Ligação ao GTP/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Protein Kinase Inhibitors); 0 (Tumor Necrosis Factor-alpha); 0 (Vimentin); 124671-05-2 (RHOA protein, human); EC 2.7.11.1 (Casein Kinase II); EC 2.7.11.1 (Proto-Oncogene Proteins c-raf); EC 2.7.11.1 (ROCK1 protein, human); EC 2.7.11.1 (rho-Associated Kinases); EC 3.6.5.2 (cdc42 GTP-Binding Protein); EC 3.6.5.2 (rhoA GTP-Binding Protein)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:180122
[Lr] Data última revisão:
180122
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170727
[St] Status:MEDLINE


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[PMID]:29179184
[Au] Autor:Yue H; Bin L; Chaoying C; Meng Z; Meng L; Xi W
[Ti] Título:Potential Regulatory Effects of Corticotropin-Releasing Factor on Tight Junction-Related Intestinal Epithelial Permeability are Partially Mediated by CK8 Upregulation.
[So] Source:Cell Physiol Biochem;44(3):1161-1173, 2017.
[Is] ISSN:1421-9778
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:BACKGROUND/AIMS: Intestinal permeability and stress have been implicated in the pathophysiology of irritable bowel syndrome (IBS). Cytokeratin 8 (CK8), for the first time, has been shown to mediate corticotropin-releasing factor (CRF)-induced changes in intestinal permeability in animal models of IBS. In this study, we investigated the regulatory effects of CRF on the permeability of human intestinal epithelial cells through the CK8-mediated tight junction. METHODS: The expression levels of corticotropin-releasing factor receptor 1 (CRFR1) and corticotropin-releasing factor receptor 2 (CRFR2) on the HT29 cell surface were determined by immunofluorescence, RT-PCR, and Western blotting. After treatment with 100 nM CRF for 72 h, the translocation of FITC-labelled dextran was measured in a transwell chamber; the structural changes of tight junctions were observed under transmission electron microscopy; the expression levels of CK8, F-actin and tight junction proteins ZO-1, claudin-1, and occludin were detected by immunoblotting and immunofluorescence. The activity of RhoA was detected by immunoprecipitation. Furthermore, the effects of CRF on intestinal epithelial permeability were examined in CK8-silenced HT29 cells, which were constructed by shRNA interference. RESULTS: CRF treatment increased FITC-labelled dextran permeability, caused the opening of tight junctions, induced increased fluorescence intensity of CK8 and decreased the intensities of ZO-1, claudin-1, and occludin, together with structural disruption. The expression levels of F-actin, occludin, claudin-1, and ZO-1 were downregulated. RhoA activity peaked at 30 min after CRF treatment. CRF-induced increased permeability, and downregulation of claudin-1 and occludin were not blocked by CK8 silencing. Nevertheless, CK8 silencing blocked the effects of CRF regarding the decrease in the expression levels of F-action and ZO-1 and increase in RhoA activity. CONCLUSION: CRF may increase intestinal epithelial permeability by upregulating CK8 expression, activating the RhoA signalling pathway, promoting intestinal epithelial actin remodelling, and decreasing the expression of the tight junction protein ZO-1. Other CK8-independent pathways may be involved in the downregulation of claudin-1 and occludin, which might also contribute to increased intestinal epithelial permeability.
[Mh] Termos MeSH primário: Hormônio Liberador da Corticotropina/farmacologia
Queratina-8/metabolismo
Permeabilidade/efeitos dos fármacos
Receptores de Hormônio Liberador da Corticotropina/metabolismo
Junções Íntimas/efeitos dos fármacos
Regulação para Cima/efeitos dos fármacos
[Mh] Termos MeSH secundário: Actinas/metabolismo
Claudina-1/metabolismo
Células HT29
Seres Humanos
Mucosa Intestinal/citologia
Mucosa Intestinal/metabolismo
Queratina-8/antagonistas & inibidores
Queratina-8/genética
Microscopia Eletrônica
Microscopia de Fluorescência
Ocludina/metabolismo
Interferência de RNA
RNA Interferente Pequeno/metabolismo
Reação em Cadeia da Polimerase em Tempo Real
Receptores de Hormônio Liberador da Corticotropina/genética
Junções Íntimas/metabolismo
Junções Íntimas/ultraestrutura
Proteína da Zônula de Oclusão-1/metabolismo
Proteína rhoA de Ligação ao GTP/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Actins); 0 (CRF receptor type 1); 0 (CRF receptor type 2); 0 (Claudin-1); 0 (Keratin-8); 0 (Occludin); 0 (RNA, Small Interfering); 0 (Receptors, Corticotropin-Releasing Hormone); 0 (Zonula Occludens-1 Protein); 9015-71-8 (Corticotropin-Releasing Hormone); EC 3.6.5.2 (rhoA GTP-Binding Protein)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180118
[Lr] Data última revisão:
180118
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171128
[St] Status:MEDLINE
[do] DOI:10.1159/000485420


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[PMID]:28465529
[Au] Autor:Hasan MK; Yu J; Chen L; Cui B; Widhopf Ii GF; Rassenti L; Shen Z; Briggs SP; Kipps TJ
[Ad] Endereço:Moores Cancer Center, University of California San Diego, La Jolla, CA, USA.
