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Pesquisa : D12.776.157.530.200.374.750.500.250 [Categoria DeCS]
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[PMID]:28350098
[Au] Autor:Zhu B; Cheng D; Hou L; Zhou S; Ying T; Yang Q
[Ad] Endereço:Department of Orthopedics, Shanghai Jiao Tong University Affiliated Sixth People's Hospital, Shanghai 200233, P.R. China.
[Ti] Título:SLC3A2 is upregulated in human osteosarcoma and promotes tumor growth through the PI3K/Akt signaling pathway.
[So] Source:Oncol Rep;37(5):2575-2582, 2017 May.
[Is] ISSN:1791-2431
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:Growing evidence indicates that SLC3A2 (solute carrier family 3 member 2) is upregulated and correlates with tumor growth in multiple types of cancers, while the role of SLC3A2 in human osteosarcoma (OS) is rarely discussed. Thus, the aim of the present study was to demonstrate the expression of SLC3A2 in human osteosarcoma and reveal its biological function and the underlying mechanisms. RT-PCR, western blot analysis and immunohistochemistry (IHC) were used to assess the expression of SLC3A2 in OS samples and cell lines. Cell cycle, Cell Counting Kit-8 (CCK-8) and colony formation assays were used to test the cell survival capacity. To investigate the potential mechanism by which SLC3A2 regulates OS growth, we used a slide-based antibody array. We demonstrated that SLC3A2 was upregulated in OS cell lines as well as OS tissues. High expression of SLC3A2 was correlated with clinical stage and tumor size in OS. Reduced expression of SLC3A2 inhibited OS cell proliferation through G2/M phase arrest. Most importantly, we found that SLC3A2 may regulate OS growth through the PI3K/Akt signaling pathway. In conclusion, SLC3A2 is upregulated in OS and plays a crucial role in tumor growth. Targeting SLC3A2 may provide a new therapeutic strategy for OS.
[Mh] Termos MeSH primário: Neoplasias Ósseas/patologia
Cadeia Pesada da Proteína-1 Reguladora de Fusão/metabolismo
Osteossarcoma/patologia
Fosfatidilinositol 3-Quinases/metabolismo
Proteínas Proto-Oncogênicas c-akt/metabolismo
[Mh] Termos MeSH secundário: Adolescente
Adulto
Neoplasias Ósseas/metabolismo
Pontos de Checagem do Ciclo Celular/genética
Linhagem Celular Tumoral
Proliferação Celular
Feminino
Cadeia Pesada da Proteína-1 Reguladora de Fusão/genética
Técnicas de Silenciamento de Genes
Seres Humanos
Masculino
Osteossarcoma/metabolismo
Fosfatidilinositol 3-Quinases/genética
Proteínas Proto-Oncogênicas c-akt/genética
Transdução de Sinais
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fusion Regulatory Protein 1, Heavy Chain); 0 (SLC3A2 protein, human); EC 2.7.1.- (Phosphatidylinositol 3-Kinases); EC 2.7.11.1 (Proto-Oncogene Proteins c-akt)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170329
[St] Status:MEDLINE
[do] DOI:10.3892/or.2017.5530


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[PMID]:28320871
[Au] Autor:Ohgaki R; Ohmori T; Hara S; Nakagomi S; Kanai-Azuma M; Kaneda-Nakashima K; Okuda S; Nagamori S; Kanai Y
[Ad] Endereço:Department of Bio-system Pharmacology, Graduate School of Medicine, Osaka University, Suita, Osaka, Japan.
[Ti] Título:Essential Roles of L-Type Amino Acid Transporter 1 in Syncytiotrophoblast Development by Presenting Fusogenic 4F2hc.
[So] Source:Mol Cell Biol;37(11), 2017 Jun 01.
