The Experts below are selected from a list of 19233 Experts worldwide ranked by ideXlab platform
Anthony Cerami - One of the best experts on this subject based on the ideXlab platform.
-
enhancing and suppressing effects of recombinant murine Macrophage Inflammatory Proteins on colony formation in vitro by bone marrow myeloid progenitor cells
Blood, 1990Co-Authors: Hal E. Broxmeyer, Scott Cooper, Barbara Sherry, Patricia Tekampolson, Byoung S Kwon, Anthony CeramiAbstract:Purified recombinant (r) Macrophage Inflammatory Proteins (MIPs) 1 alpha, 1 beta, and 2 were assessed for effects on murine (mu) and human (hu) marrow colony-forming unit-granulocyte-Macrophage (CFU-GM) and burst-forming unit-erythroid (BFU-E) colonies. Recombinant MIP-1 alpha, -1 beta, and -2 enhanced muCFU-GM colonies above that stimulated with 10 to 100 U natural mu Macrophage-colony-stimulating factor (M-CSF) or rmuGM-CSF, with enhancement seen on huCFU-GM colony formation stimulated with suboptimal rhuM-CSF or rhuGM-CSF; effects were neutralized by respective MIP-specific antibodies. Macrophage Inflammatory Proteins had no effects on mu or huBFU-E colonies stimulated with erythropoietin (Epo). However, natural MIP-1 and rMIP-1 alpha, but not rMIP-1 beta or -2, suppressed muCFU-GM stimulated with pokeweed mitogen spleen-conditioned medium (PWMSCM), huCFU-GM stimulated with optimal rhuGM-CSF plus rhu interleukin-3 (IL-3), muBFU-E and multipotential progenitors (CFU-GEMM) stimulated with Epo plus PWMSCM, and huBFU-E and CFU-GEMM stimulated with Epo plus rhuIL-3 or rhuGM-CSF. The suppressive effects of natural MIP-1 and rMIP-1 alpha were also apparent on a population of BFU-E, CFU-GEMM, and CFU-GM present in cell-sorted fractions of human bone marrow (CD34 HLA-DR+) highly enriched for progenitors with cloning efficiencies of 42% to 75%. These results, along with our previous studies, suggest that MIP-1 alpha, -1 beta, and -2 may have direct myelopoietic enhancing activity for mature progenitors, while MIP-1 alpha may have direct suppressing activity for more immature progenitors.
-
Enhancing and suppressing effects of recombinant murine Macrophage Inflammatory Proteins on colony formation in vitro by bone marrow myeloid progenitor cells
Blood, 1990Co-Authors: Hal E. Broxmeyer, Scott Cooper, Barbara Sherry, Byoung S Kwon, Li Lu, Kwi-ok Oh, Patricia Tekamp-olson, Anthony CeramiAbstract:YELOID BLOOD CELL production is a dynamic M process regulated by cell-derived cytokines.' In addition to the hematopoietic colony-stimulating factors (CSFs), which directly stimulate the proliferation of myeloid progenitors,',' other cytokines enhance or suppress CSFstimulated progenitor cell proliferation.' Such cytokines include the heparin-binding murine Macrophage Inflammatory Proteins (MIP- 1, MIP-2),3'6 which enhance proliferation of granulocyte Macrophage (GM)-CSF-and Macrophage (M)-CSF-stimulated granulocyte-Macrophage progenitors (CFU-GM).7 Macrophage Inflammatory Proteins-1 and MIP-2 do not effect erythroid (burst-forming unit-erythroid [BFU-E]) progenitor cell proliferation stimulated by erythropoietin (E~o).~ Natural murine MIP-1 is composed of two distinct peptides, MIP-la and MIP-l@.3-6 Since MIP-la and - I@ had not been biochemically sepa
Hal E. Broxmeyer - One of the best experts on this subject based on the ideXlab platform.
