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[PMID]:28743719
[Au] Autor:Del Prete A; Martínez-Muñoz L; Mazzon C; Toffali L; Sozio F; Za L; Bosisio D; Gazzurelli L; Salvi V; Tiberio L; Liberati C; Scanziani E; Vecchi A; Laudanna C; Mellado M; Mantovani A; Sozzani S
[Ad] Endereço:Department of Molecular and Translational Medicine, University of Brescia, Brescia, Italy.
[Ti] Título:The atypical receptor CCRL2 is required for CXCR2-dependent neutrophil recruitment and tissue damage.
[So] Source:Blood;130(10):1223-1234, 2017 09 07.
[Is] ISSN:1528-0020
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:CCRL2 is a 7-transmembrane domain receptor that shares structural and functional similarities with the family of atypical chemokine receptors (ACKRs). CCRL2 is upregulated by inflammatory signals and, unlike other ACKRs, it is not a chemoattractant-scavenging receptor, does not activate ß-arrestins, and is widely expressed by many leukocyte subsets. Therefore, the biological role of CCRL2 in immunity is still unclear. We report that CCRL2-deficient mice have a defect in neutrophil recruitment and are protected in 2 models of inflammatory arthritis. In vitro, CCRL2 was found to constitutively form homodimers and heterodimers with CXCR2, a main neutrophil chemotactic receptor. By heterodimerization, CCRL2 could regulate membrane expression and promote CXCR2 functions, including the activation of ß2-integrins. Therefore, upregulation of CCRL2 observed under inflammatory conditions is functional to finely tune CXCR2-mediated neutrophil recruitment at sites of inflammation.
[Mh] Termos MeSH primário: Artrite/metabolismo
Artrite/patologia
Neutrófilos/patologia
Receptores de Quimiocinas/metabolismo
Receptores de Interleucina-8B/metabolismo
[Mh] Termos MeSH secundário: Animais
Artrite/complicações
Antígenos CD18/metabolismo
Sobrevivência Celular
Modelos Animais de Doenças
Inflamação/complicações
Inflamação/patologia
Camundongos Knockout
Infiltração de Neutrófilos
Conformação Proteica
Multimerização Proteica
Receptores de Quimiocinas/química
Receptores de Quimiocinas/deficiência
Receptores de Interleucina-8B/química
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (CD18 Antigens); 0 (Ccrl2 protein, mouse); 0 (Receptors, Chemokine); 0 (Receptors, Interleukin-8B)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:180113
[Lr] Data última revisão:
180113
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170727
[St] Status:MEDLINE
[do] DOI:10.1182/blood-2017-04-777680


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[PMID]:28873429
[Au] Autor:Pierce AA; Duwaerts CC; Siao K; Mattis AN; Goodsell A; Baron JL; Maher JJ
[Ad] Endereço:Department of Medicine, University of California, San Francisco, San Francisco, California, United States of America.
[Ti] Título:CD18 deficiency improves liver injury in the MCD model of steatohepatitis.
[So] Source:PLoS One;12(9):e0183912, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Neutrophils and macrophages are important constituents of the hepatic inflammatory infiltrate in non-alcoholic steatohepatitis. These innate immune cells express CD18, an adhesion molecule that facilitates leukocyte activation. In the context of fatty liver, activation of infiltrated leukocytes is believed to enhance hepatocellular injury. The objective of this study was to determine the degree to which activated innate immune cells promote steatohepatitis by comparing hepatic outcomes in wild-type and CD18-mutant mice fed a methionine-choline-deficient (MCD) diet. After 3 weeks of MCD feeding, hepatocyte injury, based on serum ALT elevation, was 40% lower in CD18-mutant than wild-type mice. Leukocyte infiltration into the liver was not impaired in CD18-mutant mice, but leukocyte activation was markedly reduced, as shown by the lack of evidence of oxidant production. Despite having reduced hepatocellular injury, CD18-mutant mice developed significantly more hepatic steatosis than wild-type mice after MCD feeding. This coincided with greater hepatic induction of pro-inflammatory and lipogenic genes as well as a modest reduction in hepatic expression of adipose triglyceride lipase. Overall, the data indicate that CD18 deficiency curbs MCD-mediated liver injury by limiting the activation of innate immune cells in the liver without compromising intrahepatic cytokine activation. Reduced liver injury occurs at the expense of increased hepatic steatosis, which suggests that in addition to damaging hepatocytes, infiltrating leukocytes may influence lipid homeostasis in the liver.