[Is] ISSN:1098-5549
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The layers of the epithelial syncytium, i.e., syncytiotrophoblasts, differentiate from chorionic trophoblasts via cell fusion and separate maternal and fetal circulations in hemochorial placentas. L-type amino acid transporter 1 (LAT1) and its covalently linked ancillary subunit 4F2hc are colocalized on both maternal and fetal surfaces of syncytiotrophoblasts, implying their roles in amino acid transfer through the placental barrier. In this study, LAT1 knockout, in addition, revealed a novel role of LAT1 in syncytiotrophoblast development. LAT1 at midgestation was selectively expressed in trophoblastic lineages in the placenta, exclusively as a LAT1-4F2hc heterodimer. In LAT1 homozygous knockout mice, chorionic trophoblasts remained largely mononucleated, and the layers of syncytiotrophoblasts were almost completely absent. The amount of 4F2hc protein, which possesses a fusogenic function in trophoblastic cells, as well as in virus-infected cells, was drastically reduced by LAT1 knockout, with less affecting the mRNA level. Knockdown of LAT1 in trophoblastic BeWo cells also reduced 4F2hc protein and suppressed forskolin-induced cell fusion. These results demonstrate a novel fundamental role of LAT1 to support the protein expression of 4F2hc via a chaperone-like function in chorionic trophoblasts and to promote syncytiotrophoblast formation by contributing to cell fusion in the developing placenta.
[Mh] Termos MeSH primário: Cadeia Pesada da Proteína-1 Reguladora de Fusão/metabolismo
Transportador 1 de Aminoácidos Neutros Grandes/metabolismo
Trofoblastos/metabolismo
[Mh] Termos MeSH secundário: Animais
Apoptose/efeitos dos fármacos
Fusão Celular
Linhagem Celular
Linhagem da Célula
Proliferação Celular/efeitos dos fármacos
Colforsina/farmacologia
Cruzamentos Genéticos
Perda do Embrião/patologia
Feminino
Deleção de Genes
Técnicas de Silenciamento de Genes
Marcação de Genes
Homozigoto
Seres Humanos
Masculino
Camundongos Endogâmicos C57BL
Camundongos Knockout
Placenta/anormalidades
Placenta/efeitos dos fármacos
Gravidez
Trofoblastos/citologia
Trofoblastos/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fusion Regulatory Protein 1, Heavy Chain); 0 (Large Neutral Amino Acid-Transporter 1); 1F7A44V6OU (Colforsin)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170322
[St] Status:MEDLINE


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[PMID]:28274951
[Au] Autor:Loayza-Puch F; Rooijers K; Zijlstra J; Moumbeini B; Zaal EA; Oude Vrielink JF; Lopes R; Ugalde AP; Berkers CR; Agami R
[Ad] Endereço:Division of Biological Stress Response, The Netherlands Cancer Institute, Amsterdam, The Netherlands f.loayza@nki.nl r.agami@nki.nl.
[Ti] Título:TGFß1-induced leucine limitation uncovered by differential ribosome codon reading.
[So] Source:EMBO Rep;18(4):549-557, 2017 Apr.
[Is] ISSN:1469-3178
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Cancer cells modulate their metabolic networks to support cell proliferation and a higher demand of building blocks. These changes may restrict the availability of certain amino acids for protein synthesis, which can be utilized for cancer therapy. However, little is known about the amino acid demand changes occurring during aggressive and invasive stages of cancer. Recently, we developed diricore, an approach based on ribosome profiling that can uncover amino acid limitations. Here, we applied diricore to a cellular model in which epithelial breast cells respond rapidly to TGFß1, a cytokine essential for cancer progression and metastasis, and uncovered shortage of leucine. Further analyses indicated that TGFß1 treatment of human breast epithelial cells reduces the expression of SLC3A2, a subunit of the leucine transporter, which diminishes leucine uptake and inhibits cell proliferation. Thus, we identified a specific amino acid limitation associated with the TGFß1 response, a vulnerability that might be associated with aggressiveness in cancer.
