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Pesquisa : A11.284.430.214.190.500 [Categoria DeCS]
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  1 / 21206 MEDLINE  
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[PMID]:28471021
[Au] Autor:Spessott WA; Sanmillan ML; Kulkarni VV; McCormick ME; Giraudo CG
[Ad] Endereço:Department of Pathology and Laboratory Medicine, University of Pennsylvania - The Children's Hospital of Philadelphia, Philadelphia, Pennsylvania.
[Ti] Título:Syntaxin 4 mediates endosome recycling for lytic granule exocytosis in cytotoxic T-lymphocytes.
[So] Source:Traffic;18(7):442-452, 2017 Jul.
[Is] ISSN:1600-0854
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Adaptive and innate immunity utilize the perforin-killing pathway to eliminate virus-infected or cancer cells. Cytotoxic T-lymphocytes (CTLs) and natural killer cells mediate this process by releasing toxic proteins at the contact area with target cells known as immunological synapse (IS). Formation of a stable IS and exocytosis of toxic proteins requires persistent fusion of Rab11a recycling endosomes with the plasma membrane (PM) that may assure the delivery of key effector proteins. Despite the importance of the recycling endosomal compartment, the membrane fusion proteins that control this process at the IS remain elusive. Here, by performing knockdown experiments we found that syntaxin 4 (STX4) is necessary for cytotoxic activity and CD107a degranulation against target cells in a similar fashion to syntaxin 11, which is involved in lytic granule (LG) exocytosis and immunodeficiency when it is mutated. Using total internal reflection fluorescent microscopy we identified that STX4 mediates fusion of EGFP-Rab11a vesicles at the IS. Immunoprecipitation experiments in lysates of activated CTLs indicate that endogenous STX4 may drive this fusion step by interacting with cognate proteins: Munc18-3/SNAP23/VAMP7 and/or VAMP8. These results reveal the role of STX4 in mediating fusion of Rab11a endosomes upstream of lytic granules (LGs) exocytosis and further demonstrate the importance of this pathway in controlling CTL-mediated cytotoxicity.
[Mh] Termos MeSH primário: Grânulos Citoplasmáticos/metabolismo
Endossomos/metabolismo
Exocitose/imunologia
Proteínas Qa-SNARE/metabolismo
Linfócitos T Citotóxicos/metabolismo
[Mh] Termos MeSH secundário: Degranulação Celular
Linhagem Celular
Grânulos Citoplasmáticos/imunologia
Citotoxicidade Imunológica
Técnicas de Silenciamento de Genes
Seres Humanos
Proteína 1 de Membrana Associada ao Lisossomo/metabolismo
Transporte Proteico
Proteínas Qa-SNARE/genética
Linfócitos T Citotóxicos/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Lysosomal-Associated Membrane Protein 1); 0 (Qa-SNARE Proteins)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180308
[Lr] Data última revisão:
180308
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.1111/tra.12490


  2 / 21206 MEDLINE  
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[PMID]:28746974
[Au] Autor:Sheinberger J; Shav-Tal Y
[Ad] Endereço:The Mina & Everard Goodman Faculty of Life Sciences, Institute of Nanotechnology, Bar-Ilan University, Ramat Gan, Israel.
[Ti] Título:mRNPs meet stress granules.
[So] Source:FEBS Lett;591(17):2534-2542, 2017 09.
[Is] ISSN:1873-3468
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Stress granules are cytoplasmic structures that form in response to a variety of cellular stresses. They contain mRNAs and many proteins including numerous types of RNA-binding proteins, and have been studied in connection to major cellular events such as protein synthesis as well as disease. Despite the well-known fact that stress granules encapsulate mRNPs (mRNA-protein complexes), much of the research has naturally focused on the protein components of stress granules. The specific details of mRNP entry into and exit from stress granules and the functional reasons for these dynamics are not fully understood. Here, we review studies that have concentrated on the aspects of mRNP accumulation in stress granules and produced quantitative data concerning mRNP/stress granule interactions.
