Relevant bibliographies by topics / CD11b/CD18

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Academic literature on the topic 'CD11b/CD18'

Author: Grafiati
Published: 4 June 2021
Last updated: 17 February 2022

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Journal articles on the topic "CD11b/CD18"

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Hickstein, DD, E. Grunvald, G. Shumaker, DM Baker, AL Back, LJ Embree, E. Yee, and KA Gollahon. "Transfected leukocyte integrin CD11b/CD18 (Mac-1) mediates phorbol ester-activated, homotypic cell:cell adherence in the K562 cell line." Blood 82, no. 8 (October 15, 1993): 2537–45. http://dx.doi.org/10.1182/blood.v82.8.2537.2537.

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Abstract The CD11b/CD18 leukocyte integrin molecule mediates diverse neutrophil adherence-related functions, including cell:cell and cell:extracellular matrix attachments. To study the individual role of this leukocyte integrin in cell adherence in hematopoietic cells, we expressed the CD11b/CD18 complex on the surface of K562 cells, a cell line derived from an individual with chronic myelogenous leukemia in blast crisis. We used an amphotrophic retroviral vector designated LCD18SN, harboring the complete coding sequence for the CD18 subunit, to transfer the CD18 cDNA into K562 cells and select stable cell lines. The CD11b subunit in the expression plasmid pREP4 was transfected into these K562/CD18 cells by electroporation and stable cell clones were selected. These K562 cells possessed RNA and intracellular protein for each subunit, and they expressed the CD11b/CD18 heterodimer on the cell surface. When CD11b/CD18 expressing K562 cells were stimulated with phorbol myristate acetate (50 ng/mL) for 24 to 48 hours, these K562 cells formed dense cell:cell aggregates. This homotypic aggregation required both activation of the CD11b/CD18 complex and the induction of the counter- receptor for CD11b/CD18 on the conjugate cell. This cell line will (1) enable the structure-function relationships between cell activation and homotypic adherence to be assessed, (2) provide the opportunity to identify accessory molecules required for activation of the CD11b/CD18 complex, and (3) facilitate the identification of novel ligands for the CD11b/CD18 complex.
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Hickstein, DD, E. Grunvald, G. Shumaker, DM Baker, AL Back, LJ Embree, E. Yee, and KA Gollahon. "Transfected leukocyte integrin CD11b/CD18 (Mac-1) mediates phorbol ester-activated, homotypic cell:cell adherence in the K562 cell line." Blood 82, no. 8 (October 15, 1993): 2537–45. http://dx.doi.org/10.1182/blood.v82.8.2537.bloodjournal8282537.

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The CD11b/CD18 leukocyte integrin molecule mediates diverse neutrophil adherence-related functions, including cell:cell and cell:extracellular matrix attachments. To study the individual role of this leukocyte integrin in cell adherence in hematopoietic cells, we expressed the CD11b/CD18 complex on the surface of K562 cells, a cell line derived from an individual with chronic myelogenous leukemia in blast crisis. We used an amphotrophic retroviral vector designated LCD18SN, harboring the complete coding sequence for the CD18 subunit, to transfer the CD18 cDNA into K562 cells and select stable cell lines. The CD11b subunit in the expression plasmid pREP4 was transfected into these K562/CD18 cells by electroporation and stable cell clones were selected. These K562 cells possessed RNA and intracellular protein for each subunit, and they expressed the CD11b/CD18 heterodimer on the cell surface. When CD11b/CD18 expressing K562 cells were stimulated with phorbol myristate acetate (50 ng/mL) for 24 to 48 hours, these K562 cells formed dense cell:cell aggregates. This homotypic aggregation required both activation of the CD11b/CD18 complex and the induction of the counter- receptor for CD11b/CD18 on the conjugate cell. This cell line will (1) enable the structure-function relationships between cell activation and homotypic adherence to be assessed, (2) provide the opportunity to identify accessory molecules required for activation of the CD11b/CD18 complex, and (3) facilitate the identification of novel ligands for the CD11b/CD18 complex.
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Thylén, P., E. Fernvik, J. Lundahl, J. Hed, and S. H. Jacobson. "Modulation of CD11b/CD18 on Monocytes and Granulocytes following Hemodialysis Membrane Interaction in vitro." International Journal of Artificial Organs 19, no. 3 (March 1996): 156–63. http://dx.doi.org/10.1177/039139889601900304.

