Base de dados : MEDLINE
Pesquisa : A11.284.180 [Categoria DeCS]
Referências encontradas : 1312 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 132 ir para página                         

  1 / 1312 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29173819
[Au] Autor:Goudarzi M; Tarbashevich K; Mildner K; Begemann I; Garcia J; Paksa A; Reichman-Fried M; Mahabaleshwar H; Blaser H; Hartwig J; Zeuschner D; Galic M; Bagnat M; Betz T; Raz E
[Ad] Endereço:Institute for Cell Biology, ZMBE, Von-Esmarch-Strasse 56, 48149 Münster, Germany.
[Ti] Título:Bleb Expansion in Migrating Cells Depends on Supply of Membrane from Cell Surface Invaginations.
[So] Source:Dev Cell;43(5):577-587.e5, 2017 Dec 04.
[Is] ISSN:1878-1551
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cell migration is essential for morphogenesis, organ formation, and homeostasis, with relevance for clinical conditions. The migration of primordial germ cells (PGCs) is a useful model for studying this process in the context of the developing embryo. Zebrafish PGC migration depends on the formation of cellular protrusions in form of blebs, a type of protrusion found in various cell types. Here we report on the mechanisms allowing the inflation of the membrane during bleb formation. We show that the rapid expansion of the protrusion depends on membrane invaginations that are localized preferentially at the cell front. The formation of these invaginations requires the function of Cdc42, and their unfolding allows bleb inflation and dynamic cell-shape changes performed by migrating cells. Inhibiting the formation and release of the invaginations strongly interfered with bleb formation, cell motility, and the ability of the cells to reach their target.
[Mh] Termos MeSH primário: Membrana Celular/metabolismo
Movimento Celular/fisiologia
Forma Celular/fisiologia
Células Germinativas/citologia
Peixe-Zebra
[Mh] Termos MeSH secundário: Actinas/metabolismo
Animais
Estruturas da Membrana Celular/metabolismo
Extensões da Superfície Celular/metabolismo
Células Germinativas/metabolismo
Peixe-Zebra/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Actins)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180104
[Lr] Data última revisão:
180104
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171128
[St] Status:MEDLINE


  2 / 1312 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28467320
[Au] Autor:Tarle V; Gauquelin E; Vedula SRK; D'Alessandro J; Lim CT; Ladoux B; Gov NS
[Ad] Endereço:Department of Chemical Physics, Weizmann Institute of Science, Rehovot 76100, Israel.
[Ti] Título:Modeling collective cell migration in geometric confinement.
[So] Source:Phys Biol;14(3):035001, 2017 May 03.
[Is] ISSN:1478-3975
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Monolayer expansion has generated great interest as a model system to study collective cell migration. During such an expansion the culture front often develops 'fingers', which we have recently modeled using a proposed feedback between the curvature of the monolayer's leading edge and the outward motility of the edge cells. We show that this model is able to explain the puzzling observed increase of collective cellular migration speed of a monolayer expanding into thin stripes, as well as describe the behavior within different confining geometries that were recently observed in experiments. These comparisons give support to the model and emphasize the role played by the edge cells and the edge shape during collective cell motion.
[Mh] Termos MeSH primário: Movimento Celular
Extensões da Superfície Celular/fisiologia
Modelos Biológicos
[Mh] Termos MeSH secundário: Animais
Fenômenos Biomecânicos
Técnicas de Cultura de Células
Simulação por Computador
Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171226
[Lr] Data última revisão:
171226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE
[do] DOI:10.1088/1478-3975/aa6591