[Mh] Termos MeSH primário: Grânulos Citoplasmáticos/metabolismo
Ribonucleoproteínas/metabolismo
[Mh] Termos MeSH secundário: Animais
Doença/genética
Seres Humanos
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (RNA, Messenger); 0 (Ribonucleoproteins); 0 (messenger ribonucleoprotein)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:180302
[Lr] Data última revisão:
180302
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170727
[St] Status:MEDLINE
[do] DOI:10.1002/1873-3468.12765


  3 / 21206 MEDLINE  
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[PMID]:28870733
[Au] Autor:Stenger B; Gerber A; Bernhardt R; Hannemann F
[Ad] Endereço:Institute of Biochemistry, Saarland University, Saarbrücken, Germany.
[Ti] Título:Functionalized poly(3-hydroxybutyric acid) bodies as new in vitro biocatalysts.
[So] Source:Biochim Biophys Acta;1866(1):52-59, 2018 01.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Cytochromes P450 play a key role in the drug and steroid metabolism in the human body. This leads to a high interest in this class of proteins. Mammalian cytochromes P450 are rather delicate. Due to their localization in the mitochondrial or microsomal membrane, they tend to aggregate during expression and purification and to convert to an inactive form so that they have to be purified and stored in complex buffers. The complex buffers and low storage temperatures, however, limit the feasibility of fast, automated screening of the corresponding cytochrome P450-effector interactions, which are necessary to study substrate-protein and inhibitor-protein interactions. Here, we present the production and isolation of functionalized poly(3-hydroxybutyrate) granules (PHB bodies) from Bacillus megaterium MS941 strain. In contrast to the expression in Escherichia coli, where mammalian cytochromes P450 are associated to the cell membrane, when CYP11A1 is heterologously expressed in Bacillus megaterium, it is located on the PHB bodies. The surface of these particles provides a matrix for immobilization and stabilization of the CYP11A1 during the storage of the protein and substrate conversion. It was demonstrated that the PHB polymer basis is inert concerning the performed conversion. Immobilization of the CYP11A1 onto the PHB bodies allows freeze-drying of the complex without significant decrease of the CYP11A1 activity. This is the first lyophilization of a mammalian cytochrome P450, which allows storage over more than 18days at 4°C instead of storage at -80°C. In addition, we were able to immobilize the cytochrome P450 on the PHB bodies in vitro. In this case the expression of the protein is separated from the production of the immobilization matrix, which widens the application of this method. This article is part of a Special Issue entitled: Cytochrome P450 biodiversity and biotechnology, edited by Erika Plettner, Gianfranco Gilardi, Luet Wong, Vlada Urlacher, Jared Goldstone.
[Mh] Termos MeSH primário: Ácido 3-Hidroxibutírico/química
Bacillus megaterium/genética
Biotecnologia/métodos
Enzima de Clivagem da Cadeia Lateral do Colesterol/química
Proteínas Imobilizadas/biossíntese
Proteínas Mitocondriais/biossíntese
[Mh] Termos MeSH secundário: Ácido 3-Hidroxibutírico/biossíntese
Animais
Bacillus megaterium/enzimologia
Biocatálise
Bovinos
Colesterol/química
Colesterol/metabolismo
Enzima de Clivagem da Cadeia Lateral do Colesterol/genética
Enzima de Clivagem da Cadeia Lateral do Colesterol/metabolismo
Grânulos Citoplasmáticos/química
Liofilização
Expressão Gênica
Proteínas Imobilizadas/química
Proteínas Imobilizadas/genética
Proteínas Mitocondriais/química
Proteínas Mitocondriais/genética
Pregnenolona/biossíntese
Pregnenolona/química
Refrigeração
Transgenes
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Immobilized Proteins); 0 (Mitochondrial Proteins); 73R90F7MQ8 (Pregnenolone); 97C5T2UQ7J (Cholesterol); EC 1.14.15.6 (Cholesterol Side-Chain Cleavage Enzyme); TZP1275679 (3-Hydroxybutyric Acid)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180208
[Lr] Data última revisão:
180208
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170906
[St] Status:MEDLINE


  4 / 21206 MEDLINE  
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[PMID]:29200150
[Au] Autor:Lukefahr AL; Proytcheva M
[Ad] Endereço:Department of Pathology, The University of Arizona College of Medicine, Tucson/Banner University Medical Center-Tucson, Tucson, AZ.
[Ti] Título:Alder-Reilly Anomaly in the Cerebrospinal Fluid of a Child With Hurler Syndrome.