-
enhancing and suppressing effects of recombinant murine Macrophage Inflammatory Proteins on colony formation in vitro by bone marrow myeloid progenitor cells
Blood, 1990Co-Authors: Hal E. Broxmeyer, Scott Cooper, Barbara Sherry, Patricia Tekampolson, Byoung S Kwon, Anthony CeramiAbstract:Purified recombinant (r) Macrophage Inflammatory Proteins (MIPs) 1 alpha, 1 beta, and 2 were assessed for effects on murine (mu) and human (hu) marrow colony-forming unit-granulocyte-Macrophage (CFU-GM) and burst-forming unit-erythroid (BFU-E) colonies. Recombinant MIP-1 alpha, -1 beta, and -2 enhanced muCFU-GM colonies above that stimulated with 10 to 100 U natural mu Macrophage-colony-stimulating factor (M-CSF) or rmuGM-CSF, with enhancement seen on huCFU-GM colony formation stimulated with suboptimal rhuM-CSF or rhuGM-CSF; effects were neutralized by respective MIP-specific antibodies. Macrophage Inflammatory Proteins had no effects on mu or huBFU-E colonies stimulated with erythropoietin (Epo). However, natural MIP-1 and rMIP-1 alpha, but not rMIP-1 beta or -2, suppressed muCFU-GM stimulated with pokeweed mitogen spleen-conditioned medium (PWMSCM), huCFU-GM stimulated with optimal rhuGM-CSF plus rhu interleukin-3 (IL-3), muBFU-E and multipotential progenitors (CFU-GEMM) stimulated with Epo plus PWMSCM, and huBFU-E and CFU-GEMM stimulated with Epo plus rhuIL-3 or rhuGM-CSF. The suppressive effects of natural MIP-1 and rMIP-1 alpha were also apparent on a population of BFU-E, CFU-GEMM, and CFU-GM present in cell-sorted fractions of human bone marrow (CD34 HLA-DR+) highly enriched for progenitors with cloning efficiencies of 42% to 75%. These results, along with our previous studies, suggest that MIP-1 alpha, -1 beta, and -2 may have direct myelopoietic enhancing activity for mature progenitors, while MIP-1 alpha may have direct suppressing activity for more immature progenitors.
-
Enhancing and suppressing effects of recombinant murine Macrophage Inflammatory Proteins on colony formation in vitro by bone marrow myeloid progenitor cells
Blood, 1990Co-Authors: Hal E. Broxmeyer, Scott Cooper, Barbara Sherry, Byoung S Kwon, Li Lu, Kwi-ok Oh, Patricia Tekamp-olson, Anthony CeramiAbstract:YELOID BLOOD CELL production is a dynamic M process regulated by cell-derived cytokines.' In addition to the hematopoietic colony-stimulating factors (CSFs), which directly stimulate the proliferation of myeloid progenitors,',' other cytokines enhance or suppress CSFstimulated progenitor cell proliferation.' Such cytokines include the heparin-binding murine Macrophage Inflammatory Proteins (MIP- 1, MIP-2),3'6 which enhance proliferation of granulocyte Macrophage (GM)-CSF-and Macrophage (M)-CSF-stimulated granulocyte-Macrophage progenitors (CFU-GM).7 Macrophage Inflammatory Proteins-1 and MIP-2 do not effect erythroid (burst-forming unit-erythroid [BFU-E]) progenitor cell proliferation stimulated by erythropoietin (E~o).~ Natural murine MIP-1 is composed of two distinct peptides, MIP-la and MIP-l@.3-6 Since MIP-la and - I@ had not been biochemically sepa
Rui Appelberg - One of the best experts on this subject based on the ideXlab platform.
-
interferon gamma ifn γ and Macrophage Inflammatory Proteins mip 1 and 2 are involved in the regulation of the t cell dependent chronic peritoneal neutrophilia of mice infected with mycobacteria
Clinical and Experimental Immunology, 2008Co-Authors: Rui AppelbergAbstract:In mycobacterial infections of mice there is a chronic, immune-mediated mobilization of neutrophils to the infectious site. In this study we evaluated the role played by cytokines in the chronic peritoneal neutrophilia which occurs in mice intraperitoneally infected with Mycobacterium bovis BCG or M. avium. Antibodies to IFN-gamma and to MIP-1 and -2 were effective in reducing peritoneal neutrophilia when given during the infection. Whereas the former antibody was only effective when given early, the latter two were effective when administered late in infection, suggesting the MIPs were direct mediators of neutrophil recruitment. Recombinant IFN-gamma given intraperitoneally induced the accumulation of neutrophils and primed the peritoneal cells for an enhanced recruitment of neutrophils. Our data show that chronic neutrophilia during mycobacterial infection is regulated by different cytokines acting at different stages and levels of neutrophil recruitment.