  3 / 1312 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28924004
[Au] Autor:Farahnak S; McGovern TK; Kim R; O'Sullivan M; Chen B; Lee M; Yoshie H; Wang A; Jang J; Al Heialy S; Lauzon AM; Martin JG
[Ad] Endereço:Meakins-Christie Laboratories, Translational Research in Respiratory Diseases Program, The Research Institute of the McGill University Health Centre, Montreal, Quebec H4A 3J1, Canada; and.
[Ti] Título:Basic Fibroblast Growth Factor 2 Is a Determinant of CD4 T Cell-Airway Smooth Muscle Cell Communication through Membrane Conduits.
[So] Source:J Immunol;199(9):3086-3093, 2017 Nov 01.
[Is] ISSN:1550-6606
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Activated CD4 T cells connect to airway smooth muscle cells (ASMCs) in vitro via lymphocyte-derived membrane conduits (LMCs) structurally similar to membrane nanotubes with unknown intercellular signals triggering their formation. We examined the structure and function of CD4 T cell-derived LMCs, and we established a role for ASMC-derived basic fibroblast growth factor 2 (FGF2b) and FGF receptor (FGFR)1 in LMC formation. Blocking FGF2b's synthesis and FGFR1 function reduced LMC formation. Mitochondrial flux from ASMCs to T cells was partially FGF2b and FGFR1 dependent. LMC formation by CD4 T cells and mitochondrial transfer from ASMCs was increased in the presence of asthmatic ASMCs that expressed more mRNA for FGF2b compared with normal ASMCs. These observations identify ASMC-derived FGF2b as a factor needed for LMC formation by CD4 T cells, affecting intercellular communication.
[Mh] Termos MeSH primário: Linfócitos T CD4-Positivos/imunologia
Comunicação Celular/imunologia
Extensões da Superfície Celular/imunologia
Fator 2 de Crescimento de Fibroblastos/imunologia
Miócitos de Músculo Liso/imunologia
[Mh] Termos MeSH secundário: Linfócitos T CD4-Positivos/citologia
Seres Humanos
Mitocôndrias/imunologia
Miócitos de Músculo Liso/citologia
Receptor Tipo 1 de Fator de Crescimento de Fibroblastos/imunologia
Sistema Respiratório/citologia
Sistema Respiratório/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
103107-01-3 (Fibroblast Growth Factor 2); EC 2.7.10.1 (FGFR1 protein, human); EC 2.7.10.1 (Receptor, Fibroblast Growth Factor, Type 1)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171026
[Lr] Data última revisão:
171026
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170920
[St] Status:MEDLINE
[do] DOI:10.4049/jimmunol.1700164


  4 / 1312 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28803726
[Au] Autor:Solis GP; Bilousov O; Koval A; Lüchtenborg AM; Lin C; Katanaev VL
[Ad] Endereço:Department of Pharmacology and Toxicology, University of Lausanne, CH-1011 Lausanne, Switzerland. Electronic address: gonzalo.solis@unil.ch.
[Ti] Título:Golgi-Resident Gαo Promotes Protrusive Membrane Dynamics.
[So] Source:Cell;170(5):939-955.e24, 2017 Aug 24.
[Is] ISSN:1097-4172
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:To form protrusions like neurites, cells must coordinate their induction and growth. The first requires cytoskeletal rearrangements at the plasma membrane (PM), the second requires directed material delivery from cell's insides. We find that the Gαo-subunit of heterotrimeric G proteins localizes dually to PM and Golgi across phyla and cell types. The PM pool of Gαo induces, and the Golgi pool feeds, the growing protrusions by stimulated trafficking. Golgi-residing KDELR binds and activates monomeric Gαo, atypically for G protein-coupled receptors that normally act on heterotrimeric G proteins. Through multidimensional screenings identifying > 250 Gαo interactors, we pinpoint several basic cellular activities, including vesicular trafficking, as being regulated by Gαo. We further find small Golgi-residing GTPases Rab1 and Rab3 as direct effectors of Gαo. This KDELR → Gαo → Rab1/3 signaling axis is conserved from insects to mammals and controls material delivery from Golgi to PM in various cells and tissues.
[Mh] Termos MeSH primário: Membrana Celular/metabolismo
Extensões da Superfície Celular/metabolismo
Subunidades alfa Gi-Go de Proteínas de Ligação ao GTP/metabolismo
Complexo de Golgi/metabolismo
[Mh] Termos MeSH secundário: Animais
Linhagem Celular
Drosophila
Feminino
GTP Fosfo-Hidrolases/metabolismo
Seres Humanos
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Neuritos/metabolismo
Receptores Acoplados a Proteínas-G/metabolismo
Receptores de Peptídeos/metabolismo
Técnicas do Sistema de Duplo-Híbrido
Proteínas rab1 de Ligação ao GTP/metabolismo
Proteínas rab3 de Ligação ao GTP/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Receptors, G-Protein-Coupled); 0 (Receptors, Peptide); EC 3.6.1.- (GTP Phosphohydrolases); EC 3.6.5.1 (GTP-Binding Protein alpha Subunits, Gi-Go); EC 3.6.5.2 (rab1 GTP-Binding Proteins); EC 3.6.5.2 (rab3 GTP-Binding Proteins)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171005
[Lr] Data última revisão:
171005
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170815
[St] Status:MEDLINE