[Mh] Termos MeSH primário: Códon
Leucina/genética
Leucina/metabolismo
Biossíntese de Proteínas
Ribossomos/metabolismo
Fator de Crescimento Transformador beta1/metabolismo
[Mh] Termos MeSH secundário: Neoplasias da Mama/genética
Neoplasias da Mama/metabolismo
Linhagem Celular Tumoral
Feminino
Cadeia Pesada da Proteína-1 Reguladora de Fusão/genética
Cadeia Pesada da Proteína-1 Reguladora de Fusão/metabolismo
Regulação Neoplásica da Expressão Gênica/efeitos dos fármacos
Seres Humanos
Biossíntese de Proteínas/efeitos dos fármacos
Transdução de Sinais
Fator de Crescimento Transformador beta1/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Codon); 0 (Fusion Regulatory Protein 1, Heavy Chain); 0 (SLC3A2 protein, human); 0 (Transforming Growth Factor beta1); GMW67QNF9C (Leucine)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170310
[St] Status:MEDLINE
[do] DOI:10.15252/embr.201744000


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[PMID]:28012647
[Au] Autor:Baumer Y; McCurdy S; Alcala M; Mehta N; Lee BH; Ginsberg MH; Boisvert WA
[Ad] Endereço:Center for Cardiovascular Research, John A. Burns School of Medicine, University of Hawaii, Honolulu, HI, United States.
[Ti] Título:CD98 regulates vascular smooth muscle cell proliferation in atherosclerosis.
[So] Source:Atherosclerosis;256:105-114, 2017 Jan.
[Is] ISSN:1879-1484
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:BACKGROUND AND AIMS: Vascular smooth muscle cells (VSMC) migrate and proliferate to form a stabilizing fibrous cap that encapsulates atherosclerotic plaques. CD98 is a transmembrane protein made of two subunits, CD98 heavy chain (CD98hc) and one of six light chains, and is known to be involved in cell proliferation and survival. Because the influence of CD98hc on atherosclerosis development is unknown, our aim was to determine if CD98hc expressed on VSMC plays a role in shaping the morphology of atherosclerotic plaques by regulating VSMC function. METHODS: In addition to determining the role of CD98hc in VSMC proliferation and apoptosis, we utilized mice with SMC-specific deletion of CD98hc (CD98hc SM22αCre ) to determine the effects of CD98hc deficiency on VSMC function in atherosclerotic plaque. RESULTS: After culturing for 5 days in vitro, CD98hc VSMC displayed dramatically reduced cell counts, reduced proliferation, as well as reduced migration compared to control VSMC. Analysis of aortic VSCM after 8 weeks of HFD showed a reduction in CD98hc VSMC proliferation as well as increased apoptosis compared to controls. A long-term atherosclerosis study using SMC-CD98hc /ldlr mice was performed. Although total plaque area was unchanged, CD98hc mice showed reduced presence of VSMC within the plaque (2.1 ± 0.4% vs. 4.3 ± 0.4% SM22α-positive area per plaque area, p < 0.05), decreased collagen content, as well as increased necrotic core area (25.8 ± 1.9% vs. 10.9 ± 1.6%, p < 0.05) compared to control ldlr mice. CONCLUSIONS: We conclude that CD98hc is required for VSMC proliferation, and that its deficiency leads to significantly reduced presence of VSMC in the neointima. Thus, CD98hc expression in VSMC contributes to the formation of plaques that are morphologically more stable, and thereby protects against atherothrombosis.
[Mh] Termos MeSH primário: Aterosclerose/metabolismo
Proliferação Celular
Cadeia Pesada da Proteína-1 Reguladora de Fusão/metabolismo
Músculo Liso Vascular/metabolismo
Miócitos de Músculo Liso/metabolismo
[Mh] Termos MeSH secundário: Animais
Apoptose
Aterosclerose/genética
Aterosclerose/patologia
Movimento Celular
Células Cultivadas
Modelos Animais de Doenças
Elastina/metabolismo
Cadeia Pesada da Proteína-1 Reguladora de Fusão/genética
Predisposição Genética para Doença
Masculino
Camundongos Endogâmicos C57BL
Camundongos Knockout
Músculo Liso Vascular/patologia
Miócitos de Músculo Liso/patologia
Necrose
Neointima
Fenótipo
Placa Aterosclerótica
Receptores de LDL/deficiência
Receptores de LDL/genética
Ruptura Espontânea
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fusion Regulatory Protein 1, Heavy Chain); 0 (Receptors, LDL); 0 (Slc3A2 protein, mouse); 9007-58-3 (Elastin)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161226
[St] Status:MEDLINE


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[PMID]:27900521
[Au] Autor:Feral CC; Tissot FS; Tosello L; Fakhry N; Sebag F; Pacak K; Taïeb D
[Ad] Endereço:INSERM U1081, Institute for Research on Cancer and Aging of Nice (IRCAN), Nice, France.
