Interaction of human monocytes, macrophages, and polymorphonuclear leukocytes with zymosan in vitro. Role of type 3 complement receptors and macrophage-derived complement.

Ezekowitz, R. A. B.; Sim, R. B.; MacPherson, G. Gordon; Gordon, Siamon

doi:10.1172/jci112249

Cited by 96 publications

(57 citation statements)

References 19 publications

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“…Again, it has been reported that resting N-PMN have as many CR-1 and CR-3 as do A-PMN (29,30). When triggered, expression of CR-1 increases to the same extent in both N-PMN and A-PMN, whereas expression of CR-3, which mainly mediates PMN responses to STZ (18), is lower in N-PMN (29,30). This may explain our results if up-regulation is critical for the PMN response, which is not in agreement with other results previously reported (31).…”

Section: Discussionmentioning

confidence: 98%

“…STZ is made up of zymosan particles, derived from yeast polysaccharide membranes, on which complement proteins are adsorbed. Interaction of opsonized zymosan with human PMN is prevalently mediated by receptors for C3 fragments (mainly CR-1 and CR-3) (18). Both fMLP and STZ stimulate LTB, release by human PMN.…”

Section: Discussionmentioning

confidence: 99%

“…In this work, we compared the LTB, release from adult and cord blood PMN in response to three different compounds: 1 ) the calcium ionophore A23187, a soluble stimulus pro-LEUKOTRIENE B, RELE :ASE BY NEONATAL PMN 61 ducing an increase in intracellular c a 2 + concentration; 2) a synthetic tripeptide, fMLP, with both structural and chemotactic characteristics similar to naturally occurring bacterial oligopeptides (16), which binds to specific plasma-membrane receptors on PMN (17); 3) zymosan particles opsonized with serum, which induce stimulatory signals in PMN as a result of prevalently binding to complement plasma-membrane receptors (18).…”

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confidence: 99%

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Impaired Leukotriene B4 Release by Neonatal Polymorphonuclear Leukocytes

et al. 1994

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Section: Discussionmentioning

confidence: 98%

Section: Discussionmentioning

confidence: 99%

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confidence: 99%

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Impaired Leukotriene B4 Release by Neonatal Polymorphonuclear Leukocytes

et al. 1994

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“…As the cells that had ingested yeasts appeared to be less adherent than the nonphagocytic nontransfected cells, the media were aspirated and the remaining cells were treated with trypsin and then pelleted with the cells in the aspirate . Thereafter the cell pellet was fixed in 2% glutaraldehyde in cacodylate buffer, pH 7 .4, and 500-nm sections were cut and stained with toluidine blue, which stains the yeasts and the nucleus blue and viewed by light microscopy, or uranyl acetate and lead citrate-stained sections were examined by transmission electron microscopy as described (29). Quantitation of phagocytosis was undertaken by examining fixed whole mount preparations of cells after they had been incubated for 20 min at 37°C with a ratio of 20:1 Candida albicans/cells .…”

Section: Methodsmentioning

confidence: 99%

Molecular characterization of the human macrophage mannose receptor: demonstration of multiple carbohydrate recognition-like domains and phagocytosis of yeasts in Cos-1 cells.

Ezekowitz

Sastry

Bailly

et al. 1990

The Journal of Experimental Medicine

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470

235

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SummaryThe macrophage mannose receptor is an integral membrane protein expressed on the surface of tissue macrophages . After ligation ofmannose-rich glycoconjugates or pathogens, the receptor mediates endorytosis and phagocytosis of the bound ligands by macrophages. The cDNAderived primary structure of the mannose receptor predicts a cysteine-rich NH2-terminal domain, followed by a fibronectin type II region. The remainder of the ectodomain is comprised of eight carbohydrate recognition-like domains, followed by a transmembrane region, and a cytoplasmic tail. Transfection of the mannose receptor cDNA into Cos-I cells is necessary for receptor-mediated endorytosis of mannose-rich glycoconjugate as well as phagocytosis of yeasts. Deletion of the cytoplasmic tail results in a mutant receptor that is able to bind but not ingest the ligated pathogens, suggesting that the signal for phagocytosis is contained in the cytoplasmic tail.P lasma clearance and cell uptake experiments (1) indicated the existence ofa receptor that bound glycoproteins bearing high mannose chains. Receptor activity was especially evident in the liver and spleens, although most other tissues were also positive. Subsequent experiments have established that the mannose receptor is expressed on the cell surface of tissue macrophages which reside in a wide anatomical distribution throughout most organs (2) . Although originally defined by its ability to mediate endorytosis ofmannosylated or fucosylated glycoproteins, the mannose receptor's predominant role appears to be in host defense. The receptor engages yeasts (3) and parasites (4) directly resulting in the engulfment of these particles and the release ofbiologically active secretory products like reactive oxygen intermediates (5), arachidonate metabolites (6), neutral proteinases (7), and monokines like IM and tumor necrosis factor (8) . As circulating monocytes do not express the mannose receptor on their cell surface (9), the functional role for the mannose receptor appears to be on tissue macrophages, which in addition to their localization in the reticular endothelial system line the alveolus and form a reticular network beneath epithelial surfaces in the skin, the gastrointestinal tract, kidney, and placenta (10). These sites are the portals of maximum antigen load and underscore the role for the mannose receptor in first line host defense.Recent experiments suggest that a circulating hepatocytederived serum mannose-binding protein is the functional serum equivalent of the tissue macrophage mannose receptor. The human mannose-binding protein (MBP)l is an acute-phase reactant (11) that binds certain viruses (12) and other mannose rich pathogens (13). Mannose-binding proteins after engaging organisms mediate attachment, uptake, and killing of opsonized bacteria by circulating phagocytes that do not express the mannose receptor (13). Underlying structural similarity between the MBP and the mannose receptor, thereby explaining their functional equivalence, was suggested by the discovery that h...