[Ti] Título:Wnt5a induces ROR1 to complex with HS1 to enhance migration of chronic lymphocytic leukemia cells.
[So] Source:Leukemia;31(12):2615-2622, 2017 Dec.
[Is] ISSN:1476-5551
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:ROR1 (receptor tyrosine kinase-like orphan receptor 1) is a conserved, oncoembryonic surface antigen expressed in chronic lymphocytic leukemia (CLL). We found that ROR1 associates with hematopoietic-lineage-cell-specific protein 1 (HS1) in freshly isolated CLL cells or in CLL cells cultured with exogenous Wnt5a. Wnt5a also induced HS1 tyrosine phosphorylation, recruitment of ARHGEF1, activation of RhoA and enhanced chemokine-directed migration; such effects could be inhibited by cirmtuzumab, a humanized anti-ROR1 mAb. We generated truncated forms of ROR1 and found its extracellular cysteine-rich domain or kringle domain was necessary for Wnt5a-induced HS1 phosphorylation. Moreover, the cytoplamic, and more specifically the proline-rich domain (PRD), of ROR1 was required for it to associate with HS1 and allow for F-actin polymerization in response to Wnt5a. Accordingly, we introduced single amino acid substitutions of proline (P) to alanine (A) in the ROR1 PRD at positions 784, 808, 826, 841 or 850 in potential SH3-binding motifs. In contrast to wild-type ROR1, or other ROR1 mutants, ROR1 had impaired capacity to recruit HS1 and ARHGEF1 to ROR1 in response to Wnt5a. Moreover, Wnt5a could not induce cells expressing ROR1 to phosphorylate HS1 or activate ARHGEF1, and was unable to enhance CLL-cell motility. Collectively, these studies indicate HS1 plays an important role in ROR1-dependent Wnt5a-enhanced chemokine-directed leukemia-cell migration.
[Mh] Termos MeSH primário: Proteínas Sanguíneas/metabolismo
Movimento Celular/imunologia
Leucemia Linfocítica Crônica de Células B/imunologia
Leucemia Linfocítica Crônica de Células B/metabolismo
Complexos Multiproteicos/metabolismo
Receptores Órfãos Semelhantes a Receptor Tirosina Quinase/metabolismo
Proteína Wnt-5a/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Proteínas Sanguíneas/química
Quimiocinas/metabolismo
Seres Humanos
Fosforilação
Ligação Proteica
Domínios e Motivos de Interação entre Proteínas
Receptores Órfãos Semelhantes a Receptor Tirosina Quinase/química
Fatores de Troca de Nucleotídeo Guanina Rho/metabolismo
Células Tumorais Cultivadas
Proteína rhoA de Ligação ao GTP/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ARHGEF1 protein, human); 0 (Blood Proteins); 0 (Chemokines); 0 (HCLS1 protein, human); 0 (Multiprotein Complexes); 0 (Rho Guanine Nucleotide Exchange Factors); 0 (WNT5A protein, human); 0 (Wnt-5a Protein); EC 2.7.10.1 (ROR1 protein, human); EC 2.7.10.1 (Receptor Tyrosine Kinase-like Orphan Receptors); EC 3.6.5.2 (rhoA GTP-Binding Protein)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171215
[Lr] Data última revisão:
171215
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE
[do] DOI:10.1038/leu.2017.133


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[PMID]:29061808
[Au] Autor:Kim SM; Rhee YH; Kim JS
[Ad] Endereço:Department of Obstetrics and Gynecology, College of Medicine, Dankook University, Cheonan, Republic of Korea.
