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Pesquisa : D12.644.360 [Categoria DeCS]
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  1 / 33825 MEDLINE  
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[PMID]:29421438
[Au] Autor:He M; Li K; Yu C; Lv B; Zhao N; Deng J; Cao L; Huang H; Yin A; Shi T; Wang L
[Ad] Endereço:Center for Human Disease Genomics, Department of Immunology, School of Basic Medical Sciences, Health Science Center, Peking University, Beijing 100191, PR China; Key Laboratory of Medical Immunology, Ministry of Health, School of Basic Medical Science, Peking University, Beijing 100191, PR China.
[Ti] Título:In vitro study of FUZ as a novel potential therapeutic target in non-small-cell lung cancer.
[So] Source:Life Sci;197:91-100, 2018 Mar 15.
[Is] ISSN:1879-0631
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:FUZ is regarded as a planar cell polarity effector that controls multiple cellular processes during vertebrate development. However, the role of FUZ in tumor biology remains poorly studied. Our purpose of this study is to discover the physiological effects and mechanism of FUZ in non-small-cell lung cancer (NSCLC) in vitro. With the help of bioinformatics analysis, we noticed that the expression level of FUZ negatively correlates with prognosis of NSCLC patients. Exogenous FUZ expression markedly promoted cell proliferation of NSCLC cells. The phosphorylation of Erk1/2, STAT3 and related signaling molecules were induced activated after FUZ over-expression. FUZ also plays an important role in cell motility by regulating cell signaling pathways and inducing epithelial to mesenchymal transition (EMT). FUZ promotes EMT along with the up-regulation of N-cadherin, vimentin, Zeb1, Twist1 and decreased level of E-cadherin. Furthermore, we also carried out FUZ directed siRNA treatments to prove the above observations. Knockdown of FUZ resulted in delayed cell growth as well as impaired cell migration and reversed EMT phonotype. Importantly, we reported for the first time that FUZ is a BNIP3-interacting protein. Loss of FUZ resulted in decreased BNIP3 protein level, but no influence on BNIP3 mRNA level, suggesting weakened stability of BNIP3 protein. Overall, our results in vitro show that FUZ is responsible for NSCLC progression and metastasis, suggesting that FUZ can be a potential therapeutic target for NSCLC.
[Mh] Termos MeSH primário: Carcinoma Pulmonar de Células não Pequenas/metabolismo
Regulação Neoplásica da Expressão Gênica
Peptídeos e Proteínas de Sinalização Intracelular/metabolismo
Neoplasias Pulmonares/metabolismo
Sistema de Sinalização das MAP Quinases
Proteínas de Neoplasias/metabolismo
[Mh] Termos MeSH secundário: Células A549
Carcinoma Pulmonar de Células não Pequenas/tratamento farmacológico
Carcinoma Pulmonar de Células não Pequenas/genética
Carcinoma Pulmonar de Células não Pequenas/patologia
Proliferação Celular
Sistemas de Liberação de Medicamentos
Seres Humanos
Peptídeos e Proteínas de Sinalização Intracelular/genética
Neoplasias Pulmonares/tratamento farmacológico
Neoplasias Pulmonares/genética
Neoplasias Pulmonares/patologia
Proteínas de Neoplasias/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Intracellular Signaling Peptides and Proteins); 0 (Neoplasm Proteins)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180301
[Lr] Data última revisão:
180301
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180209
[St] Status:MEDLINE


  2 / 33825 MEDLINE  
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[PMID]:28464854
[Au] Autor:Chi L; Zou Y; Qin L; Ma W; Hao Y; Tang Y; Luo R; Wu Z
[Ad] Endereço:Cancer Center, TCM-Integrated Hospital, Southern Medical University, Guangzhou, 510315, China.
[Ti] Título:TIMELESS contributes to the progression of breast cancer through activation of MYC.
[So] Source:Breast Cancer Res;19(1):53, 2017 May 02.