[So] Source:J Pediatr Hematol Oncol;40(1):74-75, 2018 Jan.
[Is] ISSN:1536-3678
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Hurler syndrome is an autosomal recessive mucopolysaccharidosis characterized by intralysosomal accumulation of glycosaminoglycan fragments, with cellular accumulation of distended lysosomes resulting in interference with normal cell function. One of the peripheral blood features of mucopolysaccharidoses is the presence of numerous, dark lilac granules within lymphocytes, monocytes, and neutrophils, also known at Alder-Reilly anomaly. Here we describe intracytoplasmic granules with haloes in mononuclear cells present in the cerebrospinal fluid of a 2-year-old boy with the diagnosis of Hurler syndrome, undergoing pretransplant evaluation for an unrelated donor cord blood stem cell transplant.
[Mh] Termos MeSH primário: Líquido Cefalorraquidiano/citologia
Grânulos Citoplasmáticos/patologia
Leucócitos/patologia
Mucopolissacaridose I/complicações
[Mh] Termos MeSH secundário: Pré-Escolar
Evolução Fatal
Transplante de Células-Tronco Hematopoéticas
Seres Humanos
Leucócitos/ultraestrutura
Masculino
Mucopolissacaridose I/diagnóstico
Sepse
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180112
[Lr] Data última revisão:
180112
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171205
[St] Status:MEDLINE
[do] DOI:10.1097/MPH.0000000000001041


  5 / 21206 MEDLINE  
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[PMID]:29096075
[Au] Autor:Parchure A; Munson M; Budnik V
[Ad] Endereço:Department of Neurobiology, University of Massachusetts Medical School, Worcester, MA, USA.
[Ti] Título:Getting mRNA-Containing Ribonucleoprotein Granules Out of a Nuclear Back Door.
[So] Source:Neuron;96(3):604-615, 2017 Nov 01.
[Is] ISSN:1097-4199
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:A pivotal feature of long-lasting synaptic plasticity is the localization of RNAs and the protein synthesis machinery at synaptic sites. How and where ribonucleoprotein (RNP) transport granules that support this synthetic activity are formed is of fundamental importance. The prevailing model poses that the nuclear pore complex (NPC) is the sole gatekeeper for transit of cellular material in and out of the nucleus. However, insights from the nuclear assembly of large viral capsids highlight a back door route for nuclear escape, a process referred to nuclear envelope (NE) budding. Recent studies indicate that NE budding might be an endogenous cellular process for the nuclear export of very large RNPs and protein aggregates. In Drosophila, this mechanism is required for synaptic plasticity, but its role may extend beyond the nervous system, in tissues where local changes in translation are required. Here we discuss these recent findings and a potential relationship between NE budding and the NPC.
[Mh] Termos MeSH primário: Transporte Ativo do Núcleo Celular/fisiologia
Núcleo Celular/metabolismo
Grânulos Citoplasmáticos/metabolismo
RNA Mensageiro/metabolismo
Ribonucleoproteínas/metabolismo
[Mh] Termos MeSH secundário: Animais
Núcleo Celular/genética
Grânulos Citoplasmáticos/genética
Seres Humanos
Membrana Nuclear/genética
Membrana Nuclear/metabolismo
RNA Mensageiro/genética
Ribonucleoproteínas/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (RNA, Messenger); 0 (Ribonucleoproteins)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171113
[Lr] Data última revisão:
171113
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171103
[St] Status:MEDLINE


  6 / 21206 MEDLINE  
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[PMID]:29045428
[Au] Autor:Barraza CE; Solari CA; Marcovich I; Kershaw C; Galello F; Rossi S; Ashe MP; Portela P
[Ad] Endereço:Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales-Consejo Nacional de Investigaciones Científicas y Técnicas (IQUIBICEN-CONICET). Buenos Aires, Argentina.
[Ti] Título:The role of PKA in the translational response to heat stress in Saccharomyces cerevisiae.