[Ti] Título:F-fluorodihydroxyphenylalanine PET/CT in pheochromocytoma and paraganglioma: relation to genotype and amino acid transport system L.
[So] Source:Eur J Nucl Med Mol Imaging;44(5):812-821, 2017 May.
[Is] ISSN:1619-7089
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:PURPOSE: F-FDOPA is a highly sensitive and specific radiopharmaceutical for pheochromocytoma and paraganglioma (PPGL) imaging. However, F-FDOPA might be falsely negative in these tumors, especially those related to mutations in succinate dehydrogenase genes (SDHx). The aim of the present study was to evaluate the relationship between expression of L-DOPA transporters and F-FDOPA PET imaging results in PPGL. METHODS: From 2007 to 2015, 175 patients with non-metastatic PPGL were evaluated by F-FDOPA PET/CT for initial diagnosis/staging and follow-up. F-FDOPA PET/CT was considered as falsely negative for at least one lesion in 10/126 (8%) patients (two sporadic, six SDHD, two SDHB PPGLs). The mRNA and protein expression levels of CD98hc and LATs were evaluated in samples with different genetic backgrounds and imaging phenotypes. The qRT-PCR and immunohistochemical analyses were performed in 14 and 16 tumor samples, respectively. RESULTS: The SDHx mutated samples exhibited a significant decrease in mRNA expression of LAT3 when compared to sporadic PPGLs (P = 0.042). There was also a statistical trend toward decreased CD98hc (P = 0.147) and LAT4 (P = 0.012) levels in SDHx vs sporadic PPGLs. No difference was observed for LAT1/LAT2 mRNA levels. LAT1 protein was expressed in 15 out of 16 (93.75%) SDHx tumors, regardless of the F-FDOPA positivity. LAT1 and CD98hc were co-expressed in 6/8 F-FDOPA-negative PPGLs. In contrast, in one case with absence of LAT1/CD98hc, F-FDOPA uptake was positive and attributed to LAT4 expression. CONCLUSIONS: We conclude that down-regulation of LAT1/CD98hc cannot explain the imaging phenotype of SDHx-related PPGLs. A reduced activity of LAT1 remains the primary hypothesis possibly due to a modification of intracellular amino acid content which may reduce F-FDOPA uptake.
[Mh] Termos MeSH primário: Neoplasias das Glândulas Suprarrenais/diagnóstico por imagem
Sistema L de Transporte de Aminoácidos/genética
Di-Hidroxifenilalanina/análogos & derivados
Genótipo
Paraganglioma/diagnóstico por imagem
Feocromocitoma/diagnóstico por imagem
Tomografia Computadorizada com Tomografia por Emissão de Pósitrons
[Mh] Termos MeSH secundário: Neoplasias das Glândulas Suprarrenais/genética
Idoso
Reações Falso-Negativas
Feminino
Cadeia Pesada da Proteína-1 Reguladora de Fusão/genética
Regulação Neoplásica da Expressão Gênica
Seres Humanos
Mutação
Paraganglioma/genética
Feocromocitoma/genética
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Succinato Desidrogenase/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acid Transport System L); 0 (Fusion Regulatory Protein 1, Heavy Chain); 0 (RNA, Messenger); 2C598205QX (fluorodopa F 18); 63-84-3 (Dihydroxyphenylalanine); EC 1.3.99.1 (Succinate Dehydrogenase)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161201
[St] Status:MEDLINE
[do] DOI:10.1007/s00259-016-3586-z


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[PMID]:27687603
[Au] Autor:Liao Z; Cantor JM
[Ad] Endereço:From the Department of Medicine, University of California San Diego, La Jolla.
[Ti] Título:Endothelial Cells Require CD98 for Efficient Angiogenesis-Brief Report.
[So] Source:Arterioscler Thromb Vasc Biol;36(11):2163-2166, 2016 Nov.