[Mh] Termos MeSH primário: Antígenos CD18/genética
Antígenos CD18/fisiologia
Fígado Gorduroso/metabolismo
[Mh] Termos MeSH secundário: Tecido Adiposo/metabolismo
Animais
Colina/química
Citocinas/metabolismo
Modelos Animais de Doenças
Hepatócitos/citologia
Imunidade Inata
Inflamação
Leucócitos/citologia
Leucócitos/metabolismo
Lipase/metabolismo
Fígado/metabolismo
Masculino
Metionina/química
Camundongos
Camundongos Endogâmicos C57BL
Mutação
Oxigênio/química
Peroxidase/metabolismo
Triglicerídeos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CD18 Antigens); 0 (Cytokines); 0 (Triglycerides); AE28F7PNPL (Methionine); EC 1.11.1.7 (Peroxidase); EC 3.1.1.3 (Lipase); N91BDP6H0X (Choline); S88TT14065 (Oxygen)
[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:170906
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0183912


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[PMID]:28714582
[Au] Autor:Kragstrup TW; Juul-Madsen K; Christiansen SH; Zhang X; Krog J; Vorup-Jensen T; Kjaergaard AG
[Ad] Endereço:Department of Rheumatology, Aarhus University Hospital, Aarhus, Denmark.
[Ti] Título:Altered levels of soluble CD18 may associate immune mechanisms with outcome in sepsis.
[So] Source:Clin Exp Immunol;190(2):258-267, 2017 Nov.
[Is] ISSN:1365-2249
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The pathogenesis of sepsis involves a dual inflammatory response, with a hyperinflammatory phase followed by, or in combination with, a hypoinflammatory phase. The adhesion molecules lymphocyte function-associated antigen (LFA-1) (CD11a/CD18) and macrophage-1 (Mac-1) (CD11b/CD18) support leucocyte adhesion to intercellular adhesion molecules and phagocytosis through complement opsonization, both processes relevant to the immune response during sepsis. Here, we investigate the role of soluble (s)CD18 in sepsis with emphasis on sCD18 as a mechanistic biomarker of immune reactions and outcome of sepsis. sCD18 levels were measured in 15 septic and 15 critically ill non-septic patients. Fifteen healthy volunteers served as controls. CD18 shedding from human mononuclear cells was increased in vitro by several proinflammatory mediators relevant in sepsis. sCD18 inhibited cell adhesion to the complement fragment iC3b, which is a ligand for CD11b/CD18, also known as Mac-1 or complement receptor 3. Serum sCD18 levels in sepsis non-survivors displayed two distinct peaks permitting a partitioning into two groups, namely sCD18 'high' and sCD18 'low', with median levels of sCD18 at 2158 mU/ml [interquartile range (IQR) 2093-2811 mU/ml] and 488 mU/ml (IQR 360-617 mU/ml), respectively, at the day of intensive care unit admission. Serum sCD18 levels partitioned sepsis non-survivors into one group of 'high' sCD18 and low CRP and another group with 'low' sCD18 and high C-reactive protein. Together with the mechanistic data generated in vitro, we suggest the partitioning in sCD18 to reflect a compensatory anti-inflammatory response syndrome and hyperinflammation, respectively, manifested as part of sepsis.