[Is] ISSN:1465-542X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Breast cancer is the most common malignancy and the leading cause of cancer death among women. TIMELESS (TIM), a circadian rhythm regulator, has been recently implicated in the progression of human cancer. However, the role of TIM in the progression of breast cancer has not been well-characterized. METHODS: Immunohistochemistry (IHC) staining was used to examine TIM levels in breast cancer specimens. Mammosphere formation analysis and side population analysis were used to examine the effect of TIM on the self-renewal of breast cancer stem cells. A wound healing assay and a Transwell assay were used to determine the role of TIM in breast cancer cell migration and invasion. A soft agar growth assay in vitro and tumorigenicity in vivo were used to determine the role of TIM in tumorigenicity. RESULTS: TIM levels in both breast cancer cell lines and tissues were significantly upregulated. Patients with high TIM had poorer prognosis than patients with low TIM. Overexpression of TIM dramatically enhanced, while knockdown of TIM suppressed the self-renewal of cancer stem cells (CSCs), cell invasion and migration abilities of breast cancer cells in vitro. Moreover, overexpression of TIM significantly augmented, while knockdown of TIM reduced the tumorigenicity of breast cancer cells in vivo. Mechanism studies revealed that TIM upregulated the expression and the trans-activity of the well-known oncogene MYC. Inhibition of MYC significantly blocked the effects of TIM on CSC population, cell invasion and anchor-independent cell growth. CONCLUSION: TIM plays an important role in promoting breast cancer progression and may represent a novel therapeutic target for breast cancer.
[Mh] Termos MeSH primário: Neoplasias da Mama/genética
Proteínas de Ciclo Celular/genética
Proliferação Celular/genética
Peptídeos e Proteínas de Sinalização Intracelular/genética
Proteínas Proto-Oncogênicas c-myc/genética
[Mh] Termos MeSH secundário: Neoplasias da Mama/patologia
Progressão da Doença
Feminino
Regulação Neoplásica da Expressão Gênica
Seres Humanos
Células MCF-7
Invasividade Neoplásica/genética
Células-Tronco Neoplásicas/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cell Cycle Proteins); 0 (Intracellular Signaling Peptides and Proteins); 0 (MYC protein, human); 0 (Proto-Oncogene Proteins c-myc); 0 (TIMELESS protein, human)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180301
[Lr] Data última revisão:
180301
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE
[do] DOI:10.1186/s13058-017-0838-1


  3 / 33825 MEDLINE  
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[PMID]:28460365
[Au] Autor:Krueger-Burg D; Papadopoulos T; Brose N
[Ad] Endereço:Department of Molecular Neurobiology, Max Planck Institute of Experimental Medicine, Hermann-Rein-Straße 3, 37075 Göttingen, Germany. Electronic address: krueger@em.mpg.de.
[Ti] Título:Organizers of inhibitory synapses come of age.
[So] Source:Curr Opin Neurobiol;45:66-77, 2017 Aug.
[Is] ISSN:1873-6882
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:While the postsynaptic density of excitatory synapses is known to encompass a highly complex molecular machinery, the equivalent organizational structure of inhibitory synapses has long remained largely undefined. In recent years, however, substantial progress has been made towards identifying the full complement of organizational proteins present at inhibitory synapses, including submembranous scaffolds, intracellular signaling proteins, transsynaptic adhesion proteins, and secreted factors. Here, we summarize these findings and discuss future challenges in assigning synapse-specific functions to the newly discovered catalog of proteins, an endeavor that will depend heavily on newly developed technologies such as proximity biotinylation. Further advances are made all the more essential by growing evidence that links inhibitory synapses to psychiatric and neurological disorders.
[Mh] Termos MeSH primário: Sinapses/fisiologia
[Mh] Termos MeSH secundário: Seres Humanos
Peptídeos e Proteínas de Sinalização Intracelular/metabolismo
Proteínas do Tecido Nervoso/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Intracellular Signaling Peptides and Proteins); 0 (Nerve Tissue Proteins)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180228
[Lr] Data última revisão:
180228
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170502
[St] Status:MEDLINE


  4 / 33825 MEDLINE  
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[PMID]:28468989
[Au] Autor:D'Avino PP
[Ad] Endereço:Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QP, UK ppd21@cam.ac.uk.
[Ti] Título:Citron kinase - renaissance of a neglected mitotic kinase.
[So] Source:J Cell Sci;130(10):1701-1708, 2017 May 15.