[Is] ISSN:1524-4636
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: CD98 regulates integrin signaling and is critical for tumor cell proliferation. It is also expressed on endothelial cells (EC), but its role in angiogenesis is unclear. APPROACH AND RESULTS: We used specific genetic targeting and antibody blockade approaches to examine the function of CD98 in EC proliferation, blood vessel growth, and tumor angiogenesis. It is upregulated on angiogenic ECs, and EC-specific deletion of CD98 in mice inhibited tumor growth, retinal angiogenesis, and EC proliferation. Reconstitution with CD98 mutants showed that integrin and CD98 interaction is necessary for EC survival and growth. Moreover, anti-CD98 treatment inhibited vessel formation and reversed EC-assisted tumor growth. CONCLUSIONS: Our findings demonstrate a requirement for CD98 in EC growth and suggest that CD98-specific reagents could have a dual anticancer effect: directly by inhibiting tumor cell proliferation and indirectly by preventing tumor angiogenesis.
[Mh] Termos MeSH primário: Carcinoma Pulmonar de Lewis/metabolismo
Cadeia Pesada da Proteína-1 Reguladora de Fusão/metabolismo
Células Endoteliais da Veia Umbilical Humana/metabolismo
Melanoma Experimental/metabolismo
Neovascularização Patológica
Neovascularização Fisiológica
Neovascularização Retiniana/metabolismo
[Mh] Termos MeSH secundário: Inibidores da Angiogênese/farmacologia
Animais
Anticorpos/farmacologia
Carcinoma Pulmonar de Lewis/irrigação sanguínea
Carcinoma Pulmonar de Lewis/tratamento farmacológico
Carcinoma Pulmonar de Lewis/genética
Linhagem Celular Tumoral
Proliferação Celular
Feminino
Cadeia Pesada da Proteína-1 Reguladora de Fusão/genética
Cadeia Pesada da Proteína-1 Reguladora de Fusão/imunologia
Genótipo
Células Endoteliais da Veia Umbilical Humana/efeitos dos fármacos
Células Endoteliais da Veia Umbilical Humana/imunologia
Células Endoteliais da Veia Umbilical Humana/transplante
Seres Humanos
Integrinas/metabolismo
Masculino
Melanoma Experimental/irrigação sanguínea
Melanoma Experimental/tratamento farmacológico
Melanoma Experimental/genética
Camundongos Knockout
Neovascularização Fisiológica/efeitos dos fármacos
Fenótipo
Fosforilação
Neovascularização Retiniana/tratamento farmacológico
Neovascularização Retiniana/genética
Neovascularização Retiniana/patologia
Transdução de Sinais
Fatores de Tempo
Carga Tumoral
Fator A de Crescimento do Endotélio Vascular/farmacologia
Receptor 2 de Fatores de Crescimento do Endotélio Vascular/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Angiogenesis Inhibitors); 0 (Antibodies); 0 (Fusion Regulatory Protein 1, Heavy Chain); 0 (Integrins); 0 (Slc3A2 protein, mouse); 0 (Vascular Endothelial Growth Factor A); EC 2.7.10.1 (KDR protein, human); EC 2.7.10.1 (Vascular Endothelial Growth Factor Receptor-2)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161001
[St] Status:MEDLINE


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[PMID]:26945935
[Au] Autor:de la Ballina LR; Cano-Crespo S; González-Muñoz E; Bial S; Estrach S; Cailleteau L; Tissot F; Daniel H; Zorzano A; Ginsberg MH; Palacín M; Féral CC
[Ad] Endereço:From the Institute for Research in Biomedicine (IRB Barcelona), Barcelona Institute of Science and Technology, Baldiri Reixac 10, 08028 Barcelona, Spain and Department of Biochemistry and Molecular Biology, University of Barcelona, 08028 Barcelona, Spain, INSERM, U1081, Institute for Research on Can
[Ti] Título:Amino Acid Transport Associated to Cluster of Differentiation 98 Heavy Chain (CD98hc) Is at the Cross-road of Oxidative Stress and Amino Acid Availability.