[Mh] Termos MeSH primário: Antígenos CD18/sangue
Sepse/imunologia
Choque Séptico/imunologia
[Mh] Termos MeSH secundário: Adulto
Idoso
Idoso de 80 Anos ou mais
Biomarcadores/sangue
Adesão Celular
Feminino
Seres Humanos
Unidades de Terapia Intensiva
Leucócitos Mononucleares/efeitos dos fármacos
Leucócitos Mononucleares/imunologia
Lipopolissacarídeos/imunologia
Antígeno-1 Associado à Função Linfocitária/metabolismo
Antígeno de Macrófago 1/metabolismo
Masculino
Meia-Idade
Sepse/fisiopatologia
Choque Séptico/fisiopatologia
Resultado do Tratamento
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers); 0 (CD18 Antigens); 0 (Lipopolysaccharides); 0 (Lymphocyte Function-Associated Antigen-1); 0 (Macrophage-1 Antigen)
[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:170718
[St] Status:MEDLINE
[do] DOI:10.1111/cei.13016


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[PMID]:28619950
[Au] Autor:Begandt D; Thome S; Sperandio M; Walzog B
[Ad] Endereço:Walter Brendel Centre of Experimental Medicine, Department of Cardiovascular Physiology and Pathophysiology, Biomedical Center, Ludwig-Maximilians-Universität München, Planegg-Martinsried, Germany.
[Ti] Título:How neutrophils resist shear stress at blood vessel walls: molecular mechanisms, subcellular structures, and cell-cell interactions.
[So] Source:J Leukoc Biol;102(3):699-709, 2017 Sep.
[Is] ISSN:1938-3673
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Neutrophils are the first cells arriving at sites of tissue injury or infection to combat invading pathogens. Successful neutrophil recruitment to sites of inflammation highly depends on specific molecular mechanisms, fine-tuning the received information into signaling pathways and converting them into well-described recruitment steps. This review highlights the impact of vascular flow conditions on neutrophil recruitment and the multitude of mechanisms developed to enable this sophisticated process under wall shear stress conditions. The recruitment process underlies a complex interplay between adhesion and signaling molecules, as well as chemokines, in which neutrophils developed specific mechanisms to travel to sites of lesion in low and high shear stress conditions. Rolling, as the first step in the recruitment process, highly depends on endothelial selectins and their ligands on neutrophils, inducting of intracellular signaling and subsequently activating ß integrins, enabling adhesion and postadhesion events. In addition, subcellular structures, such as microvilli, tethers, and slings allow the cell to arrest, even under high wall shear stress. Thereby, microvilli that are pulled out from the cell body form tethers that develop into slings upon their detachment from the substrate. In addition to the above-described primary capture, secondary capture of neutrophils via neutrophil-neutrophil or neutrophil-platelet interaction promotes the process of neutrophil recruitment to sites of lesion. Thus, precise mechanisms based on a complex molecular interplay, subcellular structures, and cell-cell interactions turn the delicate process of neutrophil trafficking during flow into a robust response allowing effective neutrophil accumulation at sites of injury.
[Mh] Termos MeSH primário: Plaquetas/imunologia
Vasos Sanguíneos/imunologia
Comunicação Celular/imunologia
Neutrófilos/imunologia
Resistência ao Cisalhamento
Estresse Fisiológico/imunologia
[Mh] Termos MeSH secundário: Antígenos CD18/imunologia
Migração e Rolagem de Leucócitos/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (CD18 Antigens)
[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:170617
[St] Status:MEDLINE
[do] DOI:10.1189/jlb.3MR0117-026RR


  5 / 3581 MEDLINE  
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[PMID]:28615221
[Au] Autor:Pick R; Begandt D; Stocker TJ; Salvermoser M; Thome S; Böttcher RT; Montanez E; Harrison U; Forné I; Khandoga AG; Coletti R; Weckbach LT; Brechtefeld D; Haas R; Imhof A; Massberg S; Sperandio M; Walzog B
[Ad] Endereço:Department of Cardiovascular Physiology and Pathophysiology, Walter Brendel Center of Experimental Medicine, Biomedical Center, Ludwig-Maximilians-Universität München, Planegg-Martinsried, Germany.
[Ti] Título:Coronin 1A, a novel player in integrin biology, controls neutrophil trafficking in innate immunity.