  5 / 1312 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28688208
[Au] Autor:Schoppmeyer R; Zhao R; Cheng H; Hamed M; Liu C; Zhou X; Schwarz EC; Zhou Y; Knörck A; Schwär G; Ji S; Liu L; Long J; Helms V; Hoth M; Yu X; Qu B
[Ad] Endereço:Biophysics, Center for Integrative Physiology and Molecular Medicine, School of Medicine, Saarland University, Homburg, Germany.
[Ti] Título:Human profilin 1 is a negative regulator of CTL mediated cell-killing and migration.
[So] Source:Eur J Immunol;47(9):1562-1572, 2017 Sep.
[Is] ISSN:1521-4141
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:The actin-binding protein profilin1 (PFN1) plays a central role in actin dynamics, which is essential for cytotoxic T lymphocyte (CTL) functions. The functional role of PFN1 in CTLs, however still remains elusive. Here, we identify PFN1 as the only member of the profilin family expressed in primary human CD8 T cells. Using in vitro assays, we find that PFN1 is a negative regulator of CTL-mediated elimination of target cells. Furthermore, PFN1 is involved in activation-induced lytic granule (LG) release, CTL migration and modulation of actin structures at the immunological synapse (IS). During CTL migration, PFN1 modulates the velocity, protrusion formation patterns and protrusion sustainability. In contrast, PFN1 does not significantly affect migration persistence and the rates of protrusion emergence and retraction. Under in vitro conditions mimicking a tumor microenvironment, we show that PFN1 downregulation promotes CTL invasion into a 3D matrix, without affecting the viability of CTLs in a hydrogen peroxide-enriched microenvironment. Highlighting its potential relevance in cancer, we find that in pancreatic cancer patients, PFN1 expression is substantially decreased in peripheral CD8 T cells. Taken together, we conclude that PFN1 is a negative regulator for CTL-mediated cytotoxicity and may have an impact on CTL functionality in a tumor-related context.
[Mh] Termos MeSH primário: Movimento Celular
Extensões da Superfície Celular/ultraestrutura
Matriz Extracelular/metabolismo
Sinapses Imunológicas/ultraestrutura
Neoplasias Pancreáticas/imunologia
Profilinas/metabolismo
Linfócitos T Citotóxicos/imunologia
[Mh] Termos MeSH secundário: Citoesqueleto de Actina/ultraestrutura
Antígenos CD8/metabolismo
Células Cultivadas
Citotoxicidade Imunológica
Regulação para Baixo
Regulação Neoplásica da Expressão Gênica
Seres Humanos
Peróxido de Hidrogênio/metabolismo
Ativação Linfocitária
Neoplasias Pancreáticas/genética
Profilinas/imunologia
Linfócitos T Citotóxicos/ultraestrutura
Microambiente Tumoral
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CD8 Antigens); 0 (Profilins); BBX060AN9V (Hydrogen Peroxide)
[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:170709
[St] Status:MEDLINE
[do] DOI:10.1002/eji.201747124


  6 / 1312 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28301477
[Au] Autor:Falkenberg CV; Azeloglu EU; Stothers M; Deerinck TJ; Chen Y; He JC; Ellisman MH; Hone JC; Iyengar R; Loew LM
[Ad] Endereço:R. D. Berlin Center for Cell Analysis & Modeling, U. Connecticut School of Medicine, Farmington, CT, United States of America.
[Ti] Título:Fragility of foot process morphology in kidney podocytes arises from chaotic spatial propagation of cytoskeletal instability.
[So] Source:PLoS Comput Biol;13(3):e1005433, 2017 Mar.
[Is] ISSN:1553-7358
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Kidney podocytes' function depends on fingerlike projections (foot processes) that interdigitate with those from neighboring cells to form the glomerular filtration barrier. The integrity of the barrier depends on spatial control of dynamics of actin cytoskeleton in the foot processes. We determined how imbalances in regulation of actin cytoskeletal dynamics could result in pathological morphology. We obtained 3-D electron microscopy images of podocytes and used quantitative features to build dynamical models to investigate how regulation of actin dynamics within foot processes controls local morphology. We find that imbalances in regulation of actin bundling lead to chaotic spatial patterns that could impair the foot process morphology. Simulation results are consistent with experimental observations for cytoskeletal reconfiguration through dysregulated RhoA or Rac1, and they predict compensatory mechanisms for biochemical stability. We conclude that podocyte morphology, optimized for filtration, is intrinsically fragile, whereby local transient biochemical imbalances may lead to permanent morphological changes associated with pathophysiology.
[Mh] Termos MeSH primário: Citoesqueleto de Actina/patologia
Citoesqueleto de Actina/fisiologia
Extensões da Superfície Celular/patologia
Modelos Biológicos
Podócitos/patologia
Podócitos/fisiologia
[Mh] Termos MeSH secundário: Polaridade Celular
Tamanho Celular
Extensões da Superfície Celular/fisiologia
Células Cultivadas
Simulação por Computador
Seres Humanos
Dinâmica não Linear
Análise Espaço-Temporal
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171114
[Lr] Data última revisão:
171114
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170317
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pcbi.1005433