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We studied the generation of CD11b/CD18 mobilizing factors in serum after incubation with dialysis membrane fragments of different chemical composition. We also evaluated the relative importance of the alternative and classical pathways of the complement system in the generation of such factors. Monocytes and granulocytes from healthy blood donors were incubated in normal human serum (NHS) and in NHS that had been preincubated with Cuprophan (CU) membrane (NHS-CU), Hemophan (HE) (NHS-HE) or polysulfone (PS) (NHS-PS). NHS-CU caused the highest up-regulation of the CD11b/CD18 receptor on monocytes and granulocytes. The rank in capacity to mobilize CD11b/CD18 on granulocytes was CU>HE>PS (p<0.001), CU>HE (p<0.05) and HE>PS (p<0.001). The rank in capacity to mobilize CD11b/CD18 on monocytes was CU>HE>PS (p<0.001), CU>HE (p<0.05) and HE>PS (p<0.01). NHS-PS induced a lower up-regulation of CD11b/CD18 compared to NHS which indicates that serum factors with the ability to mobilize the CD11b/CD18 receptor on monocytes and granulocytes are deposited on or adsorbed by PS. In order to study the relative contribution of the alternative and classical pathways of the complement system in the generation of CD11b/CD18 mobilizing factors in serum, three different serum preparations (1. both pathways intact. 2. only the alternative intact and 3. only the classical pathway intact) were used. The CU membrane activated the classical pathway to a larger extent than the PS membrane (p<0.01). When only the alternative pathway was intact no difference in the generation of CD11b/CD18 mobilizing factors between the CU and PS membranes was observed. These studies show that CD11b/CD18 mobilizing serum factors are generated after incubation with CU membranes and that such factors are probably adsorbed by PS. The classical pathway of complement activation seems to contribute to the generation of CD11b/CD18 mobilizing factors in serum.
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Simms, H. H., and R. D′Amico. "Hypoxemia regulates effect of lipopolysaccharide on polymorphonuclear leukocyte CD11b/CD18 expression." Journal of Applied Physiology 76, no. 4 (April 1, 1994): 1657–63. http://dx.doi.org/10.1152/jappl.1994.76.4.1657.

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Expression of the receptor CD11b/CD18 on the polymorphonuclear leukocyte (PMN) surface is important for several aspects of PMN function during endotoxemia. The mechanisms underlying regulation of CD11b/CD18 expression during hypoxemia and endotoxemia, however, are less clear. We investigated the effects of exposure of whole blood PMNs to lipopolysaccharide (LPS) during hypoxemia. During hypoxemia (10–30% O2 saturation), LPS reduced CD11b/CD18 expression. Both kinetic assays and experiments with microfilament stabilizers (phalloidin, cytochalasin B) demonstrated that this was most likely due to receptor shedding. Incubation of whole blood PMNs with an anti-CD14 monoclonal antibody (MEM18) largely prevented the LPS-induced reduction of CD11b/CD18 expression. Decreased CD11b/CD18 expression reduced PMN functional capability, as the binding of its ligand (erythrocytes opsonized with the 3rd component of complement Cbi) and intracellular H2O2 production were reduced. After exposure to LPS, N-formyl-methionyl-leucyl-phenylalanine could rapidly induce new CD11b/CD18 receptors to the cell surface, and this was not inhibited by actinomycin D or cycloheximide. After reoxygenation (> 90% O2 saturation), CD11b/CD18 expression was restored, and this was abrogated by exposure to cytochalasin B. Lipid A was able to reproduce the effects of LPS during hypoxemia and hypoxemia-reoxygenation but required a 10-fold greater concentration to do so. These results demonstrate that during hypoxemia an important pathophysiological property of LPS is to reduce CD11b/CD18 expression. This results in diminished PMN functional capability, which would contribute to the pathogenicity of LPS during acute infectious states.
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Lo, S. K., P. A. Detmers, S. M. Levin, and S. D. Wright. "Transient adhesion of neutrophils to endothelium." Journal of Experimental Medicine 169, no. 5 (May 1, 1989): 1779–93. http://dx.doi.org/10.1084/jem.169.5.1779.

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Fluorescently labeled polymorphonuclear leukocytes (PMN) were used to measure adhesion to human umbilical vein endothelial cells (EC) cultured in vitro. Stimulation of PMN with phorbol dibutyrate (PDB), TNF, or C5a caused an increase in adhesion followed by a return to prestimulation levels of adhesion of longer times of incubation. Maximal adhesion of PMN to EC occurred rapidly in response to C5a (5 min) and more slowly with TNF or PDB (15 min). PMN stimulated to adhere with C5a detached from EC by 15 min. PMN from CD11/CD18-deficient patients and PMN incubated with anti-CD18 mAbs failed to bind to EC despite maximal stimulation. Anti-CD11a/CD18 and anti-CD11b/CD18 each partially inhibited adhesion, and a combination of these two reagents completely blocked adhesion. The adhesion we measured was therefore completely dependent on CD11/CD18, and CD11a/CD18 and CD11b/CD18 each contributed to adhesion. Stimuli that enhanced adhesion of PMN to EC also enhanced expression of CD11b/CD18 on the cell surface, but the time course of expression correlated poorly with changes in adhesivity. To determine if changes in the expression of CD11b/CD18 are necessary for the changes in adhesivity, we used enucleate cytoplasts that did not increase expression of CD11b/CD18. Cytoplasts showed a normal rise and fall in adhesivity in response to PDB. We conclude that the transient adhesion of stimulated PMN to naive EC is regulated by changes in the nature of existing CD11/CD18 molecules on the PMN surface. Changes in expression of CD11b/CD18 may contribute to enhancement of adhesivity, but a definite role for this phenomenon has yet to be established.
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Hajishengallis, George, Min Wang, Evlambia Harokopakis, Martha Triantafilou, and Kathy Triantafilou. "Porphyromonas gingivalis Fimbriae Proactively Modulate β2 Integrin Adhesive Activity and Promote Binding to and Internalization by Macrophages." Infection and Immunity 74, no. 10 (October 2006): 5658–66. http://dx.doi.org/10.1128/iai.00784-06.