[So] Source:J Biol Chem;291(18):9700-11, 2016 Apr 29.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:CD98hc functions as an amino acid (AA) transporter (together with another subunit) and integrin signaling enhancer. It is overexpressed in highly proliferative cells in both physiological and pathological conditions. CD98hc deletion induces strong impairment of cell proliferation in vivo and in vitro Here, we investigate CD98hc-associated AA transport in cell survival and proliferation. By using chimeric versions of CD98hc, the two functions of the protein can be uncoupled. Although recovering the CD98hc AA transport capacity restores the in vivo and in vitro proliferation of CD98hc-null cells, reconstitution of the integrin signaling function of CD98hc is unable to restore in vitro proliferation of those cells. CD98hc-associated transporters (i.e. xCT, LAT1, and y(+)LAT2 in wild-type cells) are crucial to control reactive oxygen species and intracellular AA levels, thus sustaining cell survival and proliferation. Moreover, in CD98hc-null cells the deficiency of CD98hc/xCT cannot be compensated, leading to cell death by ferroptosis. Supplementation of culture media with ß-mercaptoethanol rescues CD98hc-deficient cell survival. Under such conditions null cells show oxidative stress and intracellular AA imbalance and, consequently, limited proliferation. CD98hc-null cells also present reduced intracellular levels of branched-chain and aromatic amino acids (BCAAs and ARO AAs, respectively) and induced expression of peptide transporter 1 (PEPT1). Interestingly, external supply of dipeptides containing BCAAs and ARO AAs rescues cell proliferation and compensates for impaired uptake of CD98hc/LAT1 and CD98hc/y(+)LAT2. Our data establish CD98hc as a master protective gene at the cross-road of redox control and AA availability, making it a relevant therapeutic target in cancer.
[Mh] Termos MeSH primário: Aminoácidos/metabolismo
Diferenciação Celular/fisiologia
Proliferação Celular/fisiologia
Cadeia Pesada da Proteína-1 Reguladora de Fusão/metabolismo
Células-Tronco Embrionárias Murinas/metabolismo
Estresse Oxidativo
[Mh] Termos MeSH secundário: Sistema y+ de Transporte de Aminoácidos/genética
Sistema y+ de Transporte de Aminoácidos/metabolismo
Aminoácidos/genética
Animais
Transporte Biológico Ativo/fisiologia
Linhagem Celular
Sobrevivência Celular/fisiologia
Cadeia Pesada da Proteína-1 Reguladora de Fusão/genética
Cadeias Leves da Proteína-1 Reguladora de Fusão/genética
Cadeias Leves da Proteína-1 Reguladora de Fusão/metabolismo
Deleção de Genes
Camundongos
Células-Tronco Embrionárias Murinas/citologia
Espécies Reativas de Oxigênio/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Amino Acid Transport System y+); 0 (Amino Acids); 0 (Fusion Regulatory Protein 1, Heavy Chain); 0 (Fusion Regulatory Protein 1, Light Chains); 0 (Reactive Oxygen Species); 0 (SLC7A8 protein, mouse); 0 (Slc7a7 protein, mouse)
[Em] Mês de entrada:1611
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160307
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M115.704254


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[PMID]:26836475
[Au] Autor:Nishio Y; Fujino M; Cai S; Kitajima Y; Saito T; Tsumura H; Ito M; Ito Y; Nagahara Y; Li XK
[Ad] Endereço:Division of Transplantation Immunology, National Research Institute for Child Health and Development, Tokyo, Japan.
[Ti] Título:Impaired CD98 signaling protects against graft-versus-host disease by increasing regulatory T cells.
[So] Source:Transpl Immunol;35:34-9, 2016 Mar.
[Is] ISSN:1878-5492
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Graft-versus-host disease (GvHD) is a major barrier to the broader use of allogenic hematopoietic stem cell transplantation for non-malignant clinical applications. A murine model of C57BL/6 to B6D2F1 acute GvHD was employed with T lymphocytes harboring a deletion of the CD98 heavy chain (CD98hc(-/-)) as donor cells. The CD98hc(-/-) resulted in lower responses to alloantigen stimulation in a mixed leukocyte reaction assay, and prevented the mortality associated with disease progression. The percentage of donor CD8 T lymphocytes was significantly decreased, while the percentage of Foxp3-positive regulatory T cells (Tregs) in recipients was increased by CD98hc(-/-). Decreased expression of FAS, FASL, ICOS, ICOSL, PD-1 and PD-L1 by donor CD8 T cells, and mRNA expression of cytotoxic T cell-related cytokines in the recipients were shown in those with CD98hc(-/-). Fewer infiltrated cells are found in the lungs, liver, tongue and skin of recipients with CD98hc(-/-) compared with the wild type recipients. Taken together, our data indicate that T cell-specific deletion of CD98hc can contribute to the prevention of GvHD development due to the attenuation of lymphocyte migration and by increasing the generation of Treg cells. These findings are expected to make it possible to develop novel approaches for the prevention of GvHD.