  7 / 1312 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28263956
[Au] Autor:Lilja J; Zacharchenko T; Georgiadou M; Jacquemet G; De Franceschi N; Peuhu E; Hamidi H; Pouwels J; Martens V; Nia FH; Beifuss M; Boeckers T; Kreienkamp HJ; Barsukov IL; Ivaska J
[Ad] Endereço:Turku Centre for Biotechnology, University of Turku, FIN-20520 Turku, Finland.
[Ti] Título:SHANK proteins limit integrin activation by directly interacting with Rap1 and R-Ras.
[So] Source:Nat Cell Biol;19(4):292-305, 2017 Apr.
[Is] ISSN:1476-4679
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:SHANK3, a synaptic scaffold protein and actin regulator, is widely expressed outside of the central nervous system with predominantly unknown function. Solving the structure of the SHANK3 N-terminal region revealed that the SPN domain is an unexpected Ras-association domain with high affinity for GTP-bound Ras and Rap G-proteins. The role of Rap1 in integrin activation is well established but the mechanisms to antagonize it remain largely unknown. Here, we show that SHANK1 and SHANK3 act as integrin activation inhibitors by sequestering active Rap1 and R-Ras via the SPN domain and thus limiting their bioavailability at the plasma membrane. Consistently, SHANK3 silencing triggers increased plasma membrane Rap1 activity, cell spreading, migration and invasion. Autism-related mutations within the SHANK3 SPN domain (R12C and L68P) disrupt G-protein interaction and fail to counteract integrin activation along the Rap1-RIAM-talin axis in cancer cells and neurons. Altogether, we establish SHANKs as critical regulators of G-protein signalling and integrin-dependent processes.
[Mh] Termos MeSH primário: Integrina beta1/metabolismo
Proteínas do Tecido Nervoso/metabolismo
Proteínas rap1 de Ligação ao GTP/metabolismo
Proteínas ras/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Adesão Celular
Linhagem Celular
Movimento Celular
Extensões da Superfície Celular/metabolismo
Feminino
Citometria de Fluxo
Camundongos Endogâmicos C57BL
Modelos Biológicos
Mutação/genética
Proteínas do Tecido Nervoso/química
Proteínas do Tecido Nervoso/genética
Reação em Cadeia da Polimerase
Ligação Proteica
Domínios Proteicos
Ratos Wistar
Alinhamento de Sequência
Talina/metabolismo
Ubiquitinas/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Integrin beta1); 0 (Nerve Tissue Proteins); 0 (SHARPIN protein, human); 0 (Talin); 0 (Ubiquitins); EC 3.6.1.- (RRAS protein, human); EC 3.6.5.2 (rap1 GTP-Binding Proteins); EC 3.6.5.2 (ras Proteins)
[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:170307
[St] Status:MEDLINE
[do] DOI:10.1038/ncb3487