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ABSTRACT In monocytes, the fimbriae of the oral pathogen Porphyromonas gingivalis activate cross talk signaling from Toll-like receptor 2 (TLR2) to the β2 integrin CD11b/CD18, leading to the induction of the high-affinity state of the latter receptor. CD14 plays an important role in this “inside-out” proadhesive pathway by binding fimbriae and facilitating the activation of TLR2 and phosphatidylinositol 3-kinase signaling. In its high-affinity state, CD11b/CD18 mediates monocyte adhesion to endothelial cells and transmigration to sites of infection. We have now shown that P. gingivalis fimbriae function as both an activator and a ligand of CD11b/CD18; thus, fimbriae proactively promote their own binding to monocytes. Indeed, treatments that interfered with fimbria-induced activation of CD11b/CD18 (i.e., blockade of CD14, TLR2, or phosphatidylinositol 3-kinase signaling) also suppressed the cell binding activity of fimbriae, which was largely inducible and CD11b/CD18 dependent. Development of a recombinant inside-out signaling system in Chinese hamster ovary cells confirmed the ability of fimbriae to activate CD14/TLR2 signaling and induce their own CD11b/CD18-dependent binding. Induction of this proadhesive pathway by P. gingivalis fimbriae appeared to take place in lipid rafts. Indeed, methyl-β-cyclodextrin, a cholesterol-sequestering agent that disrupts lipid raft organization, was found to inhibit the fimbria-induced assembly of CD14/TLR2 signaling complexes and the activation of the high-affinity state of CD11b/CD18. Experiments using macrophages from mice deficient in various pattern recognition receptors indicated that the receptors involved in the inside-out proadhesive pathway (CD14, TLR2, and CD11b/CD18) are important for mediating P. gingivalis internalization within macrophages. It therefore appears that P. gingivalis proactively modulates β2 integrin adhesive activity for intracellular uptake.
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Forsyth, Christopher B., and Herbert L. Mathews. "Lymphocyte Adhesion to Candida albicans." Infection and Immunity 70, no. 2 (February 2002): 517–27. http://dx.doi.org/10.1128/iai.70.2.517-527.2002.

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ABSTRACT Adherence of lymphocytes to the fungus is the first step in the direct lymphocyte-mediated antifungal effect against Candida albicans. In this study we identified macrophage-1 antigen (Mac-1) (CD11b/CD18, αM/β2) as the lymphocyte surface structure responsible for the adhesion of activated lymphocytes to the hyphal form of the fungus. Antibodies specific for epitopes of the α-subunit (CD11b) and the β2-subunit (CD18) of Mac-1 were shown to completely eliminate lymphocyte adhesion to C. albicans hyphae. Lymphocyte adhesion to C. albicans was also inhibited significantly by known ligands of Mac-1, including the extracellular matrix proteins laminin and fibrinogen, as well as engineered peptides containing arginine-glycine-aspartic acid sequences and the disintegrin echistatin. N-Acetyl-d-glucosamine and β-glucan, which inhibit Mac-1-mediated adhesion to the yeast, blocked lymphocyte adhesion to hyphae. NIH 3T3 fibroblast transfectants expressing human CD11b/CD18 bound to C. albicans, and their binding was inhibited by antibodies specific for CD11b/CD18. Finally, antibodies specific for CD11b/CD18 effectively inhibited the capacity of activated lymphocytes to have an antifungal effect against hyphae. Our results clearly identify Mac-1 (CD11b/CD18) as the lymphocyte surface structure that mediates activated lymphocyte adhesion to C. albicans and the resultant antifungal effect of the lymphocytes.
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Detmers, P. A., S. K. Lo, E. Olsen-Egbert, A. Walz, M. Baggiolini, and Z. A. Cohn. "Neutrophil-activating protein 1/interleukin 8 stimulates the binding activity of the leukocyte adhesion receptor CD11b/CD18 on human neutrophils." Journal of Experimental Medicine 171, no. 4 (April 1, 1990): 1155–62. http://dx.doi.org/10.1084/jem.171.4.1155.