[Mh] Termos MeSH primário: Movimento Celular/imunologia
Cadeia Pesada da Proteína-1 Reguladora de Fusão/imunologia
Doença Enxerto-Hospedeiro/imunologia
Transplante de Células-Tronco Hematopoéticas
Transdução de Sinais/imunologia
Linfócitos T Reguladores/imunologia
[Mh] Termos MeSH secundário: Aloenxertos
Animais
Movimento Celular/genética
Feminino
Cadeia Pesada da Proteína-1 Reguladora de Fusão/genética
Doença Enxerto-Hospedeiro/genética
Doença Enxerto-Hospedeiro/patologia
Camundongos
Transdução de Sinais/genética
Linfócitos T Reguladores/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Fusion Regulatory Protein 1, Heavy Chain)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160203
[St] Status:MEDLINE


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[PMID]:26687840
[Au] Autor:Zuchero YJ; Chen X; Bien-Ly N; Bumbaca D; Tong RK; Gao X; Zhang S; Hoyte K; Luk W; Huntley MA; Phu L; Tan C; Kallop D; Weimer RM; Lu Y; Kirkpatrick DS; Ernst JA; Chih B; Dennis MS; Watts RJ
[Ad] Endereço:Department of Neuroscience, Genentech, Inc., 1 DNA Way, South San Francisco, CA 94080, USA. Electronic address: joy.yu929@gmail.com.
[Ti] Título:Discovery of Novel Blood-Brain Barrier Targets to Enhance Brain Uptake of Therapeutic Antibodies.
[So] Source:Neuron;89(1):70-82, 2016 Jan 06.
[Is] ISSN:1097-4199
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The blood-brain barrier (BBB) poses a major challenge for developing effective antibody therapies for neurological diseases. Using transcriptomic and proteomic profiling, we searched for proteins in mouse brain endothelial cells (BECs) that could potentially be exploited to transport antibodies across the BBB. Due to their limited protein abundance, neither antibodies against literature-identified targets nor BBB-enriched proteins identified by microarray facilitated significant antibody brain uptake. Using proteomic analysis of isolated mouse BECs, we identified multiple highly expressed proteins, including basigin, Glut1, and CD98hc. Antibodies to each of these targets were significantly enriched in the brain after administration in vivo. In particular, antibodies against CD98hc showed robust accumulation in brain after systemic dosing, and a significant pharmacodynamic response as measured by brain Aß reduction. The discovery of CD98hc as a robust receptor-mediated transcytosis pathway for antibody delivery to the brain expands the current approaches available for enhancing brain uptake of therapeutic antibodies.
[Mh] Termos MeSH primário: Anticorpos/uso terapêutico
Transporte Biológico/fisiologia
Barreira Hematoencefálica/metabolismo
Encéfalo/metabolismo
Receptores da Transferrina/metabolismo
[Mh] Termos MeSH secundário: Animais
Anticorpos/imunologia
Células Endoteliais/metabolismo
Cadeia Pesada da Proteína-1 Reguladora de Fusão/imunologia
Camundongos
Proteômica/métodos
Transcitose/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies); 0 (Fusion Regulatory Protein 1, Heavy Chain); 0 (Receptors, Transferrin)
[Em] Mês de entrada:1605
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151222
[St] Status:MEDLINE


  10 / 128 MEDLINE  
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[PMID]:26621329
[Au] Autor:Le Vee M; Jouan E; Lecureur V; Fardel O
[Ad] Endereço:Institut de Recherches en Santé, Environnement et Travail (IRSET), UMR INSERM U1085, Faculté de Pharmacie, 2 Avenue du Pr Léon Bernard, 35043 Rennes, France.
[Ti] Título:Aryl hydrocarbon receptor-dependent up-regulation of the heterodimeric amino acid transporter LAT1 (SLC7A5)/CD98hc (SLC3A2) by diesel exhaust particle extract in human bronchial epithelial cells.