  8 / 1312 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28251924
[Au] Autor:Dey SK; Singh RK; Chattoraj S; Saha S; Das A; Bhattacharyya K; Sengupta K; Sen S; Jana SS
[Ad] Endereço:Department of Biological Chemistry, Indian Association for the Cultivation of Science, Jadavpur, Kolkata 700032, India.
[Ti] Título:Differential role of nonmuscle myosin II isoforms during blebbing of MCF-7 cells.
[So] Source:Mol Biol Cell;28(8):1034-1042, 2017 Apr 15.
[Is] ISSN:1939-4586
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Bleb formation has been correlated with nonmuscle myosin II (NM-II) activity. Whether three isoforms of NM-II (NM-IIA, -IIB and -IIC) have the same or differential roles in bleb formation is not well understood. Here we report that ectopically expressed, GFP-tagged NM-II isoforms exhibit different types of membrane protrusions, such as multiple blebs, lamellipodia, combinations of both, or absence of any such protrusions in MCF-7 cells. Quantification suggests that 50% of NM-IIA-GFP-, 29% of NM-IIB-GFP-, and 19% of NM-IIC1-GFP-expressing MCF-7 cells show multiple bleb formation, compared with 36% of cells expressing GFP alone. Of interest, NM-IIB has an almost 50% lower rate of dissociation from actin filament than NM-IIA and -IIC1 as determined by FRET analysis both at cell and bleb cortices. We induced bleb formation by disruption of the cortex and found that all three NM-II-GFP isoforms can reappear and form filaments but to different degrees in the growing bleb. NM-IIB-GFP can form filaments in blebs in 41% of NM-IIB-GFP-expressing cells, whereas filaments form in only 12 and 3% of cells expressing NM-IIA-GFP and NM-IIC1-GFP, respectively. These studies suggest that NM-II isoforms have differential roles in the bleb life cycle.
[Mh] Termos MeSH primário: Extensões da Superfície Celular/metabolismo
Miosina não Muscular Tipo IIA/metabolismo
Miosina não Muscular Tipo IIB/metabolismo
[Mh] Termos MeSH secundário: Citoesqueleto de Actina/metabolismo
Linhagem Celular Tumoral
Movimento Celular/fisiologia
Citoesqueleto/metabolismo
Seres Humanos
Células MCF-7
Isoformas de Proteínas
Pseudópodes/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Protein Isoforms); EC 3.6.1.- (Nonmuscle Myosin Type IIA); EC 3.6.1.- (Nonmuscle Myosin Type IIB)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170714
[Lr] Data última revisão:
170714
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170303
[St] Status:MEDLINE
[do] DOI:10.1091/mbc.E16-07-0524


  9 / 1312 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28250113
[Au] Autor:Pacitto R; Gaeta I; Swanson JA; Yoshida S
[Ad] Endereço:Department of Microbiology and Immunology, University of Michigan Medical School, Ann Arbor, Michigan, USA.
[Ti] Título:CXCL12-induced macropinocytosis modulates two distinct pathways to activate mTORC1 in macrophages.
[So] Source:J Leukoc Biol;101(3):683-692, 2017 Mar.
[Is] ISSN:1938-3673
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Although growth factors and chemokines elicit different overall effects on cells-growth and chemotaxis, respectively-and activate distinct classes of cell-surface receptors, nonetheless, they trigger similar cellular activities and signaling pathways. The growth factor M-CSF and the chemokine CXCL12 both stimulate the endocytic process of macropinocytosis, and both activate the mechanistic target of rapamycin complex 1 (mTORC1), a protein complex that regulates cell metabolism. Recent studies of signaling by M-CSF in macrophages identified a role for macropinocytosis in the activation of mTORC1, in which delivery of extracellular amino acids into lysosomes via macropinocytosis was required for activation of mTORC1. Here, we analyzed the regulation of macropinosome (MP) formation in response to CXCL12 and identified 2 roles for macropinocytosis in the activation of mTORC1. Within 5 min of adding CXCL12, murine macrophages increased ruffling, macropinocytosis and amino acid-dependent activation of mTORC1. Inhibitors of macropinocytosis blocked activation of mTORC1, and various isoform-specific inhibitors of type 1 PI3K and protein kinase C (PKC) showed similar patterns of inhibition of macropinocytosis and mTORC1 activity. However, unlike the response to M-CSF, Akt phosphorylation (pAkt) in response to CXCL12 required the actin cytoskeleton and the formation of macropinocytic cups. Quantitative fluorescence microscopy showed that phosphatidylinositol (3,4,5)-trisphosphate (PIP ), a product of PI3K and an upstream activator of Akt, localized to macropinocytic cups and that pAkt occurred primarily in cups. These results indicate that CXCL12 activates mTORC1 via 2 mechanisms: 1) that the macropinocytic cup localizes Akt signaling and 2) that MPs convey extracellular nutrients to lysosomes.
[Mh] Termos MeSH primário: Quimiocina CXCL12/farmacologia
Macrófagos/citologia
Macrófagos/metabolismo
Complexos Multiproteicos/metabolismo
Pinocitose/efeitos dos fármacos
Transdução de Sinais/efeitos dos fármacos
Serina-Treonina Quinases TOR/metabolismo
[Mh] Termos MeSH secundário: Aminoácidos/metabolismo
Animais
Células da Medula Óssea/citologia
Extensões da Superfície Celular/efeitos dos fármacos
Extensões da Superfície Celular/metabolismo
Espaço Extracelular/metabolismo
Isoenzimas/metabolismo
Macrófagos/efeitos dos fármacos
Alvo Mecanístico do Complexo 1 de Rapamicina
Camundongos Endogâmicos C57BL
Modelos Biológicos
Fosfatidilinositol 3-Quinases/metabolismo
Fosforilação/efeitos dos fármacos
Inibidores de Proteínas Quinases/farmacologia
Proteínas Proto-Oncogênicas c-akt/metabolismo
Proteínas Quinases S6 Ribossômicas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acids); 0 (Chemokine CXCL12); 0 (Isoenzymes); 0 (Multiprotein Complexes); 0 (Protein Kinase Inhibitors); EC 2.7.1.- (Phosphatidylinositol 3-Kinases); EC 2.7.1.1 (TOR Serine-Threonine Kinases); EC 2.7.11.1 (Mechanistic Target of Rapamycin Complex 1); EC 2.7.11.1 (Proto-Oncogene Proteins c-akt); EC 2.7.11.1 (Ribosomal Protein S6 Kinases)
[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:170303
[St] Status:MEDLINE
[do] DOI:10.1189/jlb.2A0316-141RR