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The cytokine NAP-1/IL-8 is produced by a variety of different cells in response to inflammatory stimuli and elicits several biological responses from PMN. Experiments presented here demonstrate that PMN exposed to NAP-1/IL-8 expressed increased amounts of CD11b/CD18, as well as CD11c/CD18 and CR1, on their cell surface, while expression of Fc gamma RIII and HLA-A,B,C remained essentially unchanged. Increased CD11b/CD18 and CD11c/CD18 appears to correspond with the release of specific granules by NAP-1/IL-8. NAP-1/IL-8 was also a potent stimulator of several of the binding activities of CD11b/CD18. Ligation of EC3bi by CD11b/CD18 was rapidly enhanced by NAP-1/IL-8, but phagocytosis of the ligated particles was not induced by the agonist. In addition, enhanced binding of EC3bi was observed in the absence of an increase in receptor expression as shown with PMN cytoplasts. NAP-1/IL-8 promoted additional adhesive interactions between CD11b/CD18 and the biosynthetic precursor of LPS, lipid IVa, fibrinogen, and endothelial cells, suggesting that NAP-1/IL-8 may promote leukocyte adhesion in vivo that could lead to recruitment of PMN to sites of tissue inflammation.
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Li, R., J. Xie, C. Kantor, V. Koistinen, D. C. Altieri, P. Nortamo, and C. G. Gahmberg. "A peptide derived from the intercellular adhesion molecule-2 regulates the avidity of the leukocyte integrins CD11b/CD18 and CD11c/CD18." Journal of Cell Biology 129, no. 4 (May 15, 1995): 1143–53. http://dx.doi.org/10.1083/jcb.129.4.1143.

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beta 2 integrin (CD11a,b,c/CD18)-mediated cell adhesion is required for many leukocyte functions. Under normal circumstances, the integrins are nonadhesive, and become adhesive for their cell surface ligands, the intercellular adhesion molecules (ICAMs), or soluble ligands such as fibrinogen and iC3b, when leukocytes are activated. Recently, we defined a peptide derived from ICAM-2, which specifically binds to purified CD11a/CD18. Furthermore, this peptide strongly induces T cell aggregation mainly mediated by CD11a/CD18-ICAM-1 interaction, and natural killer cell cytotoxicity. In the present study, we show that the same ICAM-2 peptide also avidly binds to purified CD11b/CD18, but not to CD11c/CD18. This binding can be blocked by the CD11b antibody OKM10. The peptide strongly stimulates CD11b/CD18-ICAM-1-mediated cell aggregations of the monocytic cell lines THP-1 and U937. The aggregations are energy and divalent cation-dependent. The ICAM-2 peptide also induces CD11b/CD18 and CD11c/CD18-mediated binding of THP-1 cells to fibrinogen and iC3b coated on plastic. These findings indicate that in addition to induction of CD11a/CD18-mediated cell adhesion, the ICAM-2 peptide may also serve as a "trigger" for high avidity ligand binding of other beta 2 integrins.
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Zen, Ke, Markus Utech, Yuan Liu, Illena Soto, Asma Nusrat, and Charles A. Parkos. "Association of BAP31 with CD11b/CD18." Journal of Biological Chemistry 279, no. 43 (August 4, 2004): 44924–30. http://dx.doi.org/10.1074/jbc.m402115200.

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Dissertations / Theses on the topic "CD11b/CD18"

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Weitzman, Jonathan B. "Characterisation of the 5' regions of the leukocyte integrin CD11b/CD18 genes." Thesis, University of Oxford, 1991. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.292365.

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Gesenberg, Jan [Verfasser]. "CD11b/CD18 Knock-Out reduziert die Anfälligkeit für ventrikuläre Tachykardie und die Infarktgröße / Jan Gesenberg." Köln : Deutsche Zentralbibliothek für Medizin, 2018. http://d-nb.info/1153425432/34.

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BLOUIN, ERIC. "Etude des mecanismes de regulation de l'activation des integrines 2 cd11b/cd18 des polynucleaires neutrophiles." Paris 6, 2001. http://www.theses.fr/2001PA066271.