[Ti] Título:The Anticancer Effects of Radachlorin-mediated Photodynamic Therapy in the Human Endometrial Adenocarcinoma Cell Line HEC-1-A.
[So] Source:Anticancer Res;37(11):6251-6258, 2017 11.
[Is] ISSN:1791-7530
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:AIM: We investigated the effect of photodynamic therapy (PDT) using radachlorin on invasion, vascular formation and apoptosis by targeting epidermal growth factor receptor (EGFR)/vascular endothelial growth factor receptor 2 (VEGFR2) signaling pathways in the HEC-1-A endometrial adenocarcinoma cell line. MATERIALS AND METHODS: To investigate the apoptotic pathway, we performed the 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) assay, terminal deoxynucleotidyl transferase dUTP nick-end labeling (TUNEL) assay, and western blot analysis. We also evaluated the effects of PDT on tubular capillary formation in and invasion by HEC-1-A cells with a tube formation assay, invasion assay, prostaglandin E2 (PGE2) assay, and western blot analysis. RESULTS: PDT had anticancer effects on HEC-1-A through activation of the intrinsic pathway of apoptosis via caspase-9 and poly-(ADP-ribose) polymerase (PARP). PDT also inhibited tubular capillary formation in and invasion by HEC-1-A under VEGF pretreatment, that resulted from down-regulation of VEGFR2, EGFR, Ras homolog gene family/ member A (RhoA) and PGE2. These results are indicative of the specificity of radachlorin-mediated PDT to VEGF. CONCLUSION: The major advantage of radachlorin-mediated PDT is its selectivity for cancer tissue while maintaining adjacent normal endometrial tissue. Therefore, radachlorin-mediated PDT might offer high anticancer efficacy for endometrial adenocarcinoma and an especially useful modality for preserving fertility.
[Mh] Termos MeSH primário: Adenocarcinoma/patologia
Neoplasias do Endométrio/patologia
Luz
Fotoquimioterapia
Fármacos Fotossensibilizantes/farmacologia
Porfirinas/farmacologia
[Mh] Termos MeSH secundário: Adenocarcinoma/tratamento farmacológico
Adenocarcinoma/metabolismo
Apoptose/efeitos dos fármacos
Proliferação Celular/efeitos dos fármacos
Combinação de Medicamentos
Neoplasias do Endométrio/tratamento farmacológico
Neoplasias do Endométrio/metabolismo
Feminino
Seres Humanos
Receptor do Fator de Crescimento Epidérmico/metabolismo
Células Tumorais Cultivadas
Fator A de Crescimento do Endotélio Vascular/metabolismo
Receptor 2 de Fatores de Crescimento do Endotélio Vascular/metabolismo
Proteína rhoA de Ligação ao GTP/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Drug Combinations); 0 (Photosensitizing Agents); 0 (Porphyrins); 0 (VEGFA protein, human); 0 (Vascular Endothelial Growth Factor A); 0 (bremachlorin); EC 2.7.10.1 (EGFR protein, human); EC 2.7.10.1 (KDR protein, human); EC 2.7.10.1 (Receptor, Epidermal Growth Factor); EC 2.7.10.1 (Vascular Endothelial Growth Factor Receptor-2); EC 3.6.5.2 (rhoA GTP-Binding Protein)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171025
[St] Status:MEDLINE


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[PMID]:28889652
[Au] Autor:Hiruma S; Kamasaki T; Otomo K; Nemoto T; Uehara R
[Ad] Endereço:Graduate School of Life Science, Hokkaido University, Japan.
[Ti] Título:Dynamics and function of ERM proteins during cytokinesis in human cells.
[So] Source:FEBS Lett;591(20):3296-3309, 2017 Oct.
[Is] ISSN:1873-3468
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The molecular mechanism that governs cytoskeleton-membrane interaction during animal cytokinesis remains elusive. Here, we investigated the dynamics and functions of ERM (Ezrin/Radixin/Moesin) proteins during cytokinesis in human cultured cells. We found that ezrin is recruited to the cleavage furrow through its membrane-associated domain in a cholesterol-dependent but largely Rho-independent manner. While ERMs are dispensable for furrow ingression, they play a pivotal role in contractile activity of the polar cortex. Notably, when anillin and supervillin are codepleted, ERMs increasingly accumulate at the cleavage furrow and substantially contribute to the furrow ingression. These results reveal a supportive role of ERMs in cortical activities during cytokinesis, and also provide insight into the selective mechanism that preferentially associates cytokinesis-relevant proteins with the division site.