[Is] ISSN:1477-9137
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Cell division controls the faithful segregation of genomic and cytoplasmic materials between the two nascent daughter cells. Members of the Aurora, Polo and cyclin-dependent (Cdk) kinase families are known to regulate multiple events throughout cell division, whereas another kinase, citron kinase (CIT-K), for a long time has been considered to function solely during cytokinesis, the last phase of cell division. CIT-K was originally proposed to regulate the ingression of the cleavage furrow that forms at the equatorial cortex of the dividing cell after chromosome segregation. However, studies in the last decade have clarified that this kinase is, instead, required for the organization of the midbody in late cytokinesis, and also revealed novel functions of CIT-K earlier in mitosis and in DNA damage control. Moreover, CIT-K mutations have recently been linked to the development of human microcephaly, and CIT-K has been identified as a potential target in cancer therapy. In this Commentary, I describe and re-evaluate the functions and regulation of CIT-K during cell division and its involvement in human disease. Finally, I offer my perspectives on the open questions and future challenges that are necessary to address, in order to fully understand this important and yet unjustly neglected mitotic kinase.
[Mh] Termos MeSH primário: Peptídeos e Proteínas de Sinalização Intracelular/metabolismo
Mitose
Proteínas Serina-Treonina Quinases/metabolismo
[Mh] Termos MeSH secundário: Animais
Citocinese
Seres Humanos
Modelos Biológicos
Transdução de Sinais
Proteínas rho de Ligação ao GTP/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Intracellular Signaling Peptides and Proteins); EC 2.7.1.- (citron-kinase); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 3.6.5.2 (rho GTP-Binding Proteins)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180223
[Lr] Data última revisão:
180223
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.1242/jcs.200253


  5 / 33825 MEDLINE  
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[PMID]:29412778
[Au] Autor:Xiao S; Wang R; Wu X; Liu W; Ma S
[Ad] Endereço:1 The First Section of Radiotherapy for Head and Neck, Hunan Cancer Hospital and the Affiliated Cancer Hospital of Xiangya School of Medicine, Central South University , Changsha, Hunan, China .
[Ti] Título:The Long Noncoding RNA TP73-AS1 Interacted with miR-124 to Modulate Glioma Growth by Targeting Inhibitor of Apoptosis-Stimulating Protein of p53.
[So] Source:DNA Cell Biol;37(2):117-125, 2018 Feb.
[Is] ISSN:1557-7430
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:P73 antisense RNA 1T (non-protein coding), known as TP73-AS1 or PDAM, is a long noncoding RNA (lncRNA), which may regulate apoptosis by regulation of p53-dependent antiapoptotic genes. An abnormal change of TP73-AS1 expression was noticed in cancers. The effects of TP73-AS1 in brain glioma growth and the underlying mechanism remain unclear so far. In this study, the effect of TP73-AS1 in human brain glioma cell lines and clinical tumor samples was detected so as to reveal its role and function. In this study, TP73-AS1 was specifically upregulated in brain glioma cell lines and promoted glioma cell growth through targeting miR-124. TP73-AS1 knocking down suppressed human brain glioma cell proliferation, invasion, and metastasis in vitro. The inhibitory effect of TP73-AS1 knocking down on glioma cell proliferation and invasion could partly be restored by miR-124 inhibition. In addition, miR-124-dependent inhibitor of apoptosis-stimulating protein of p53 (iASPP) regulation was required in TP73-AS1-induced brain glioma cell growth. Data from this study revealed that TP73-AS1 inhibited the brain glioma growth and metastasis as a competing endogenous RNA (ceRNA) through miR-124-dependent iASPP regulation. In conclusion, we regarded TP73-AS1 as an oncogenic lncRNA promoting brain glioma proliferation and metastasis and a potential target for human brain glioma treatment.