[So] Source:Blood;130(7):847-858, 2017 Aug 17.
[Is] ISSN:1528-0020
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Trafficking of polymorphonuclear neutrophils (PMNs) during inflammation critically depends on the ß integrins lymphocyte function-associated antigen 1 (LFA-1) (CD11a/CD18) and macrophage-1 antigen (CD11b/CD18). Here, we identify coronin 1A (Coro1A) as a novel regulator of ß integrins that interacts with the cytoplasmic tail of CD18 and is crucial for induction of PMN adhesion and postadhesion events, including adhesion strengthening, spreading, and migration under flow conditions. Transition of PMN rolling to firm adhesion critically depends on Coro1A by regulating the accumulation of high-affinity LFA-1 in focal zones of adherent cells. Defective integrin affinity regulation in the genetic absence of impairs leukocyte adhesion and extravasation in inflamed cremaster muscle venules in comparison with control animals. In a mouse infection model, PMN infiltration into the gastric mucosa is dramatically reduced in mice, resulting in an attenuated gastric inflammation. Thus, Coro1A represents an important novel player in integrin biology, with key functions in PMN trafficking during innate immunity.
[Mh] Termos MeSH primário: 4-Butirolactona/análogos & derivados
Antígenos CD18/metabolismo
Movimento Celular
Imunidade Inata
Neutrófilos/citologia
Neutrófilos/metabolismo
[Mh] Termos MeSH secundário: 4-Butirolactona/metabolismo
Actinas/metabolismo
Animais
Sinalização do Cálcio
Adesão Celular
Gastrite/imunologia
Gastrite/microbiologia
Gastrite/patologia
Helicobacter pylori/fisiologia
Antígeno-1 Associado à Função Linfocitária/metabolismo
Antígeno de Macrófago 1/metabolismo
Camundongos Endogâmicos C57BL
Receptores Acoplados a Proteínas-G/metabolismo
Reologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Actins); 0 (CD18 Antigens); 0 (Lymphocyte Function-Associated Antigen-1); 0 (Macrophage-1 Antigen); 0 (Receptors, G-Protein-Coupled); 0 (coronin); OL659KIY4X (4-Butyrolactone)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170616
[St] Status:MEDLINE
[do] DOI:10.1182/blood-2016-11-749622


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[PMID]:28580688
[Au] Autor:Panezai J; Bergdahl E; Sundqvist KG
[Ad] Endereço:Division of Periodontology, Department of Dental Medicine, Karolinska Institute at Karolinska University Hospital, Stockholm, Sweden.
[Ti] Título:T-cell regulation through a basic suppressive mechanism targeting low-density lipoprotein receptor-related protein 1.
[So] Source:Immunology;152(2):308-327, 2017 Oct.
[Is] ISSN:1365-2567
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Cell adhesion is generally considered to depend on positive regulation through ligation of integrins and cytokine receptors. However, here we show that T-cell adhesion, and notably also T-cell receptor (TCR) -induced activation, are subject to constant suppression through shedding of low-density lipoprotein receptor-related protein 1 (LRP1). The broad-spectrum metalloprotease inhibitor GM6001 abrogated shedding, so inducing prominent cell surface expression of LRP1 while enhancing TCR-induced activation and adhesion to ß and ß integrin ligands, hence arresting the cells. Integrin ligands also inhibited shedding but the effect was less potent than that of GM6001. Unlike GM6001, integrin ligands also induced cell surface expression of full-length thrombospondin-1 (TSP170) and TSP130, which associated with LRP1, and TSP110, which did not associate with LRP1. Cell surface expression of LRP1 and TSP130 were induced exclusively in adhering cells, expression of TSP110 preferentially in non-adhering cells and expression of TSP170 correlated with T-cell motility. The pro-adhesive chemokine CXCL12 also inhibited LRP1 shedding and induced surface expression of TSP170 and TSP130 while inhibiting TSP110. Exogenous TSP-1 and ligation of CD28 inhibited shedding although less effectively than GM6001, and the inhibition through CD28 was independent of TSP-1. Small interfering RNA silencing experiments confirmed involvement of LRP1 and TSP-1 in integrin-dependent adhesion and TCR-induced activation. Hence, the poor LRP1 expression in T cells depends on shedding. Integrin ligands and CXCL12 antagonize shedding through a TSP-1-dependent pathway and ligation of CD28 antagonizes shedding independent of TSP-1. The disappearance of LRP1 from the cell surface may provide basic immunosuppression at the T-cell level.