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Les neutrophiles sont les premiers leucocytes a acceder au site inflammatoire. C'est l'adherence, via les integrines 2, qui leur permet d'assurer leurs fonctions. Les mecanismes d'activation de ces integrines sont mal connus. Cette etude analyse donc le role de l'oxydoreduction dans l'activation des integrines 2 des neutrophiles. Nous montrons que les oxydants activent les integrines 2, se traduisant par l'adherence des neutrophiles et l'apparition de la conformation active des integrines. Cette activation implique les tyrosine kinases et la formation de ponts disulfure. Ensuite, le dpi (diphenyleneiodonium) et les piegeurs de radicaux libres inhibent l'adherence et l'apparition de la conformation active des integrines 2, induite apres la stimulation des neutrophiles par le tnf-. L'oxydase impliquee dans le mecanisme n'est pas la nadph-oxydase, puisque les memes resultats sont retrouves avec les neutrophiles de patients cgd (granulomatose septique chronique). Le pp2, inhibiteur specifique des kinases src, bloque l'adherence des neutrophiles et l'apparition de la conformation active des integrines 2 induite par le tnf-. Parmi les kinases src, seules les kinases fgr sont activees par le tnf- et ceci de facon dependante de l'oxydoreduction, car inhibee par le dpi et les piegeurs de radicaux libres. De la meme facon, le sb203580, inhibiteur specifique des map kinases p38, bloque l'adherence des neutrophiles et l'apparition de la conformation active des integrines 2 induite par le tnf-. Cette activation est regulee de facon dependante de l'oxydoreduction, car elle est bloquee par le dpi et les piegeurs de radicaux libres. Nous avons donc mis en evidence un nouveau mecanisme de regulation de l'activation des integrines 2, impliquant la stimulation d'une oxydase, differente de la nadph-oxydase, qui modifie le potentiel d'oxydoreduction du neutrophile, entrainant l'oxydation de groupements thiols et l'activation des kinases p38 et fgr.
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Rieu, Philippe. "Etude de l'integrine cd11b/cd18 : analyse moleculaire et role au cours de l'adherence des neutrophiles." Paris 7, 1997. http://www.theses.fr/1997PA077273.

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Pour defendre l'organisme face a une agression tissulaire, les polynucleaires neutrophiles adherent a l'endothelium, le traversent et migrent dans le tissu conjonctif jusqu'au site inflammatoire ou ils liberent leurs produits de secretions, phagocytent les particules cibles, puis meurent par apoptose. Ce sont les integrines leucocytaires (cd11a, b, c, d/cd18) qui assurent les fonctions adhesives des neutrophiles. Parmi ces integrines, nous avons montre avec une souris invalide en cd11b, que le recepteur cd11b/cd18 est l'adhesine majeure des neutrophiles qui intervient dans l'adherence de ces cellules aux surfaces proteiques, dans la phagocytose et l'explosion respiratoire, et de facon inattendue, dans l'apoptose de ces cellules. Nous n'avons pas retrouve de recepteur des autres familles d'integrines en dehors d'une faible quantite de l'heterodimere cd49f/cd29. Par ailleurs, nous avons montre que la leucosialine (cd43), une mucine anti-adhesive fortement exprimee par les neutrophiles, subissait un clivage proteolytique au cours de l'activation cellulaire, ce qui pourrait faciliter la liaison de cd11b/cd18 avec ses ligands. Pour comprendre cette derniere interaction, nous avons caracterise le domaine d'adherence de l'integrine cd11b/cd18. Il s'agit d'un domaine extracellulaire d'environ 200 acides amines (domaine a ou i) qui adopte une structure de type alpha/beta et qui contient un site de fixation pour cation divalent a sa surface appele midas, metal ion-dependent adhesion site. C'est au niveau de ce site que se lient l'antagoniste nif (neutrophil inhibitory factor) et l'opsonine ic3b, deux ligands de cd11b/cd18. Le changement de conformation qui survient lors de l'activation des integrines pourrait modifier la coordination du metal du domaine a et faciliter ainsi l'interaction de midas avec ses ligands. Si la reaction inflammatoire est vitale pour l'organisme, une reponse excessive peut aggraver le traumatisme initial. La connaissance du role et du mode d'action des integrines leucocytaires devrait aider a la conception de nouveaux anti-inflammatoires.
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Santos, Andressa Cristina Antunes. "Efeito da desnutrição proteica sobre aspectos da mobilização, migração e sinalização celular. Papel da glutamina na modulação desses processos." Universidade de São Paulo, 2016. http://www.teses.usp.br/teses/disponiveis/9/9136/tde-28042016-104055/.