[Mh] Termos MeSH primário: Neoplasias Encefálicas/genética
Glioma/genética
Peptídeos e Proteínas de Sinalização Intracelular/genética
MicroRNAs/genética
RNA Longo não Codificante/genética
Proteínas Repressoras/genética
[Mh] Termos MeSH secundário: Sequência de Bases
Sítios de Ligação
Neoplasias Encefálicas/metabolismo
Neoplasias Encefálicas/patologia
Linhagem Celular Tumoral
Movimento Celular
Proliferação Celular
Regulação Neoplásica da Expressão Gênica
Glioma/metabolismo
Glioma/patologia
Seres Humanos
Peptídeos e Proteínas de Sinalização Intracelular/metabolismo
MicroRNAs/metabolismo
Invasividade Neoplásica
Interferência de RNA
RNA Longo não Codificante/metabolismo
Proteínas Repressoras/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Intracellular Signaling Peptides and Proteins); 0 (MIRN124 microRNA, human); 0 (MicroRNAs); 0 (PPP1R13L protein, human); 0 (RNA, Long Noncoding); 0 (Repressor Proteins); 0 (long non-coding RNA KIAA0495, human)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180222
[Lr] Data última revisão:
180222
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180208
[St] Status:MEDLINE
[do] DOI:10.1089/dna.2017.3941


  6 / 33825 MEDLINE  
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[PMID]:29254286
[Au] Autor:Robuffo I; Toniato E; Tettamanti L; Mastrangelo F; Ronconi G; Frydas I; Caraffa A; Kritas SK; Conti P
[Ad] Endereço:Institute of Molecular Genetics, CNR, Sede di Chieti, Italy.
[Ti] Título:Mast cell in innate immunity mediated by proinflammatory and antiinflammatory IL-1 family members.
[So] Source:J Biol Regul Homeost Agents;31(4):837-842, 2017 Oct-Dec.
[Is] ISSN:0393-974X
[Cp] País de publicação:Italy
[La] Idioma:eng
[Ab] Resumo:Innate immunity consists of physical and chemical barriers which provide the early defense against infections. Innate immunity orchestrates the defense of the host with cellular and biochemical proteins. Mast cells (MCs) are involved in innate and adaptive immunity and are the first line of defense which generates multiple inflammatory cytokines/chemokines in response to numerous antigens. MC-activated antigen receptor Fc-RI provokes a number of important biochemical pathways with secretion of numerous vasoactive, chemoattractant and inflammatory compounds which participate in allergic and inflammatory diseases. MCs can also be activated by Th1 cytokines and generate pre-formed and de novo inflammatory mediators, including TNF. IL-37 is an anti-inflammatory cytokine which binds IL-18R-alpha chain and reduces the production of inflammatory IL-1 family members. IL-37 down-regulates innate immunity by inhibiting macrophage response and its accumulation and reduces the cytokines that mediate inflammatory diseases. Here, we discuss the relationship between MCs, innate immunity, and pro-inflammatory and anti-inflammatory cytokines.
[Mh] Termos MeSH primário: Inflamação/imunologia
Interleucina-1/imunologia
Macrófagos/imunologia
Mastócitos/imunologia
Receptores de Interleucina-1/imunologia
[Mh] Termos MeSH secundário: Imunidade Adaptativa
Linfócitos B/imunologia
Linfócitos B/patologia
Comunicação Celular
Regulação da Expressão Gênica
Seres Humanos
Imunidade Inata
Inflamação/genética
Inflamação/patologia
Interleucina-1/genética
Subunidade alfa de Receptor de Interleucina-18/genética
Subunidade alfa de Receptor de Interleucina-18/imunologia
Peptídeos e Proteínas de Sinalização Intracelular/genética
Peptídeos e Proteínas de Sinalização Intracelular/imunologia
Macrófagos/patologia
Mastócitos/patologia
Receptores de Interleucina-1/genética
Transdução de Sinais
Linfócitos T/imunologia
Linfócitos T/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (FcRI protein, human); 0 (IL18R1 protein, human); 0 (IL37 protein, human); 0 (Interleukin-1); 0 (Interleukin-18 Receptor alpha Subunit); 0 (Intracellular Signaling Peptides and Proteins); 0 (Receptors, Interleukin-1)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180222
[Lr] Data última revisão:
180222
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171220
[St] Status:MEDLINE


  7 / 33825 MEDLINE  
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[PMID]:29293680
[Au] Autor:Jin T; Huang M; Jiang J; Smith P; Xiao TS
[Ad] Endereço:Laboratory of structural immunology, CAS Key Laboratory of innate immunity and chronic diseases, CAS Center for Excellence in Molecular Cell Science, School of Life Sciences and Medical Center, University of Science and Technology of China, Hefei, Anhui, PRC.