[Mh] Termos MeSH primário: Adesão Celular
Movimento Celular
Tolerância Imunológica
Proteína-1 Relacionada a Receptor de Lipoproteína de Baixa Densidade/metabolismo
Ativação Linfocitária
Linfócitos T/metabolismo
[Mh] Termos MeSH secundário: Antígenos CD18/imunologia
Antígenos CD18/metabolismo
Antígenos CD28/imunologia
Antígenos CD28/metabolismo
Adesão Celular/efeitos dos fármacos
Linhagem Celular Tumoral
Movimento Celular/efeitos dos fármacos
Quimiocina CXCL12/farmacologia
Dipeptídeos/farmacologia
Seres Humanos
Tolerância Imunológica/efeitos dos fármacos
Integrina beta1/imunologia
Integrina beta1/metabolismo
Ligantes
Proteína-1 Relacionada a Receptor de Lipoproteína de Baixa Densidade/genética
Proteína-1 Relacionada a Receptor de Lipoproteína de Baixa Densidade/imunologia
Ativação Linfocitária/efeitos dos fármacos
Inibidores de Metaloproteinases de Matriz/farmacologia
Fragmentos de Peptídeos/imunologia
Fragmentos de Peptídeos/metabolismo
Interferência de RNA
Receptores de Antígenos de Linfócitos T/imunologia
Receptores de Antígenos de Linfócitos T/metabolismo
Transdução de Sinais
Linfócitos T/efeitos dos fármacos
Linfócitos T/imunologia
Trombospondina 1/genética
Trombospondina 1/imunologia
Trombospondina 1/metabolismo
Fatores de Tempo
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CD18 Antigens); 0 (CD28 Antigens); 0 (Chemokine CXCL12); 0 (Dipeptides); 0 (Integrin beta1); 0 (LRP1 protein, human); 0 (Ligands); 0 (Low Density Lipoprotein Receptor-Related Protein-1); 0 (Matrix Metalloproteinase Inhibitors); 0 (N-(2(R)-2-(hydroxamidocarbonylmethyl)-4-methylpentanoyl)-L-tryptophan methylamide); 0 (Peptide Fragments); 0 (Receptors, Antigen, T-Cell); 0 (Thrombospondin 1); 0 (thrombospondin-1, human)
[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:170606
[St] Status:MEDLINE
[do] DOI:10.1111/imm.12770


  7 / 3581 MEDLINE  
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[PMID]:28515093
[Au] Autor:Panicker SR; Mehta-D'souza P; Zhang N; Klopocki AG; Shao B; McEver RP
[Ad] Endereço:Cardiovascular Biology Research Program, Oklahoma Medical Research Foundation, Oklahoma City, OK; and.
[Ti] Título:Circulating soluble P-selectin must dimerize to promote inflammation and coagulation in mice.
[So] Source:Blood;130(2):181-191, 2017 Jul 13.