-
Macrophage Inflammatory Proteins mip 1 and mip 2 are involved in t cell mediated neutrophil recruitment
Journal of Leukocyte Biology, 1992Co-Authors: Rui AppelbergAbstract:Mice intraperitoneally (i.p.) infected with Mycobacterium bovis bacille Calmette-Guerin (BCG) respond to an i.p. challenge with mycobacterial antigen with an acute and extensive accumulation of neutrophils. This influx was not mimicked by the inoculation of recombinant interferon-gamma (IFN-gamma) or tumor necrosis factor alpha (TNF-alpha). The antigen-induced recruitment of neutrophils was not affected by coinoculation of anti-IFN-gamma antibodies, was enhanced by anti-TNF-alpha antisera, and was significantly reduced by antisera against Macrophage Inflammatory Proteins MIP-1 and MIP-2. The latter two sera had no additive effects. We hypothesize that mycobacteria-specific T cells are triggered by antigen to secrete MIP-1 and MIP-2, which directly mediate, at least partly, the influx of neutrophils that takes place in this model.
Kevin E. Driscoll - One of the best experts on this subject based on the ideXlab platform.
-
Macrophage Inflammatory Proteins: Biology and Role in Pulmonary Inflammation
Experimental Lung Research, 1994Co-Authors: Kevin E. DriscollAbstract:Macrophage Inflammatory Proteins 1α and β (MIP-1α and β and Macrophage Inflammatory protein 2 (MIP-2) are ∼6-8 kd, heparin binding Proteins that exhibit a number of Inflammatory and immunoregulatorcoy activities. The MIP Proteins are members of a superfamily of cytokines called chemokines, many of which have been shown to possess chemotactic activity for Inflammatory and immune effector cells. While MIPs were originally identified as secretory products of endotoxin-stimulated mouse Macrophages, these chemokines are produced by a variety of cell types including neutrophils, fibroblasts, and epithelial cells. In addition, Proteins with a high degree of structural and functional homology to murine MIP-1α and β and MIP-2 have been identified in other species including humans. MlP-1α and β are chemotactic for monocytes and lymphocytes and MIP-2 is a potent chemotactic factor for neutrophils. MIPs likely also play a role in regulating hematopoiesis and stimulating production of other Inflammatory mediators such...
-
Macrophage Inflammatory Proteins: Biology and Role in Pulmonary Inflammation
Experimental lung research, 1994Co-Authors: Kevin E. DriscollAbstract:Macrophage Inflammatory Proteins 1 alpha and beta (MIP-1 alpha and beta) and Macrophage Inflammatory protein 2 (MIP-2) are approximately 6-8 kd, heparin binding Proteins that exhibit a number of Inflammatory and immunoregulatory activities. The MIP Proteins are members of a superfamily of cytokines called chemokines, many of which have been shown to possess chemotactic activity for Inflammatory and immune effector cells. While MIPs were originally identified as secretory products of endotoxin-stimulated mouse Macrophages, these chemokines are produced by a variety of cell types including neutrophils, fibroblasts, and epithelial cells. In addition, Proteins with a high degree of structural and functional homology to murine MIP-1 alpha and beta and MIP-2 have been identified in other species including humans. MIP-1 alpha and beta are chemotactic for monocytes and lymphocytes and MIP-2 is a potent chemotactic factor for neutrophils. MIPs likely also play a role in regulating hematopoiesis and stimulating production of other Inflammatory mediators such as IL-1, TNF alpha, and histamine. Studies using animal models of lung injury and inflammation have implicated MIPs as important mediators of lung defense. Increased MIP expression has been observed in models of bacterial sepsis, silicosis, and oxidant-induced lung injury. Studies in humans indicate MIP-1 alpha contributes to the Inflammatory cell response associated with sarcoidosis and idiopathic pulmonary fibrosis. Given the bioactivities of MIP-1 alpha and beta and MIP-2 and the recent studies demonstrating their association with lung inflammation, it is likely these chemokines play a significant role in respiratory tract defenses and may contribute to the pathogenesis of Inflammatory lung disease.