[Ti] Título:Crystal structure of human NLRP12 PYD domain and implication in homotypic interaction.
[So] Source:PLoS One;13(1):e0190547, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:NLRP12 is a NOD-like receptor that plays multiple roles in both inflammation and tumorigenesis. Despite the importance, little is known about its mechanism of action at the molecular level. Here, we report the crystal structure of NLRP12 PYD domain at 1.70 Å fused with an maltose-binding protein (MBP) tag. Interestingly, the PYD domain forms a dimeric configuration through a disulfide bond in the crystal. The possible biological significance is discussed in the context of ROS induced NF-κB activation.
[Mh] Termos MeSH primário: Peptídeos e Proteínas de Sinalização Intracelular/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Cristalografia por Raios X
Seres Humanos
Peptídeos e Proteínas de Sinalização Intracelular/metabolismo
Modelos Moleculares
Ligação Proteica
Conformação Proteica
Homologia de Sequência de Aminoácidos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Intracellular Signaling Peptides and Proteins); 0 (NLRP12 protein, human)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180221
[Lr] Data última revisão:
180221
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180103
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0190547


  8 / 33825 MEDLINE  
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[PMID]:29293652
[Au] Autor:Stockum A; Snijders AP; Maertens GN
[Ad] Endereço:Imperial College London, Department of Medicine, Division of Infectious Diseases, Norfolk Place, London, United Kingdom.
[Ti] Título:USP11 deubiquitinates RAE1 and plays a key role in bipolar spindle formation.
[So] Source:PLoS One;13(1):e0190513, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Correct segregation of the mitotic chromosomes into daughter cells is a highly regulated process critical to safeguard genome stability. During M phase the spindle assembly checkpoint (SAC) ensures that all kinetochores are correctly attached before its inactivation allows progression into anaphase. Upon SAC inactivation, the anaphase promoting complex/cyclosome (APC/C) E3 ligase ubiquitinates and targets cyclin B and securin for proteasomal degradation. Here, we describe the identification of Ribonucleic Acid Export protein 1 (RAE1), a protein previously shown to be involved in SAC regulation and bipolar spindle formation, as a novel substrate of the deubiquitinating enzyme (DUB) Ubiquitin Specific Protease 11 (USP11). Lentiviral knock-down of USP11 or RAE1 in U2OS cells drastically reduces cell proliferation and increases multipolar spindle formation. We show that USP11 is associated with the mitotic spindle, does not regulate SAC inactivation, but controls ubiquitination of RAE1 at the mitotic spindle, hereby functionally modulating its interaction with Nuclear Mitotic Apparatus protein (NuMA).
[Mh] Termos MeSH primário: Proteínas Associadas à Matriz Nuclear/metabolismo
Proteínas de Transporte Nucleocitoplasmático/metabolismo
Fuso Acromático
Tioléster Hidrolases/metabolismo
[Mh] Termos MeSH secundário: Linhagem Celular Tumoral
Proliferação Celular
Técnicas de Silenciamento de Genes
Células HEK293
Seres Humanos
Peptídeos e Proteínas de Sinalização Intracelular/metabolismo
Ligação Proteica
Especificidade por Substrato
Tioléster Hidrolases/genética
Ubiquitinação
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Intracellular Signaling Peptides and Proteins); 0 (Nuclear Matrix-Associated Proteins); 0 (Nucleocytoplasmic Transport Proteins); 0 (RAE1 protein, human); 0 (SPRY3 protein, human); EC 3.1.2.- (Thiolester Hydrolases); EC 3.1.2.15 (USP11 protein, human)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180221
[Lr] Data última revisão:
180221
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180103
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0190513


  9 / 33825 MEDLINE  
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[PMID]:29248131
[Au] Autor:Wilde L; Roche M; Domingo-Vidal M; Tanson K; Philp N; Curry J; Martinez-Outschoorn U
[Ad] Endereço:Department of Medical Oncology Thomas Jefferson University, Philadelphia, PA.
[Ti] Título:Metabolic coupling and the Reverse Warburg Effect in cancer: Implications for novel biomarker and anticancer agent development.