[Is] ISSN:1528-0020
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Leukocyte adhesion to P-selectin on activated platelets and endothelial cells induces shedding of the P-selectin ectodomain into the circulation. Plasma soluble P-selectin (sP-selectin) is elevated threefold to fourfold in patients with cardiovascular disease. Circulating sP-selectin is thought to trigger signaling in leukocytes that directly contributes to inflammation and thrombosis. However, sP-selectin likely circulates as a monomer, and in vitro studies suggest that sP-selectin must dimerize to induce signaling in leukocytes. To address this discrepancy, we expressed the entire ectodomain of mouse P-selectin as a monomer (sP-selectin) or as a disulfide-linked dimer fused to the Fc portion of mouse immunoglobulin G (sP-selectin-Fc). Dimeric sP-selectin-Fc, but not monomeric sP-selectin, triggered integrin-dependent adhesion of mouse leukocytes in vitro. Antibody-induced oligomerization of sP-selectin or sP-selectin-Fc was required to trigger formation of neutrophil extracellular traps. Injecting sP-selectin-Fc, but not sP-selectin, into mice augmented integrin-dependent adhesion of neutrophils in venules, generated tissue factor-bearing microparticles, shortened plasma-clotting times, and increased thrombus frequency in the inferior vena cava. Furthermore, transgenic mice that overexpressed monomeric sP-selectin did not exhibit increased inflammation or thrombosis. We conclude that elevated plasma sP-selectin is a consequence rather than a cause of cardiovascular disease.
[Mh] Termos MeSH primário: Armadilhas Extracelulares/imunologia
Neutrófilos/imunologia
Selectina-P/sangue
Trombose/genética
Veia Cava Inferior/imunologia
[Mh] Termos MeSH secundário: Animais
Anticorpos/farmacologia
Antígenos CD18/genética
Antígenos CD18/imunologia
Células CHO
Adesão Celular/efeitos dos fármacos
Cricetulus
Dissulfetos/química
Armadilhas Extracelulares/efeitos dos fármacos
Regulação da Expressão Gênica
Fragmentos Fc das Imunoglobulinas/sangue
Fragmentos Fc das Imunoglobulinas/genética
Inflamação
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Transgênicos
Neutrófilos/efeitos dos fármacos
Neutrófilos/patologia
Selectina-P/química
Selectina-P/genética
Selectina-P/imunologia
Domínios Proteicos
Multimerização Proteica
Proteínas Recombinantes de Fusão/sangue
Proteínas Recombinantes de Fusão/genética
Proteínas Recombinantes de Fusão/imunologia
Transdução de Sinais
Tromboplastina/genética
Tromboplastina/imunologia
Trombose/imunologia
Trombose/patologia
Veia Cava Inferior/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies); 0 (CD18 Antigens); 0 (Disulfides); 0 (Immunoglobulin Fc Fragments); 0 (P-Selectin); 0 (Recombinant Fusion Proteins); 9035-58-9 (Thromboplastin)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170519
[St] Status:MEDLINE
[do] DOI:10.1182/blood-2017-02-770479


  8 / 3581 MEDLINE  
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[PMID]:28500072
[Au] Autor:Aziz MH; Cui K; Das M; Brown KE; Ardell CL; Febbraio M; Pluskota E; Han J; Wu H; Ballantyne CM; Smith JD; Cathcart MK; Yakubenko VP
[Ad] Endereço:Department of Biomedical Sciences, Quillen College of Medicine, East Tennessee State University, Johnson City, TN 37604.
[Ti] Título:The Upregulation of Integrin α ß (CD11d/CD18) on Inflammatory Macrophages Promotes Macrophage Retention in Vascular Lesions and Development of Atherosclerosis.
[So] Source:J Immunol;198(12):4855-4867, 2017 Jun 15.
[Is] ISSN:1550-6606
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Macrophage accumulation is a critical step during development of chronic inflammation, initiating progression of many devastating diseases. Leukocyte-specific integrin α ß (CD11d/CD18) is dramatically upregulated on macrophages at inflammatory sites. Previously we found that CD11d overexpression on cell surfaces inhibits in vitro cell migration due to excessive adhesion. In this study, we have investigated how inflammation-mediated CD11d upregulation contributes to macrophage retention at inflammatory sites during atherogenesis. Atherosclerosis was evaluated in CD11d /ApoE mice after 16 wk on a Western diet. CD11d deficiency led to a marked reduction in lipid deposition in aortas and isolated macrophages. Macrophage numbers in aortic sinuses of CD11d mice were reduced without affecting their apoptosis and proliferation. Adoptive transfer of fluorescently labeled wild-type and CD11d monocytes into ApoE mice demonstrated similar recruitment from circulation, but reduced accumulation of CD11d macrophages within the aortas. Furthermore, CD11d expression was significantly upregulated on macrophages in atherosclerotic lesions and M1 macrophages in vitro. Interestingly, expression of the related ligand-sharing integrin CD11b was not altered. This difference defines their distinct roles in the regulation of macrophage migration. CD11d-deficient M1 macrophages demonstrated improved migration in a three-dimensional fibrin matrix and during resolution of peritoneal inflammation, whereas migration of CD11b M1 macrophages was not affected. These results prove the contribution of high densities of CD11d to macrophage arrest during atherogenesis. Because high expression of CD11d was detected in several inflammation-dependent diseases, we suggest that CD11d/CD18 upregulation on proinflammatory macrophages may represent a common mechanism for macrophage retention at inflammatory sites, thereby promoting chronic inflammation and disease development.