[So] Source:Toxicol Appl Pharmacol;290:74-85, 2016 Jan 01.
[Is] ISSN:1096-0333
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The heterodimeric L-type amino acid transporter (LAT) 1/CD98hc is overexpressed in lung cancers with a poor prognosis factor. Factors that contribute to LAT1/CD98hc overexpression in lung cells remain however to be determined, but the implication of atmospheric pollution can be suspected. The present study was therefore designed to analyze the effects of diesel exhaust particle (DEP) extract (DEPe) on LAT1/CD98hc expression in bronchial epithelial BEAS-2B cells. Exposure to DEPe up-regulated LAT1 and CD98hc mRNA levels in a concentration-dependent manner, with DEPe EC50 values (around 0.2 µg/mL) relevant to environmental situations. DEPe concomitantly induced LAT1/CD98hc protein expression and LAT1-mediated leucine accumulation in BEAS-2B cells. Inhibition of the aryl hydrocarbon receptor (AhR) pathway through the use of a chemical AhR antagonist or the siRNA-mediated silencing of AhR expression was next found to prevent DEPe-mediated induction of LAT1/CD98hc, indicating that this regulation depends on AhR, known to be activated by major chemical DEP components like polycyclic aromatic hydrocarbons. DEPe exposure was finally shown to induce mRNA expression and activity of matrix metalloproteinase (MMP)-2 in BEAS-2B cells, in a CD98hc/focal adhesion kinase (FAK)/extracellular regulated kinase (ERK) manner, thus suggesting that DEPe-mediated induction of CD98hc triggers activation of the integrin/FAK/ERK signaling pathway known to be involved in MMP-2 regulation. Taken together, these data demonstrate that exposure to DEPe induces functional overexpression of the amino acid transporter LAT1/CD98hc in lung cells. Such a regulation may participate to pulmonary carcinogenic effects of DEPs, owing to the well-documented contribution of LAT1 and CD98hc to cancer development.
[Mh] Termos MeSH primário: Cadeia Pesada da Proteína-1 Reguladora de Fusão/metabolismo
Transportador 1 de Aminoácidos Neutros Grandes/metabolismo
Pulmão/efeitos dos fármacos
Receptores de Hidrocarboneto Arílico/metabolismo
Regulação para Cima
Emissões de Veículos/toxicidade
[Mh] Termos MeSH secundário: Células Epiteliais/efeitos dos fármacos
Células Epiteliais/metabolismo
Proteína-Tirosina Quinases de Adesão Focal/genética
Proteína-Tirosina Quinases de Adesão Focal/metabolismo
Cadeia Pesada da Proteína-1 Reguladora de Fusão/genética
Seres Humanos
Transportador 1 de Aminoácidos Neutros Grandes/genética
Pulmão/citologia
Pulmão/metabolismo
Metaloproteinase 2 da Matriz/genética
Metaloproteinase 2 da Matriz/metabolismo
Alvo Mecanístico do Complexo 1 de Rapamicina
Complexos Multiproteicos/genética
Complexos Multiproteicos/metabolismo
Hidrocarbonetos Aromáticos Policíclicos/toxicidade
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Receptores de Hidrocarboneto Arílico/genética
Serina-Treonina Quinases TOR/genética
Serina-Treonina Quinases TOR/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fusion Regulatory Protein 1, Heavy Chain); 0 (Large Neutral Amino Acid-Transporter 1); 0 (Multiprotein Complexes); 0 (Polycyclic Aromatic Hydrocarbons); 0 (RNA, Messenger); 0 (Receptors, Aryl Hydrocarbon); 0 (SLC3A2 protein, human); 0 (Vehicle Emissions); EC 2.7.1.1 (TOR Serine-Threonine Kinases); EC 2.7.10.2 (Focal Adhesion Protein-Tyrosine Kinases); EC 2.7.11.1 (Mechanistic Target of Rapamycin Complex 1); EC 3.4.24.24 (MMP2 protein, human); EC 3.4.24.24 (Matrix Metalloproteinase 2)
[Em] Mês de entrada:1605
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151202
[St] Status:MEDLINE



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