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A desnutrição é uma condição nutricional que pode afetar muitos aspectos da resposta imunológica, como alterações na migração celular, na fagocitose, na resposta bactericida, mudanças na produção de radicais livres e espécies de nitrogênio e na produção de citocinas pró-inflamatórias. Logo, indivíduos desnutridos apresentam maior susceptibilidade a infecções. Visto que a glutamina é um aminoácido de extrema importância para a funcionalidade de diversas células do sistema imune e que as mesmas apresentam aumento da utilização desse aminoácido durante processos infecciosos, investigou-se, neste trabalho, quais os efeitos da glutamina sobre alguns aspectos da mobilização, migração e sinalização celular em um modelo experimental de desnutrição proteica. Para tanto, utilizou-se camundongos da linhagem BALB/c machos, os quais foram divididos em dois grupos, Controle e Desnutrido, que passaram a receber dietas isocalóricas contendo 12% (normoproteica) e 2% de caseína (hipoproteica), respectivamente, durante 5 semanas. Para as avaliações in vivo, animais de ambos os grupos receberam por via endovenosa 100µL de solução contendo 1,25µg de LPS e após 1 hora 0,75mg/Kg de L-glutamina (GLUT). Após o período de desnutrição ou de indução ao processo inflamatório, os animais foram eutanasiados e as amostras biológicas coletas. Foram avaliados nos animais estimulados in vivo hemograma, mielograma, as citocinas IL-10 e TNF-α circulantes e a expressão de CD11b/CD18 nos granulócitos do sangue periférico. Foi avaliado, in vitro, a capacidade migratória, a expressão de CD11b/CD18 de polimorfonucleados da medula óssea e do sangue periférico, bem como a síntese de citocinas IL-1α, IL-6, IL-10, IL-12 e TNF-α e a expressão de NF-κB e IκBα em células cultivadas em meio com 0; 0,6; 2 e 10 mM de GLUT. Os animais desnutridos apresentaram anemia, leucopenia, hipoplasia medular e diminuição na concentração sérica de proteínas, albumina e pré-albumina. A GLUT, in vitro, apresentou capacidade de reduzir a produção de IL-1α e IL-6, bem como a ativação da via do NF-κB. No modelo in vivo a GLUT, em animais estimulados com LPS, alterou a cinética de migração neutrofílica e reduziu a expressão de CD18, bem como diminuiu os níveis de TNFα circulantes.
Malnutrition is a nutritional condition that can affect many aspects of immune responses, affecting cell migration, phagocytosis, bactericidal response and changing free radicals production as nitrogen species and production of proinflammatory cytokines. Therefore, malnourished individuals are more susceptible to infections. Once glutamine is an amino acid of extreme importance to the functionality of various immune cells and those cells exhibit increased use of this amino acid during infectious processes. In this work was investigated, the effects of glutamine in some aspects of mobilization, cell migration and signaling in an experimental model of protein malnutrition. For this purpose, we used BALB/c mice, which received isocaloric diets, normoproteic or hypoproteic, containing respectively, 12% (Control group) and 2% (Malnourished group) of protein for a period of 5 weeks. The animals in both groups, for in vivo evaluations, received intravenous 100 µl of a solution containing 1.25µg of LPS and after 1 hour 0.75mg/kg of L-glutamine (GLUT). After the malnutrition period or the inflammatory process induction, the animals were euthanized and biological samples were collected. Were evaluated blood count, bone marrow, the cytokines IL-10 and TNF-α circulating and expression of CD11b/CD18 in granulocytes from peripheral blood of animals stimulated in vivo. In vitro were evaluated the migratory capacity, the expression of CD11b/CD18 polymorphonuclear bone marrow and peripheral blood, as well as the cytokines synthesis IL-1α, IL-6, IL-10, IL-12 and TNF-α and the expression of NF-κB and IκBα in cultured cells in media with 0; 0.6; 2 and 10 mM GLUT. Malnourished animals presented anemia, leukopenia, marrow hypoplasia and lower serum proteins, albumin and prealbumin. The GLUT in vitro has the capacity to reduce IL-1α and IL-6 as well as the activation of the NF-κB. In in vivo model, the GLUT altered neutrophil migration kinetics and reduced the expression of CD18, as well as decreased levels of circulating TNF-α in animals stimulated with LPS.
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Berti, Verena Dorothea [Verfasser], and Karlheinz [Akademischer Betreuer] Peter. "Die molekulare MR-Bildgebung des Monozytenintegrins Mac-1 (CD11b/CD18) optimiert nicht die Detektion von Monozyten in atherosklerotischen Plaques von ApoE−/−-Mäusen." Freiburg : Universität, 2011. http://d-nb.info/1123460205/34.

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Thieblemont, Nathalie. "Role des recepteurs cr1 (cd35) et cr3 (cd11b/cd18) dans la penetration et la replication du virus de l'immunodeficience humaine (vih) dans les monocytes/macrophages." Paris 6, 1993. http://www.theses.fr/1993PA066651.