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“…STZ is made up of zymosan particles, derived from yeast polysaccharide membranes, on which complement proteins and Ig are adsorbed. Interaction of opsonized zymosan with human PMN is prevalently mediated by receptors for C3 fragments (25).…”

Section: Discussionmentioning

confidence: 99%

Impaired D-myo-Inositol 1,4,5-Triphosphate Generation from Cord Blood Polymorphonuclear Leukocytes

et al. 1995

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D-myo-Inositol 1,4,5-triphosphate (IP,) is a key second messenger in many cells, including macrophages, T and B cells, and neutrophils, in which it regulates free intracellular calcium ion levels. In human polymorphonuclear leukocytes the rise of intracellular [Ca2+] is the signal that activates a number of functions such as adherence, aggregation, chemotaxis, and degranulation, which are typically depressed in newborn infants. IP, generation can be stimulated by N-formyl-methionyl-leucylphenylalanine (fMLP) tripeptide, which mimics the naturally occurring bacterial oligopeptides. In this study both neonatal and adult polymorphonuclear leukocytes were stimulated by fMLP (1 X lop6 M) and the levels of IP, were assayed by a specific radiometric method. The time course of IP, generation was studied for up to 60 s in a total of 10 samples. The response appeared reduced in cord blood samples. To confirm this observation, we extended our study to a larger number of samples, quantitating [IP,] at the time peak of 10 s. As expected IP, generation was significantly (F test, p < 0.0001, n = 39) lower in newborns than in adults (means 2 SD = 0.64 + 0.25; 1.26 + 0.36, ng/106 cells, respectively). Besides soluble stimulus, neutrophils were treated with a particulate stimulus, namely serumtreated zymosan, which is also able to stimulate IP, synthesis from polymorphonuclear leukocytes. Serum-treated zymosan produced a prolonged elevation in the level of IP,, reaching a Human PMN are the first line of defense against nonviral infections. In response to an appropriate stimulus, they are able to diapedese through the endothelium and vessel wall in to the inflammatory focus killing and/or inactivating the invading organisms.Newborn infants show an increased susceptibility to serious and overwhelming bacterial and fungal infections. This leads to increased morbidity and mortality, in spite of advances in antibiotic therapy. Although abnormalities have been described in all compartments of the neonatal host defense system (I), FMLP is a synthetic tripeptide with structural and chemotactic characteristics similar to the naturally occurring bacterial oligopeptides (3). It is able to stimulate chemotaxis by binding to specific plasma membrane receptors of polymorphonuclear cells (4). The signal is transduced by the dissociation of the pertussis toxin-sensitive a-GTP complex from the heterotrimeric G protein and the consequent activation of a phospholipase C (5, 6). This, in turn, hydrolyzes PIP2 into two second messengers, namely DAG and IP,. The simultaneous generation of these two second messengers is responsible for activating a cascade of events that results in the cellular response. In particular, IP, is able to mobilize ca2+ from the intracellular

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Interaction of human monocytes, macrophages, and polymorphonuclear leukocytes with zymosan in vitro. Role of type 3 complement receptors and macrophage-derived complement.

Abstract: Macrophages take up zymosan in the absence of exogenous complement via receptors for iC3b (

Cited by 96 publications

References 19 publications

Impaired Leukotriene B4 Release by Neonatal Polymorphonuclear Leukocytes

Impaired Leukotriene B4 Release by Neonatal Polymorphonuclear Leukocytes

Molecular characterization of the human macrophage mannose receptor: demonstration of multiple carbohydrate recognition-like domains and phagocytosis of yeasts in Cos-1 cells.

Impaired D-myo-Inositol 1,4,5-Triphosphate Generation from Cord Blood Polymorphonuclear Leukocytes

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