[Mh] Termos MeSH primário: Aterosclerose/imunologia
Vasos Sanguíneos/patologia
Antígenos CD11/genética
Antígenos CD18/genética
Cadeias alfa de Integrinas/genética
Macrófagos/imunologia
[Mh] Termos MeSH secundário: Animais
Aorta/imunologia
Aorta/patologia
Apolipoproteínas E/deficiência
Aterosclerose/etiologia
Aterosclerose/patologia
Vasos Sanguíneos/imunologia
Antígenos CD11/imunologia
Antígenos CD18/imunologia
Dieta Ocidental
Seres Humanos
Inflamação/patologia
Mediadores da Inflamação/metabolismo
Cadeias alfa de Integrinas/deficiência
Cadeias alfa de Integrinas/imunologia
Macrófagos/metabolismo
Macrófagos/patologia
Camundongos
Camundongos Knockout
Peritonite/imunologia
Peritonite/patologia
Ativação Transcricional
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Apolipoproteins E); 0 (CD11 Antigens); 0 (CD18 Antigens); 0 (ITGAD protein, human); 0 (Inflammation Mediators); 0 (Integrin alpha Chains); 0 (integrin alphaD, mouse)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170514
[St] Status:MEDLINE
[do] DOI:10.4049/jimmunol.1602175


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[PMID]:28320610
[Au] Autor:Inoue K; Patterson EK; Capretta A; Lawendy AR; Fraser DD; Cepinskas G
[Ad] Endereço:Centre for Critical Illness Research, Lawson Health Research Institute, London, Ontario, Canada.
[Ti] Título:Carbon Monoxide-Releasing Molecule-401 Suppresses Polymorphonuclear Leukocyte Migratory Potential by Modulating F-Actin Dynamics.
[So] Source:Am J Pathol;187(5):1121-1133, 2017 May.
[Is] ISSN:1525-2191
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Carbon monoxide-releasing molecules (CORMs) suppress inflammation by reducing polymorphonuclear leukocyte (PMN) recruitment to the affected organs. We investigated modulation of PMN-endothelial cell adhesive interactions by water-soluble CORM-401 using an experimental model of endotoxemia in vitro. Human umbilical vein endothelial cells (HUVEC) grown on laminar-flow perfusion channels were stimulated with 1 µg/mL lipopolysaccharide for 6 hours and perfused with 100 µmol/L CORM-401 (or inactive compound iCORM-401)-pretreated PMN for 5 minutes in the presence of 1.0 dyn/cm shear stress. HUVEC: PMN co-cultures were perfused for additional 15 minutes with PMN-free medium containing CORM-401/inactive CORM-401. The experiments were videorecorded (phase-contrast microscopy), and PMN adhesion/migration were assessed off-line. In parallel, CORM-401-dependent modulation of PMN chemotaxis, F-actin expression/distribution, and actin-regulating pathways [eg, p21-activated protein kinases (PAK1/2) and extracellular signal-regulated kinase (ERK)/C-Jun N-terminal kinase (JNK) mitogen-activated protein kinases (MAPK)] were assessed in response to N-formyl-methionyl-leucyl-phenylalanine (fMLP) stimulation. Pretreating PMN with CORM-401 did not suppress PMN adhesion to HUVEC, but significantly reduced PMN transendothelial migration (P < 0.0001) and fMLP-induced PMN chemotaxis (ie, migration directionality and velocity). These changes were associated with CORM-401-dependent suppression of F-actin levels/cellular distribution and fMLP-induced phosphorylation of PAK1/2 and ERK/JNK MAPK (P < 0.05). CORM-401 had no effect on p38 MAPK activation. In summary, this study demonstrates, for the first time, CORM-401-dependent suppression of neutrophil migratory potential associated with modulation of PAK1/2 and ERK/JNK MAPK signaling and F-actin dynamics.