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Nous avons demontre que les glycoproteines recombinantes gp160 et gp120 du vih1 activent le complement humain en l'absence d'anticorps. Les glycoproteines gp160 et gp120 induisent un clivage de c3 dans du serum humain normal. Ce clivage est lie a une activation de la voie classique du complement qui peut etre augmente en presence d'anticorps anti-vih1. Cette activation du complement permet aussi une opsonisation des particules virales puisque l'infection de cellules cibles par le vih1 ou le vih2 peut etre facilitee par une pre-incubation du virus dans du serum humain normal. La pre-incubation des cellules avec des anticorps anti-cr1 ou anti-cr3 inhibe l'infection des cellules des lignees pro-monocytaires, comme des monocytes, indiquant que la penetration du virus s'effectue par l'intermediaire des recepteurs cr1 (cd35) et cr3 (cd11b/cd18). L'infection mediee par les molecules cr1 et cr3 se produit independamment des molecules cd4. Nos etudes montre par ailleurs que la stimulation des recepteurs du complement induit simultanement dans les cellules infectees, une translocation du nf-kappab, une augmentation de la replication virale et une deregulation de la synthese des cytokines. Cette deregulation pourrait etre une consequence d'une anomalie de maturation des cellules. D'autre part, nous avons identifie l'apparition chez les patients infectes par le vih d'une sous-population de monocytes plus matures dont l'emergence dependrait de la deregulation de l'equilibre des cytokines lymphocytaires
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8

Faulhaber, Fabrízia Rennó Sodero. "Expressão de marcadores de superfície de neutrófilos em recém nascidos ictéricos antes e após a fototerapia." reponame:Biblioteca Digital de Teses e Dissertações da UFRGS, 2017. http://hdl.handle.net/10183/179819.

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A icterícia por hiperbilirrubinemia indireta afeta mais de 60% dos recém-nascidos a termo. O tratamento, quando necessário, é realizado através da fototerapia. Não existem estudos na literatura avaliando os efeitos da fototerapia na função dos neutrófilos de recém-nascidos. O melhor entendimento da função dos neutrófilos nos recém-nascidos antes e após a fototerapia seria importante para avaliar as possíveis repercussões na expressão dos neutrófilos desencadeadas pelo tratamento fototerápico. O objetivo deste estudo foi avaliar e comparar a função dos neutrófilos, através da mensuração pela citometria de fluxo da expressão dos principais marcadores de superfície em recémnascidos ictéricos, antes e após 24 horas de fototerapia. Metodologia: Foram incluídos recém-nascidos com idade gestacional ≥ 35 semanas e peso de nascimento ≥ 2000g, que possuiam critérios da Academia Americana de Pediatria para tratamento fototerápico. Os critérios de exclusão foram: mal-formações congênitas, síndromes com alterações cromossômicas, erro inato do metabolismo, infecções do grupo STORCH, asfixia neonatal, sepse ou suspeita de sepse, exsanguineotransfusão, transfusão de hemocomponentes e uso de imunoglobulina. Foi realizada a avaliação de expressão da intensidade média de fluorescência (IMF) de CD10, CD11b, CD11c, CD15, CD16, CD18, CD62L, CD64 e CD66, antes do início e após 24 horas do início da fototerapia. Foram utilizados o teste T de Student para análise dos dados. Resultados: Foram incluídos 25 recém-nascidos no estudo, com idade mediana de 53 (27.5-75.5) horas de vida e bilirrubina média de 13.6±2.85 mg/dL. Não houve diferença estatística na expressão de CD11b, CD15, CD18, CD62L, CD64 e percentual de neutrófilos antes e após 24 horas de fototerapia. Ocorreu aumento da expressão de CD10 8 (p=0.038) e CD16 (p=0.017) e redução da expressão de CD11c (p=0.023) e CD66acde (p=0.004) após 24 horas de fototerapia. Conclusão: Os recém-nascidos submetidos ao tratamento fototerápico apresentaram aumento da expressão de CD10 e de CD16 e diminuição da expressão de CD11c e de CD66acde após 24 horas de exposição, que pode estar relacionado a um efeito antiinflamatório da fototerapia nos recém-nascidos expostos a este tratamento.
Jaundice due to indirect hyperbilirubinemia affects more than 60% of term neonates. The treatment when necessary is carried out using phototherapy. There are no studies in the literature evaluating the effect of phototherapy on the function of neonates' neutrophils. A better understanding of the function of neutrophils in neonates before and after phototherapy would be important in order to assess potential effects on the expression of neutrofils triggered by the phototherapy treatment. The aim of this study was to assess and compare the function of neutrophils by measuring the expression of the main surface markers in icteric neonates, using flow cytometry, before and after 24 hours of phototherapy. Methodology: Neonates at a gestational age ≥ 35 weeks and at a birth weight ≥ 2000g who met the criteria of the American Academy of Pediatrics for phototherapy were included. The exclusion criteria were: congenital malformations, syndromes with chromosomal alterations, inborn errors of metabolism, infections of the STORCH group, neonatal asphyxia, sepsis or suspicion of sepsis, exchange transfusion, transfusion of blood components, and use of immunoglobulin. The evaluation of the MFI expression of CD10, CD11b, CD11c, CD15, CD16, CD18, CD62L, CD64 and CD66 was performed before and 24 hours after the initiation of phototherapy. The chi-square and Student T tests were used for data analysis. Results: Twenty-five neonates were included in the study at the mean age of 53 (27.5- 75.5) hours of life and with a mean bilirubin level of 13.6±2.85 mg/dL. There was no statistical difference in the expression of CD11b, CD15, CD18, CD62L, CD64 and percentage of neutrophils before and after 24 hours of phototherapy. There was an increase in the expression of CD10 (p=0.038) and CD16 (p=0.017) and a reduction in 10 the expression of CD11c (p=0.023) and CD66acde (p=0.004) after 24 hours of phototherapy. Conclusion: The newborns submitted to phototherapy had increased expression of CD10 and CD16 and decreased expression of CD11c and CD66acde after 24 hours of exposure, which may be related to an anti-inflammatory effect of phototherapy on the neonates exposed to this treatment.
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Schallner, Nils. "Evaluation des diagnostischen und therapeutischen Potentials des aktivationsspezifischen, gegen das Leukozytenintegrin Mac-1 (CD11b/CD18, alphaM/beta2) gerichteten, monoklonalen Einzelketten-Antikörper MAN-1 funktionelle Charakterisierung und ex-vivo Evaluation an Sepsis-Patienten /." [S.l. : s.n.], 2006. http://nbn-resolving.de/urn:nbn:de:bsz:25-opus-49341.

