Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P43026 (lipopolysaccharide)
62,215 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The present study was conducted to determine the manner in which monocytes increase mesangial matrices, particularly glycosaminoglycans (GAGs) which interact with various other matrix components such as collagens, laminin, fibronectin and lipoproteins. A supernatant of human peripheral blood monocyte cultures activated by lipopolysaccharide (LPS) contains stimulating factors for glycosaminoglycan synthesis in rat mesangial cells (MCs). The culture supernatant in this study was concentrated and fractionated by gel chromatography and the GAG-stimulatory factor was found to have a molecular weight of 10-17 kD. This factor was shown to be present in fractions different from that of IL-1. Gel and ion-exchange chromatography studies of GAGs synthesized by MCs indicated the elution patterns of GAGs in the presence and absence of the monocyte culture supernatant to be essentially the same. Local infiltration of monocytes into the glomerulus, often seen in various types of glomerular injury, may be an important factor in the accumulation of the mesangial matrix.
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PMID:Monocytes secrete factors regulating glycosaminoglycan synthesis in mesangial cells in vitro. 200 89

A new method to monitor macrophage attachment on protein-coated surfaces and spreading in response to activating agents is described. Murine macrophages were cultured on small gold electrodes coated with protein, and attachment and spreading were detected as electrical impedance changes. The rate of attachment of cells to fibronectin-coated electrodes was measured to be significantly greater than to other proteins tested. Activation agents used included interferon-gamma, lipopolysaccharide and heat killed Listeria monocytogenes. Addition of each agent to macrophages on electrodes resulted in characteristic patterns in the impedance time course with impedance changes as large as 40%.
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PMID:Measurement of macrophage adherence and spreading with weak electric fields. 210 21

Adherence is an important initial step in the transition of a circulating monocyte to a tissue macrophage. This differentiation is accompanied by an augmented capacity to generate growth factors. We hypothesized that adherence itself might be an important trigger for a sequence of gene activation culminating in cells with increased mRNA encoding profibrotic growth factors such as platelet-derived growth factor B subunit (PDGF[B]) and transforming growth factor-beta (TGF-beta). After in vitro adherence, human monocytes had a biphasic increase in PDGF(B) mRNA with peaks at 6 h and 13 d. No increase in TGF-beta mRNA was observed. The 6-h increase in PDGF(B) mRNA was adherence dependent, and in addition, was abrogated when the cytoskeletal integrity was compromised by cytochalasin D. The 6-h increase in PDGF(B) mRNA was unaltered by adherence in the presence of the monocyte stimulus lipopolysaccharide. Adherence to either fibronectin or collagen-coated plastic had little consistent effect on PDGF(B) mRNA accumulation. The increased PDGF(B) mRNA observed in adherent monocytes was accompanied by increases in mRNAs of the early growth response genes c-fos (maximal at 20 min), c-jun, and EGR2 (maximal at 6-24 h). The increase in c-jun and EGR2, but not c-fos, mRNA was also abrogated by cytochalasin D. These observations suggest that adherence results in increases of c-fos, c-jun, EGR2, and PDGF(B) mRNA. In addition, the increases in c-jun, EGR2, and PDGF(B) may depend on cytoskeletal rearrangement. Modulation of these events at the time of adherence offers a mechanism by which differential priming of the cells may be accomplished.
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PMID:Adherence-dependent increase in human monocyte PDGF(B) mRNA is associated with increases in c-fos, c-jun, and EGR2 mRNA. 212 46

Fibronectin (Fn), an extracellular matrix glycoprotein with binding sites for collagen, fibrin, heparin, and cell surfaces, is a nonimmune opsonin which up-regulates phagocytic function and facilitates adherence of human monocytes. We have developed a simple assay to study adherence of peripheral blood monocytes to Fn on a gelatin matrix. While cell adherence was enhanced by the presence of Fn in a dose-dependent manner, it was inhibited by peptides containing the Arg-Gly-Asp (RGD) cell attachment sequence or by coating the matrix with antibodies directed against Fn. Preincubation of monocytes for 30 min with Escherichia coli lipopolysaccharide (LPS) at doses of 1-50 micrograms/ml increased adherence to Fn-gelatin but not to gelatin alone, while longer preincubation (24 hr) resulted in similar changes at lower doses (0.01-1.0 micrograms/ml). Enhanced Fn adherence may be essential for monocyte localization to sites of inflammation.
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PMID:Lipopolysaccharide enhances monocyte adherence to matrix-bound fibronectin. 214 32