[Mh] Termos MeSH primário: Citoesqueleto de Actina/metabolismo
Membrana Celular/metabolismo
Citocinese/genética
Proteínas do Citoesqueleto/genética
Proteínas de Membrana/genética
Proteínas dos Microfilamentos/genética
[Mh] Termos MeSH secundário: Citoesqueleto de Actina/ultraestrutura
Linhagem Celular Transformada
Membrana Celular/ultraestrutura
Proteínas do Citoesqueleto/metabolismo
Regulação da Expressão Gênica
Genes Reporter
Proteínas de Fluorescência Verde/genética
Proteínas de Fluorescência Verde/metabolismo
Células HeLa
Seres Humanos
Luciferases/genética
Luciferases/metabolismo
Proteínas de Membrana/metabolismo
Proteínas dos Microfilamentos/metabolismo
Simulação de Dinâmica Molecular
Transdução de Sinais
Proteína rhoA de Ligação ao GTP/genética
Proteína rhoA de Ligação ao GTP/metabolismo
[Pt] Tipo de publicação:LETTER
[Nm] Nome de substância:
0 (Cytoskeletal Proteins); 0 (Membrane Proteins); 0 (Microfilament Proteins); 0 (SVIL protein, human); 0 (actin-binding protein anillin, human); 0 (ezrin); 124671-05-2 (RHOA protein, human); 144131-77-1 (moesin); 144517-21-5 (radixin); 147336-22-9 (Green Fluorescent Proteins); EC 1.13.12.- (Luciferases); EC 3.6.5.2 (rhoA GTP-Binding Protein)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170911
[St] Status:MEDLINE
[do] DOI:10.1002/1873-3468.12844


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[PMID]:28887414
[Au] Autor:Halaoui R; Rejon C; Chatterjee SJ; Szymborski J; Meterissian S; Muller WJ; Omeroglu A; McCaffrey L
[Ad] Endereço:Rosalind and Morris Goodman Cancer Research Centre, McGill University, Montreal, Quebec H3A 1A3, Canada.
[Ti] Título:Progressive polarity loss and luminal collapse disrupt tissue organization in carcinoma.
[So] Source:Genes Dev;31(15):1573-1587, 2017 Aug 01.
[Is] ISSN:1549-5477
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Epithelial cancers (carcinoma) account for 80%-90% of all cancers. The development of carcinoma is associated with disrupted epithelial organization and solid ductal structures. The mechanisms underlying the morphological development of carcinoma are poorly understood, but it is thought that loss of cell polarity is an early event. Here we report the characterization of the development of human breast lesions leading to carcinoma. We identified a unique mechanism that generates solid ducts in carcinoma through progressive loss of polarity and collapse of the luminal architecture. This program initiates with asymmetric divisions of polarized cells that generate a stratified epithelium containing both polarized and depolarized cells. Stratified regions form cords that penetrate into the lumen, subdividing it into polarized secondary lumina. The secondary lumina then collapse with a concomitant decrease in RhoA and myosin II activity at the apical membrane and ultimately lose apical-basal polarity. By restoring RhoA activity in mice, ducts maintained lumen and cell polarity. Notably, disrupted tissue architecture through luminal collapse was reversible, and ducts with a lumen were re-established after oncogene suppression in vivo. This reveals a novel and common mechanism that contributes to carcinoma development by progressively disrupting cell and tissue organization.
[Mh] Termos MeSH primário: Neoplasias da Mama/patologia
Carcinogênese
Carcinoma/patologia
Polaridade Celular/fisiologia
[Mh] Termos MeSH secundário: Animais
Membrana Celular
Células Cultivadas
Feminino
Imunofluorescência
Seres Humanos
Camundongos
Microscopia Confocal
Miosina Tipo II/metabolismo
Cultura Primária de Células
Proteína rhoA de Ligação ao GTP/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.6.1.- (Myosin Type II); EC 3.6.5.2 (rhoA GTP-Binding Protein)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171027
[Lr] Data última revisão:
171027
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170910
[St] Status:MEDLINE
[do] DOI:10.1101/gad.300566.117



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