[So] Source:PLoS One;12(10):e0185416, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cellular responses to stress stem from a variety of different mechanisms, including translation arrest and relocation of the translationally repressed mRNAs to ribonucleoprotein particles like stress granules (SGs) and processing bodies (PBs). Here, we examine the role of PKA in the S. cerevisiae heat shock response. Under mild heat stress Tpk3 aggregates and promotes aggregation of eIF4G, Pab1 and eIF4E, whereas severe heat stress leads to the formation of PBs and SGs that contain both Tpk2 and Tpk3 and a larger 48S translation initiation complex. Deletion of TPK2 or TPK3 impacts upon the translational response to heat stress of several mRNAs including CYC1, HSP42, HSP30 and ENO2. TPK2 deletion leads to a robust translational arrest, an increase in SGs/PBs aggregation and translational hypersensitivity to heat stress, whereas TPK3 deletion represses SGs/PBs formation, translational arrest and response for the analyzed mRNAs. Therefore, this work provides evidence indicating that Tpk2 and Tpk3 have opposing roles in translational adaptation during heat stress, and highlight how the same signaling pathway can be regulated to generate strikingly distinct physiological outputs.
[Mh] Termos MeSH primário: Subunidades Catalíticas da Proteína Quinase Dependente de AMP Cíclico/metabolismo
Resposta ao Choque Térmico
Biossíntese de Proteínas
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/enzimologia
Estresse Fisiológico
[Mh] Termos MeSH secundário: Proteínas Quinases Dependentes de AMP Cíclico/metabolismo
Grânulos Citoplasmáticos/metabolismo
Agregados Proteicos
Subunidades Proteicas/metabolismo
Frações Subcelulares/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Protein Aggregates); 0 (Protein Subunits); 0 (Saccharomyces cerevisiae Proteins); EC 2.7.11.11 (Cyclic AMP-Dependent Protein Kinase Catalytic Subunits); EC 2.7.11.11 (Cyclic AMP-Dependent Protein Kinases); EC 2.7.11.11 (TPK2 protein, S cerevisiae); EC 2.7.11.11 (Tpk3 protein, S cerevisiae)
[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:171019
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0185416


  7 / 21206 MEDLINE  
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[PMID]:28977508
[Au] Autor:Bailey JK; Shen W; Liang XH; Crooke ST
[Ad] Endereço:Department of Core Antisense Research, Ionis Pharmaceuticals, Inc. 2855 Gazelle Court, Carlsbad, CA 92010, USA.
[Ti] Título:Nucleic acid binding proteins affect the subcellular distribution of phosphorothioate antisense oligonucleotides.
[So] Source:Nucleic Acids Res;45(18):10649-10671, 2017 Oct 13.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Antisense oligonucleotides (ASOs) are versatile tools that can regulate multiple steps of RNA biogenesis in cells and living organisms. Significant improvements in delivery, potency, and stability have been achieved through modifications within the oligonucleotide backbone, sugar and heterocycles. However, these modifications can profoundly affect interactions between ASOs and intracellular proteins in ways that are only beginning to be understood. Here, we report that ASOs with specific backbone and sugar modifications can become localized to cytoplasmic ribonucleoprotein granules such as stress granules and those seeded by the aggregation of specific ASO-binding proteins such as FUS/TLS (FUS) and PSF/SFPQ (PSF). Further investigation into the basis for ASO-FUS binding illustrated the importance of ASO backbone and hydrophobic 2' sugar modifications and revealed that the C-terminal region of FUS is sufficient to retain ASOs in cellular foci. Taken together, the results of this study demonstrate that affinities of various nucleic acid binding domains for ASO depend on chemical modifications and further demonstrate how ASO-protein interactions influence the localization of ASOs.