[Mh] Termos MeSH primário: Monóxido de Carbono/metabolismo
Movimento Celular/fisiologia
Neutrófilos/fisiologia
[Mh] Termos MeSH secundário: Actinas/metabolismo
Antígenos CD18/metabolismo
Adesão Celular/fisiologia
Células Cultivadas
Células Endoteliais da Veia Umbilical Humana
Seres Humanos
MAP Quinase Quinase 4/metabolismo
Sistema de Sinalização das MAP Quinases/fisiologia
Quinases de Proteína Quinase Ativadas por Mitógeno/metabolismo
Fosforilação/fisiologia
Molécula-1 de Adesão Celular Endotelial de Plaquetas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Actins); 0 (CD18 Antigens); 0 (Platelet Endothelial Cell Adhesion Molecule-1); 7U1EE4V452 (Carbon Monoxide); EC 2.7.12.2 (MAP Kinase Kinase 4); EC 2.7.12.2 (Mitogen-Activated Protein Kinase Kinases)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170322
[St] Status:MEDLINE


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[PMID]:28306722
[Au] Autor:Toscani AM; Sampayo RG; Barabas FM; Fuentes F; Simian M; Coluccio Leskow F
[Ad] Endereço:Universidad de Buenos Aires, Facultad de Ciencias Exactas y Naturales, Departamento de Química Biológica, Buenos Aires, Argentina.
[Ti] Título:Distinct ErbB2 receptor populations differentially interact with beta1 integrin in breast cancer cell models.
[So] Source:PLoS One;12(3):e0174230, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:ErbB2 is a member of the ErbB family of tyrosine kinase receptors that plays a major role in breast cancer progression. Located at the plasma membrane, ErbB2 forms large clusters in spite of the presence of growth factors. Beta1 integrin, membrane receptor of extracellular matrix proteins, regulates adhesion, migration and invasiveness of breast cancer cells. Physical interaction between beta1 integrin and ErbB2 has been suggested although published data are contradictory. The aim of the present work was to study the interaction between ErbB2 and beta1 integrin in different scenarios of expression and activation. We determined that beta1 integrin and ErbB2 colocalization is dependent on the expression level of both receptors exclusively in adherent cells. In suspension cells, lack of focal adhesions leave integrins free to diffuse on the plasma membrane and interact with ErbB2 even at low expression levels of both receptors. In adherent cells, high expression of beta1 integrin leaves unbound receptors outside focal complexes that diffuse within the plasma membrane and interact with ErbB2 membrane domains. Superresolution imaging showed the existence of two distinct populations of ErbB2: a major population located in large clusters and a minor population outside these structures. Upon ErbB2 overexpression, receptors outside large clusters can freely diffuse at the membrane and interact with integrins. These results reveal how expression levels of beta1 integrin and ErbB2 determine their frequency of colocalization and show that extracellular matrix proteins shape membrane clusters distribution, regulating ErbB2 and beta1 integrin activity in breast cancer cells.
[Mh] Termos MeSH primário: Neoplasias da Mama/patologia
Antígenos CD18/metabolismo
Receptor ErbB-2/metabolismo
[Mh] Termos MeSH secundário: Linhagem Celular Tumoral
Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CD18 Antigens); EC 2.7.10.1 (ERBB2 protein, human); EC 2.7.10.1 (Receptor, ErbB-2)
[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:170318
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0174230



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