  10 / 1312 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28228548
[Au] Autor:Ramirez-San Juan GR; Oakes PW; Gardel ML
[Ad] Endereço:Graduate Program in Biophysical Sciences, University of Chicago, Chicago, IL 60637.
[Ti] Título:Contact guidance requires spatial control of leading-edge protrusion.
[So] Source:Mol Biol Cell;28(8):1043-1053, 2017 Apr 15.
[Is] ISSN:1939-4586
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In vivo, geometric cues from the extracellular matrix (ECM) are critical for the regulation of cell shape, adhesion, and migration. During contact guidance, the fibrillar architecture of the ECM promotes an elongated cell shape and migration along the fibrils. The subcellular mechanisms by which cells sense ECM geometry and translate it into changes in shape and migration direction are not understood. Here we pattern linear fibronectin features to mimic fibrillar ECM and elucidate the mechanisms of contact guidance. By systematically varying patterned line spacing, we show that a 2-µm spacing is sufficient to promote cell shape elongation and migration parallel to the ECM, or contact guidance. As line spacing is increased, contact guidance increases without affecting migration speed. To elucidate the subcellular mechanisms of contact guidance, we analyze quantitatively protrusion dynamics and find that the structured ECM orients cellular protrusions parallel to the ECM. This spatial organization of protrusion relies on myosin II contractility, and feedback between adhesion and Rac-mediated protrusive activity, such that we find Arp2/3 inhibition can promote contact guidance. Together our data support a model for contact guidance in which the ECM enforces spatial constraints on the lamellipodia that result in cell shape elongation and enforce migration direction.
[Mh] Termos MeSH primário: Movimento Celular/fisiologia
Extensões da Superfície Celular/fisiologia
Matriz Extracelular/fisiologia
Orientação Espacial/fisiologia
[Mh] Termos MeSH secundário: Actinas/metabolismo
Animais
Adesão Celular/fisiologia
Comunicação Celular/fisiologia
Forma Celular/fisiologia
Extensões da Superfície Celular/metabolismo
Matriz Extracelular/metabolismo
Fibronectinas/metabolismo
Integrinas/metabolismo
Camundongos
Miosina Tipo II/metabolismo
Células NIH 3T3
Proteínas rac1 de Ligação ao GTP/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Actins); 0 (Fibronectins); 0 (Integrins); EC 3.6.1.- (Myosin Type II); EC 3.6.5.2 (rac1 GTP-Binding Protein)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171018
[Lr] Data última revisão:
171018
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170224
[St] Status:MEDLINE
[do] DOI:10.1091/mbc.E16-11-0769



página 1 de 132 ir para página                         
   


Refinar a pesquisa
  Base de dados : MEDLINE Formulário avançado   

    Pesquisar no campo  
1  
2
3
 
           



Search engine: iAH v2.6 powered by WWWISIS

BIREME/OPAS/OMS - Centro Latino-Americano e do Caribe de Informação em Ciências da Saúde