-
Macrophage Inflammatory Proteins 1 and 2 expression by rat alveolar Macrophages fibroblasts and epithelial cells and in rat lung after mineral dust exposure
American Journal of Respiratory Cell and Molecular Biology, 1993Co-Authors: Kevin E. Driscoll, Diana G Hassenbein, Janet M Carter, James Poynter, Thomas N Asquith, Raymond A Grant, Julie Whitten, Michael P Purdon, Ray TakigikuAbstract:Macrophage Inflammatory Proteins 1α and 2 (MIP-1α, MIP-2) are members of a growing family of cytokines thought to play a role in host defense. MIP-1α and MIP-2 were previously identified in the mouse and shown to stimulate Inflammatory cell recruitment. To better understand the potential role of MIP-1α and MIP-2 in lung defense, we investigated the ability of rat lung cells to express mRNA for and/or secrete MIP-1α and MIP-2 Proteins in vitro and characterized expression of these cytokines in rat lung after in vivo exposure to silica (SiO2) or titanium dioxide (TiO2). In response to lipopolysaccharide, rat alveolar Macrophages expressed increased levels of MIP-1α and MIP-2 mRNA and secreted Proteins (identified by N-terminal sequencing) homologous to mouse MIP-1α and MIP-2. Rat alveolar Macrophage MIP-1α and MIP-2 mRNA expression was also increased by tumor necrosis factor-α (TNF) and adherence to plastic. Studies with a rat fibroblast and epithelial cell line demonstrated that MIP-2, but not MIP-1α, expr...
Byoung S Kwon - One of the best experts on this subject based on the ideXlab platform.
-
enhancing and suppressing effects of recombinant murine Macrophage Inflammatory Proteins on colony formation in vitro by bone marrow myeloid progenitor cells
Blood, 1990Co-Authors: Hal E. Broxmeyer, Scott Cooper, Barbara Sherry, Patricia Tekampolson, Byoung S Kwon, Anthony CeramiAbstract:Purified recombinant (r) Macrophage Inflammatory Proteins (MIPs) 1 alpha, 1 beta, and 2 were assessed for effects on murine (mu) and human (hu) marrow colony-forming unit-granulocyte-Macrophage (CFU-GM) and burst-forming unit-erythroid (BFU-E) colonies. Recombinant MIP-1 alpha, -1 beta, and -2 enhanced muCFU-GM colonies above that stimulated with 10 to 100 U natural mu Macrophage-colony-stimulating factor (M-CSF) or rmuGM-CSF, with enhancement seen on huCFU-GM colony formation stimulated with suboptimal rhuM-CSF or rhuGM-CSF; effects were neutralized by respective MIP-specific antibodies. Macrophage Inflammatory Proteins had no effects on mu or huBFU-E colonies stimulated with erythropoietin (Epo). However, natural MIP-1 and rMIP-1 alpha, but not rMIP-1 beta or -2, suppressed muCFU-GM stimulated with pokeweed mitogen spleen-conditioned medium (PWMSCM), huCFU-GM stimulated with optimal rhuGM-CSF plus rhu interleukin-3 (IL-3), muBFU-E and multipotential progenitors (CFU-GEMM) stimulated with Epo plus PWMSCM, and huBFU-E and CFU-GEMM stimulated with Epo plus rhuIL-3 or rhuGM-CSF. The suppressive effects of natural MIP-1 and rMIP-1 alpha were also apparent on a population of BFU-E, CFU-GEMM, and CFU-GM present in cell-sorted fractions of human bone marrow (CD34 HLA-DR+) highly enriched for progenitors with cloning efficiencies of 42% to 75%. These results, along with our previous studies, suggest that MIP-1 alpha, -1 beta, and -2 may have direct myelopoietic enhancing activity for mature progenitors, while MIP-1 alpha may have direct suppressing activity for more immature progenitors.
-
Enhancing and suppressing effects of recombinant murine Macrophage Inflammatory Proteins on colony formation in vitro by bone marrow myeloid progenitor cells
Blood, 1990Co-Authors: Hal E. Broxmeyer, Scott Cooper, Barbara Sherry, Byoung S Kwon, Li Lu, Kwi-ok Oh, Patricia Tekamp-olson, Anthony CeramiAbstract:YELOID BLOOD CELL production is a dynamic M process regulated by cell-derived cytokines.' In addition to the hematopoietic colony-stimulating factors (CSFs), which directly stimulate the proliferation of myeloid progenitors,',' other cytokines enhance or suppress CSFstimulated progenitor cell proliferation.' Such cytokines include the heparin-binding murine Macrophage Inflammatory Proteins (MIP- 1, MIP-2),3'6 which enhance proliferation of granulocyte Macrophage (GM)-CSF-and Macrophage (M)-CSF-stimulated granulocyte-Macrophage progenitors (CFU-GM).7 Macrophage Inflammatory Proteins-1 and MIP-2 do not effect erythroid (burst-forming unit-erythroid [BFU-E]) progenitor cell proliferation stimulated by erythropoietin (E~o).~ Natural murine MIP-1 is composed of two distinct peptides, MIP-la and MIP-l@.3-6 Since MIP-la and - I@ had not been biochemically sepa