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Welcker, Silvia. "Selektion konformationsspezifischer Aptamere sowohl gegen das aktivierte Leukozytenintegrin Mac-1 (alphaM beta 2, CD11b, CD18) als auch gegen den nicht aktivierten und aktivierten Integrin-Rezeptor alphaV Beta 3 (Vitronektin-Rezeptor, CD51,CD61)." [S.l. : s.n.], 2007. http://nbn-resolving.de/urn:nbn:de:bsz:25-opus-44251.

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Book chapters on the topic "CD11b/CD18"

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Dana, Nava, Dehmani M. Fathallah, and M. Amin Arnaout. "Function of a Soluble Human β2 Integrin CD11b/CD18." In Structure, Function, and Regulation of Molecules Involved in Leukocyte Adhesion, 34–44. New York, NY: Springer New York, 1993. http://dx.doi.org/10.1007/978-1-4613-9266-8_4.

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Hughes, B. J., J. C. Hollers, and C. Wayne Smith. "Mac-1 (CD11b/CD18) and Adherence-Dependent Neutrophil Locomotion." In Structure, Function, and Regulation of Molecules Involved in Leukocyte Adhesion, 45–57. New York, NY: Springer New York, 1993. http://dx.doi.org/10.1007/978-1-4613-9266-8_5.

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Nielsen, Gitte Krogh, and Thomas Vorup-Jensen. "Detection of Soluble CR3 (CD11b/CD18) by Time-Resolved Immunofluorometry." In The Complement System, 355–64. Totowa, NJ: Humana Press, 2013. http://dx.doi.org/10.1007/978-1-62703-724-2_30.

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Shields, D. A., S. K. Andaz, C. A. Timothy-Antoine, J. H. Scurr, and J. B. Porter. "CD11b/CD18 as a Marker of Neutrophil Adhesion in Experimental Venous Hypertension." In Phlebology ’95, 220–21. London: Springer London, 1995. http://dx.doi.org/10.1007/978-1-4471-3095-6_99.

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Todd, Robert F., Paul J. Simpson, and Benedict R. Lucchesi. "Anti-Inflammatory Properties of Monoclonal Anti-Mo1 (CD11b/CD18) Antibodies In Vitro and In Vivo." In Leukocyte Adhesion Molecules, 125–37. New York, NY: Springer New York, 1990. http://dx.doi.org/10.1007/978-1-4612-3234-6_10.

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Jones, Douglas H., Frank C. Schmalstieg, Hal K. Hawkins, Bean L. Burr, Helen E. Rudloff, Sharon Krater, C. Wayne Smith, and Donald C. Anderson. "Characterization of a New Mobilizable Mac-1 (CD11b/CD18) Pool That Co-Localizes with Gelatinase in Human Neutrophils." In Leukocyte Adhesion Molecules, 106–24. New York, NY: Springer New York, 1990. http://dx.doi.org/10.1007/978-1-4612-3234-6_9.

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Buyon, Jill P., Mark R. Philips, Steven B. Abramson, Seth G. Slade, Gerald Weissmann, and Robert Winchester. "Mechanism Regulating Recruitment of CD11b/CD18 to the Cell Surface is Distinct From That Which Induces Adhesion in Homotypic Neutrophil Aggregation." In Leukocyte Adhesion Molecules, 72–83. New York, NY: Springer New York, 1990. http://dx.doi.org/10.1007/978-1-4612-3234-6_5.

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