[Mh] Termos MeSH primário: Oligonucleotídeos Antissenso/análise
Fator de Processamento Associado a PTB/metabolismo
Oligonucleotídeos Fosforotioatos/análise
Proteína FUS de Ligação a RNA/metabolismo
[Mh] Termos MeSH secundário: Linhagem Celular
Núcleo Celular/química
Grânulos Citoplasmáticos/química
Seres Humanos
Mutação
Oligonucleotídeos Antissenso/química
Oligonucleotídeos Antissenso/metabolismo
Fator de Processamento Associado a PTB/genética
Oligonucleotídeos Fosforotioatos/química
Oligonucleotídeos Fosforotioatos/metabolismo
Agregados Proteicos
Ligação Proteica
Proteína-Arginina N-Metiltransferases/metabolismo
Proteína FUS de Ligação a RNA/análise
Proteína FUS de Ligação a RNA/química
Proteína FUS de Ligação a RNA/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Oligonucleotides, Antisense); 0 (PTB-Associated Splicing Factor); 0 (Phosphorothioate Oligonucleotides); 0 (Protein Aggregates); 0 (RNA-Binding Protein FUS); EC 2.1.1.319 (Protein-Arginine N-Methyltransferases)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171107
[Lr] Data última revisão:
171107
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171005
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx709


  8 / 21206 MEDLINE  
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[PMID]:28965817
[Au] Autor:Hubstenberger A; Courel M; Bénard M; Souquere S; Ernoult-Lange M; Chouaib R; Yi Z; Morlot JB; Munier A; Fradet M; Daunesse M; Bertrand E; Pierron G; Mozziconacci J; Kress M; Weil D
[Ad] Endereço:UPMC Univ Paris 06, Institut de Biologie Paris-Seine (IBPS), CNRS UMR 7622, F-75005 Paris, France; Université Côte d'Azur, CNRS, Inserm, iBV, Nice, France. Electronic address: ahubsten@yahoo.fr.
[Ti] Título:P-Body Purification Reveals the Condensation of Repressed mRNA Regulons.
[So] Source:Mol Cell;68(1):144-157.e5, 2017 Oct 05.
[Is] ISSN:1097-4164
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Within cells, soluble RNPs can switch states to coassemble and condense into liquid or solid bodies. Although these phase transitions have been reconstituted in vitro, for endogenous bodies the diversity of the components, the specificity of the interaction networks, and the function of the coassemblies remain to be characterized. Here, by developing a fluorescence-activated particle sorting (FAPS) method to purify cytosolic processing bodies (P-bodies) from human epithelial cells, we identified hundreds of proteins and thousands of mRNAs that structure a dense network of interactions, separating P-body from non-P-body RNPs. mRNAs segregating into P-bodies are translationally repressed, but not decayed, and this repression explains part of the poor genome-wide correlation between RNA and protein abundance. P-bodies condense thousands of mRNAs that strikingly encode regulatory processes. Thus, we uncovered how P-bodies, by condensing and segregating repressed mRNAs, provide a physical substrate for the coordinated regulation of posttranscriptional mRNA regulons.
[Mh] Termos MeSH primário: Regulação da Expressão Gênica
Proteoma/genética
RNA Mensageiro/genética
Regulon
Ribonucleoproteínas/genética
[Mh] Termos MeSH secundário: Fracionamento Celular
Citoplasma/metabolismo
Grânulos Citoplasmáticos/química
Grânulos Citoplasmáticos/metabolismo
Ontologia Genética
Células HEK293
Células HeLa
Seres Humanos
Anotação de Sequência Molecular
Transição de Fase
Biossíntese de Proteínas
Proteoma/metabolismo
Estabilidade de RNA
RNA Mensageiro/metabolismo
Ribonucleoproteínas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Proteome); 0 (RNA, Messenger); 0 (Ribonucleoproteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171017
[Lr] Data última revisão:
171017
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171003
[St] Status:MEDLINE


  9 / 21206 MEDLINE  
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[PMID]:28898277
[Au] Autor:Leftin A; Ben-Chetrit N; Klemm F; Joyce JA; Koutcher JA
[Ad] Endereço:Department of Medical Physics Memorial Sloan Kettering Cancer Center, New York, New York, United States of America.
[Ti] Título:Iron imaging reveals tumor and metastasis macrophage hemosiderin deposits in breast cancer.
[So] Source:PLoS One;12(9):e0184765, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Iron-deposition is a metabolic biomarker of macrophages in both normal and pathological situations, but the presence of iron in tumor and metastasis-associated macrophages is not known. Here we mapped and quantified hemosiderin-laden macrophage (HLM) deposits in murine models of metastatic breast cancer using iron and macrophage histology, and in vivo MRI. Iron MRI detected high-iron pixel clusters in mammary tumors, lung metastasis, and brain metastasis as well as liver and spleen tissue known to contain the HLMs. Iron histology showed these regions to contain clustered macrophages identified by their common iron status and tissue-intrinsic association with other phenotypic macrophage markers. The in vivo MRI and ex vivo histological images were further processed to determine the frequencies and sizes of the iron deposits, and measure the number of HLMs in each deposit to estimate the in vivo MRI sensitivity for these cells. Hemosiderin accumulation is a macrophage biomarker and intrinsic contrast source for cellular MRI associated with the innate function of macrophages in iron metabolism systemically, and in metastatic cancer.