[So] Source:Semin Oncol;44(3):198-203, 2017 06.
[Is] ISSN:1532-8708
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Glucose is a key metabolite used by cancer cells to generate ATP, maintain redox state and create biomass. Glucose can be catabolized to lactate in the cytoplasm, which is termed glycolysis, or alternatively can be catabolized to carbon dioxide and water in the mitochondria via oxidative phosphorylation. Metabolic heterogeneity exists in a subset of human tumors, with some cells maintaining a glycolytic phenotype while others predominantly utilize oxidative phosphorylation. Cells within tumors interact metabolically with transfer of catabolites from supporting stromal cells to adjacent cancer cells. The Reverse Warburg Effect describes when glycolysis in the cancer-associated stroma metabolically supports adjacent cancer cells. This catabolite transfer, which induces stromal-cancer metabolic coupling, allows cancer cells to generate ATP, increase proliferation, and reduce cell death. Catabolites implicated in metabolic coupling include the monocarboxylates lactate, pyruvate, and ketone bodies. Monocarboxylate transporters (MCT) are critically necessary for release and uptake of these catabolites. MCT4 is involved in the release of monocarboxylates from cells, is regulated by catabolic transcription factors such as hypoxia inducible factor 1 alpha (HIF1A) and nuclear factor kappa-light-chain-enhancer of activated B cells (NF-κB), and is highly expressed in cancer-associated fibroblasts. Conversely, MCT1 is predominantly involved in the uptake of these catabolites and is highly expressed in a subgroup of cancer cells. MYC and TIGAR, which are genes involved in cellular proliferation and anabolism, are inducers of MCT1. Profiling human tumors on the basis of an altered redox balance and intra-tumoral metabolic interactions may have important biomarker and therapeutic implications. Alterations in the redox state and mitochondrial function of cells can induce metabolic coupling. Hence, there is interest in redox and metabolic modulators as anticancer agents. Also, markers of metabolic coupling have been associated with poor outcomes in numerous human malignancies and may be useful prognostic and predictive biomarkers.
[Mh] Termos MeSH primário: Trifosfato de Adenosina/metabolismo
Glucose/metabolismo
Neoplasias/metabolismo
[Mh] Termos MeSH secundário: Antineoplásicos
Proliferação Celular
Descoberta de Drogas
Fibroblastos/metabolismo
Glicólise
Seres Humanos
Subunidade alfa do Fator 1 Induzível por Hipóxia/metabolismo
Peptídeos e Proteínas de Sinalização Intracelular/metabolismo
Corpos Cetônicos/metabolismo
Ácido Láctico/metabolismo
Transportadores de Ácidos Monocarboxílicos/metabolismo
Proteínas Musculares/metabolismo
NF-kappa B/metabolismo
Neoplasias/tratamento farmacológico
Proteínas Proto-Oncogênicas c-myc/metabolismo
Ácido Pirúvico/metabolismo
Células Estromais/metabolismo
Simportadores/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (C12orf5 protein, human); 0 (HIF1A protein, human); 0 (Hypoxia-Inducible Factor 1, alpha Subunit); 0 (Intracellular Signaling Peptides and Proteins); 0 (Ketone Bodies); 0 (MYC protein, human); 0 (Monocarboxylic Acid Transporters); 0 (Muscle Proteins); 0 (NF-kappa B); 0 (Proto-Oncogene Proteins c-myc); 0 (SLC16A4 protein, human); 0 (Symporters); 0 (monocarboxylate transport protein 1); 33X04XA5AT (Lactic Acid); 8558G7RUTR (Pyruvic Acid); 8L70Q75FXE (Adenosine Triphosphate); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:180222
[Lr] Data última revisão:
180222
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171218
[St] Status:MEDLINE


  10 / 33825 MEDLINE  
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[PMID]:29259037
[Au] Autor:Falch CM; Sundaram AYM; Øystese KA; Normann KR; Lekva T; Silamikelis I; Eieland AK; Andersen M; Bollerslev J; Olarescu NC
[Ad] Endereço:Section of Specialized EndocrinologyDepartment of Endocrinology cafal14@student.sdu.dk.
[Ti] Título:Gene expression profiling of fast- and slow-growing non-functioning gonadotroph pituitary adenomas.