Recombinant tumor necrosis factor alpha (rTNF alpha) and beta (rTNF beta) did not trigger H2O2 release from PMN in suspension. However, when PMN were plated on polystyrene surfaces coated with serum, fibronectin, vitronectin, laminin, or human umbilical vein endothelial cells (HUVEC), rTNFs induced a massive, prolonged secretory response, similar to that elicited by phorbol myristate acetate (PMA) or bacteria. On serum-coated plates, the maximum sustained rate of H2O2 release in response to rTNF alpha was 2.6 +/- 0.2 nmol/min per 10(6) PMN, the same as that with PMA; release continued for 73 +/- 4 min. On laminin-coated surfaces or HUVEC, release of H2O2 in response to rTNFs was slower, but lasted approximately 3.5 h, reaching the same total (greater than 100 nmol/10(6) PMN). Not only was this response far longer and larger than for other soluble stimuli of the respiratory burst studied with PMN in suspension, but the concentration necessary to elicit a half-maximal response (EC50) for rTNF alpha was orders of magnitude lower (55 pM). Responses were similar with FMLP, but ranged from zero to small with recombinant IFN alpha, recombinant IFN beta, recombinant IFN gamma, platelet-derived growth factor, recombinant IL-1 beta, or bacterial lipopolysaccharide. Adherent monocytes did not secrete H2O2 in response to rTNFs. H2O2 secretion by adherent PMN was first detectable 15-90 min after addition of rTNFs or FMLP. This lag period was unaffected by prior exposure of PMN to rTNF alpha in suspension, by allowing PMN to adhere before adding rTNF alpha, or by incubating adherent PMN in medium conditioned by rTNF alpha-treated PMN. Cytochalasins abolished H2O2 secretion in response to rTNFs, but not FMLP, if added during, but not after, the lag period. Thus, H2O2 secretion from rTNF alpha-treated PMN appears to be a direct but delayed response that requires assembly of microfilaments during exposure to the cytokine. These results suggest that PMN adherent to intra- or extravascular surfaces may undergo a massive, prolonged respiratory burst at the command of macrophages and lymphocytes reacting to microbial products and antigens.
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PMID:Neutrophil activation on biological surfaces. Massive secretion of hydrogen peroxide in response to products of macrophages and lymphocytes. 244 80

We have localized several major extracellular matrix protein receptors in the specific granules of human polymorphonuclear (PMN) and monocytic leukocytes using double label immunoelectron microscopy (IEM) with ultrathin frozen sections and colloidal-gold conjugates. Rabbit antibodies to 67-kD human laminin receptor (LNR) were located on the inner surface of the specific granule membrane and within its internal matrix. LNR antigens co-distributed with lactoferrin, a marker of specific granules, but did not co-localize with elastase in azurophilic granules of PMNs. Further, CD11b/CD18 (leukocyte receptor for C3bi, fibrinogen, endothelial cells, and endotoxin), mammalian fibronectin receptor (FNR), and vitronectin receptor (VNR) antigens were also co-localized with LNR in PMN specific granules. A similar type of granule was found in monocytes which stained for LNR, FNR, VNR, CD18, and lysozyme. Activation of PMNs with either PMA, f-met-leu-phe (fMLP), tumor necrosis factor (TNF), or monocytic leukocytes with lipopolysaccharide (LPS), induced fusion of specific granules with the cell membrane and expression of both LNR and CD18 antigens on the outer cell surface. Further, stimulation led to augmented PMN adhesion on LN substrata, and six- to eightfold increases in specific binding of soluble LN that was inhibited by LNR antibody. These results indicate that four types of extracellular matrix receptors are located in leukocyte specific granules, and suggest that up-regulation of these receptors during inflammation may mediate leukocyte adhesion and extravasation. We have thus termed leukocyte specific granules adhesomes.
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PMID:Adhesomes: specific granules containing receptors for laminin, C3bi/fibrinogen, fibronectin, and vitronectin in human polymorphonuclear leukocytes and monocytes. 248 Mar 53