[Mh] Termos MeSH primário: Hemossiderina/metabolismo
Ferro/metabolismo
Macrófagos/metabolismo
Neoplasias Mamárias Experimentais/diagnóstico por imagem
[Mh] Termos MeSH secundário: Animais
Grânulos Citoplasmáticos/metabolismo
Grânulos Citoplasmáticos/patologia
Feminino
Macrófagos/patologia
Imagem por Ressonância Magnética
Neoplasias Mamárias Experimentais/patologia
Camundongos
Metástase Neoplásica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
9011-92-1 (Hemosiderin); E1UOL152H7 (Iron)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171012
[Lr] Data última revisão:
171012
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170913
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0184765


  10 / 21206 MEDLINE  
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[PMID]:28887433
[Au] Autor:Drube S; Grimlowski R; Deppermann C; Fröbel J; Kraft F; Andreas N; Stegner D; Dudeck J; Weber F; Rödiger M; Göpfert C; Drube J; Reich D; Nieswandt B; Dudeck A; Kamradt T
[Ad] Endereço:Institute of Immunology, Jena University Hospital, 07743 Jena, Germany; Sebastian.Drube@med.uni-jena.de.
[Ti] Título:The Neurobeachin-like 2 Protein Regulates Mast Cell Homeostasis.
[So] Source:J Immunol;199(8):2948-2957, 2017 Oct 15.
[Is] ISSN:1550-6606
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The neurobeachin-like 2 protein (Nbeal2) belongs to the family of beige and Chediak-Higashi (BEACH) domain proteins. Loss-of-function mutations in the human gene or Nbeal2 deficiency in mice cause gray platelet syndrome, a bleeding disorder characterized by macrothrombocytopenia, splenomegaly, and paucity of α-granules in megakaryocytes and platelets. We found that in mast cells, Nbeal2 regulates the activation of the Shp1-STAT5 signaling axis and the composition of the c-Kit/STAT signalosome. Furthermore, Nbeal2 mediates granule formation and restricts the expression of the transcription factors, IRF8, GATA2, and MITF as well as of the cell-cycle inhibitor p27, which are essential for mast cell differentiation, proliferation, and cytokine production. These data demonstrate the relevance of Nbeal2 in mast cells above and beyond granule biosynthesis.
[Mh] Termos MeSH primário: Proteínas Sanguíneas/metabolismo
Grânulos Citoplasmáticos/metabolismo
Síndrome da Plaqueta Cinza/genética
Mastócitos/fisiologia
Megacariócitos/fisiologia
[Mh] Termos MeSH secundário: Animais
Proteínas Sanguíneas/genética
Ciclo Celular
Células Cultivadas
Fator de Transcrição GATA2/genética
Fator de Transcrição GATA2/metabolismo
Hemorragia
Fatores Reguladores de Interferon/genética
Fatores Reguladores de Interferon/metabolismo
Camundongos
Camundongos Knockout
Mutação/genética
Proteína Tirosina Fosfatase não Receptora Tipo 6/metabolismo
Proteínas Proto-Oncogênicas c-kit/metabolismo
Fator de Transcrição STAT5/metabolismo
Transdução de Sinais
Esplenomegalia
Trombocitopenia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Blood Proteins); 0 (GATA2 Transcription Factor); 0 (Gata2 protein, mouse); 0 (Interferon Regulatory Factors); 0 (Nbeal2 protein, mouse); 0 (STAT5 Transcription Factor); 0 (interferon regulatory factor-8); EC 2.7.10.1 (Proto-Oncogene Proteins c-kit); EC 3.1.3.48 (Protein Tyrosine Phosphatase, Non-Receptor Type 6)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171101
[Lr] Data última revisão:
171101
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170910
[St] Status:MEDLINE
[do] DOI:10.4049/jimmunol.1700556



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