[So] Source:Eur J Endocrinol;178(3):295-307, 2018 Mar.
[Is] ISSN:1479-683X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: Reliable biomarkers associated with aggressiveness of non-functioning gonadotroph adenomas (GAs) are lacking. As the growth of tumor remnants is highly variable, molecular markers for growth potential prediction are necessary. We hypothesized that fast- and slow-growing GAs present different gene expression profiles and reliable biomarkers for tumor growth potential could be identified, focusing on the specific role of epithelial-mesenchymal transition (EMT). DESIGN AND METHODS: Eight GAs selected for RNA sequencing were equally divided into fast- and slow-growing group by the tumor volume doubling time (TVDT) median (27.75 months). Data were analyzed by tophat2, cufflinks and cummeRbund pipeline. 40 genes were selected for RT-qPCR validation in 20 GAs based on significance, fold-change and pathway analyses. The effect of silencing (metadherin) and (endomucin) on migration of human adenoma cells was evaluated. RESULTS: 350 genes were significantly differentially expressed (282 genes upregulated and 68 downregulated in the fast group, -adjusted <0.05). Among 40 selected genes, 11 showed associations with TVDT (-0.669< <-0.46, < 0.05). These were and six EMT-related genes ( and ). , but not , demonstrated involvement in cell migration and association with EMT markers. CONCLUSIONS: Fast- and slow-growing GAs present different gene expression profiles, and genes related to EMT have higher expression in fast-growing tumors. In addition to , identified as an important contributor to aggressiveness, the other genes might represent markers for tumor growth potential and possible targets for drug therapy.
[Mh] Termos MeSH primário: Adenoma/genética
Transição Epitelial-Mesenquimal/genética
Neoplasias Hipofisárias/genética
RNA Mensageiro/metabolismo
[Mh] Termos MeSH secundário: Proteínas Adaptadoras de Transdução de Sinal/genética
Adenoma/metabolismo
Adulto
Idoso
Caderinas/genética
Moléculas de Adesão Celular/genética
Movimento Celular/genética
Subunidades Catalíticas da Proteína Quinase Dependente de AMP Cíclico/genética
Feminino
Hormônio Foliculoestimulante/metabolismo
Perfilação da Expressão Gênica
Regulação Neoplásica da Expressão Gênica
Inativação Gênica
Seres Humanos
Técnicas In Vitro
Peptídeos e Proteínas de Sinalização Intracelular/genética
Hormônio Luteinizante/metabolismo
Masculino
Glicoproteínas de Membrana/genética
Proteínas Associadas aos Microtúbulos/genética
Meia-Idade
Miosina Tipo I/genética
Proteínas do Tecido Nervoso/genética
Neoplasias Hipofisárias/metabolismo
Proteínas Proto-Oncogênicas/genética
Receptores de Superfície Celular/genética
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Ribonucleases/genética
Sialoglicoproteínas/genética
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (Cadherins); 0 (Cell Adhesion Molecules); 0 (EMCN protein, human); 0 (GPM6A protein, human); 0 (Intracellular Signaling Peptides and Proteins); 0 (MTDH protein, human); 0 (MYO1B protein, human); 0 (Membrane Glycoproteins); 0 (Microtubule-Associated Proteins); 0 (Nerve Tissue Proteins); 0 (PCDH18 protein, human); 0 (Proto-Oncogene Proteins); 0 (RNA, Messenger); 0 (Receptors, Cell Surface); 0 (SKIL protein, human); 0 (SPAG9 protein, human); 0 (Sialoglycoproteins); 0 (UNC5H4 protein, human); 0 (hook1 protein, human); 9002-67-9 (Luteinizing Hormone); 9002-68-0 (Follicle Stimulating Hormone); EC 2.7.11.11 (Cyclic AMP-Dependent Protein Kinase Catalytic Subunits); EC 2.7.11.11 (PRKACB protein, human); EC 3.1.- (CNOT6L protein, human); EC 3.1.- (Ribonucleases); EC 3.6.1.- (Myosin Type I)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180220
[Lr] Data última revisão:
180220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171221
[St] Status:MEDLINE
[do] DOI:10.1530/EJE-17-0702



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