Production of fibronectin (Fn) and prostaglandin E2 (PGE2) by human alveolar macrophages (AM) which were obtained by bronchoalveolar lavage was studied in vitro. AM obtained from patients with idiopathic interstitial pneumonia (IIP) produced much more Fn than those from normal volunteers but produced less amounts of PGE2. We also tested the effect of lipopolysaccharide (LPS), phorbol 12-myristate 13-acetate (PMA), zymosan and albumin-anti albumin complex (alb-anti alb) on production of Fn and PGE2 from AM. LPS, PMA and zymosan suppressed Fn production but stimulated PGE2 production by AM from patients with IIP but indomethacin reversed the suppressive effect of LPS, PMA and zymosan on Fn production. On the contrary, alb-anti alb stimulated Fn production by AM. Furthermore, exogenous PGE2 suppressed Fn production by AM from patients with IIP in a dose-dependent manner. These data suggest that Fn production by AM may be changed by different stimuli or different states of disease, and there is close relationship between the production of Fn and PGE2 by AM.
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PMID:[Production of fibronectin and PGE2 by cultured human alveolar macrophages]. 262 10

The secretion of fibronectin (Fn) by rat peritoneal macrophages was found to be down-regulated by LPS. A sensitive ELISA was used to quantitate both substrate-attached and supernatant Fn. Thioglycollate-elicited peritoneal exudate cells were observed to release a considerable amount of Fn during the adherence procedure for macrophage purification. After this procedure, macrophage Fn levels peaked within 2 hr and then declined steadily to baseline levels by 96 hr. Fn release by exudate cells during adherence purification was less affected by cycloheximide treatment than was subsequent Fn secretion by purified macrophages. Macrophages elicited with thioglycollate and P. acnes displayed enhanced Fn secretory activity when compared with resident unstimulated cells. Exposure to lipopolysaccharide (LPS) suppressed the levels of immunoreactive Fn in supernatants of elicited cells. This inhibition was shown to be dose-dependent and most significant after 24 hr of incubation. The inclusion of polymyxin B in the culture medium did not reverse the LPS-induced inhibition of Fn production but did prevent LPS stimulation of interleukin-1 secretion in the macrophage cultures. These observations demonstrate that Fn secretion by macrophages is regulated according to the functional state of the cell.
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PMID:Modulation of macrophage fibronectin secretion by LPS. 278 47

These studies involved the evaluation of human monocyte/macrophage activation by biomedical polymers coated with human blood proteins. The biomedical polymers were polyethylene, polydimethylsiloxane, woven Dacron fabric, expanded polytetrafluoroethylene, Biomer, and tissue culture treated polystyrene as the control. They were adsorbed with human blood proteins: albumin, fibrinogen, fibronectin, hemoglobin, and gamma globulin. The protein adsorbed polymers were evaluated for their potential to activate the monocyte/macrophage cellular population in vitro as assessed by the induction of the monocyte/macrophage inflammatory mediator, Interleukin 1 (IL1). Suppression of IL1 was observed when protein adsorbed polymers were compared to the appropriate protein adsorbed control. Protein adsorbed polymers, when compared to polymers without protein adsorption, stimulated IL1 production. The data presented in this manuscript show the level of induction and secretion of IL1 was dependent on the biomedical polymer and the protein adsorbed, as well as the requirement of lipopolysaccharide. These results show differential interactions occur between the proteins, monocytes/macrophages, and biomedical polymers which alter activation and induction of IL1.
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PMID:Plasma protein adsorbed biomedical polymers: activation of human monocytes and induction of interleukin 1. 278 77

On the basis of their recent studies, several researchers have suggested that the infertility associated with mild endometriosis is due to the alteration of peritoneal fluid, resulting in impairment of the viability of gametes or embryos. Elevated numbers of macrophages and lymphocytes have been reported in the peritoneal fluid of patients with endometriosis. Interleukin-1 (IL-1) a major product of activated macrophages and Interleukin-2 (IL-2), a product of most activated T-cells, have been postulated to play a role in the infertility associated with this disease, possibly by acting as direct embryotoxic agents. We have examined the effect of purified recombinant IL-1 and IL-2, which are not species-specific, on in vitro development of mouse embryos. Both interleukins had no effect on development to the blastocyst stage or on early stages of implantation, as measured in vitro by attachment and outgrowth of blastocysts to fibronectin-coated dishes. Moreover, co-culture of mouse embryos with activated human peritoneal macrophages had no effect on embryogenesis. We conclude that neither IL-1, nor other products of human macrophages activated by lipopolysaccharide, nor IL-2 are directly toxic to early mouse embryonic development.
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PMID:Absence of a direct effect of recombinant interleukins and cultured peritoneal macrophages on early embryonic development in the mouse. 278 73


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