Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P15088 (mast cell)
 14,925 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The possible role of mast cells in the initiation of inflammation was studied in genetically mast cell-deficient mice, WBB6F1-W/Wv. Inflammation was induced by i.p. injection of thioglycollate. The influx of neutrophils was markedly delayed in WBB6F1-W/Wv mice as compared to the WBB6F1-+/+, mice (congeneic controls). At the time (14 h) of maximum influx of neutrophils in WBB6F1-+/+ mice, thioglycollate caused a 3-fold increase in the total cell number in the peritoneal lavage fluid, and the neutrophil count was elevated 14-fold. At the same time point in W/Wv mice, the total cell number in the peritoneal lavage fluid was not increased significantly and the neutrophils were increased only three- to four-fold. Not only was the neutrophil influx in WBB6F1-W/Wv mice delayed, but the length of time during which the neutrophil count was elevated in the peritoneal fluid was significantly shortened. Transfer (i.p.) of mast cells cultured from the bone marrow of congeneic controls corrected the delay in the neutrophil influx. The magnitude of the neutrophil influx in WBB6F1-W/Wv mice was equivalent to that of congeneic controls 9 days after mast cell repletion. Histologic studies were performed to follow the migration and differentiation of mast cells after adoptive transfer into WBB6F1-W/Wv mice. No connective tissue mast cells could be identified on day 9 when the inflammatory reaction was restored. Migration of mast cells into the tissue, as studied in the cecum, progressed steadily. On day 9 after adoptive transfer, the mast cell number was 38% of congeneic controls. Therefore, the increase in thioglycollate-induced neutrophil influx in WBB6F1W/Wv mice after mast cell repletion seemed to be correlated, at least to some extent, with the migration of mast cells into tissues and not with differentiation into connective tissue mast cells. However, a certain maturation and differentiation may have occurred. These results suggest that mast cells play an important role, although they do not seem to be the only cell type responsible for the initiation of inflammation.
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PMID:The role of mast cells in thioglycollate-induced inflammation. 317 Nov 73

A new method has been developed that allows in vitro differentiation of rat mast cells from precursor cells in the absence of feeder layers. In the present investigation, the precursor cells are further characterized as to their nature, state of activation and distribution in different organs of the rat. The data support our previously published evidence, based on morphology and enzyme-cytochemical reaction patterns that the precursor cells are mononuclear phagocytes. Peritoneal macrophages elicited by mineral oil, thioglycollate or proteose-peptone have lost the ability to differentiate into mast cells. Single cell suspensions of spleen and bone marrow contain mast cell precursors, while cells from mesenteric lymph nodes and thymus or purified lymphocytes never yield mast cells in this culture system.
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PMID:Evidence that tissue mast cells derive from mononuclear phagocytes. 617 34

That M1/70, a monoclonal anti-murine macrophage antibody, recognizes murine natural killer cells (NK) and that there is an increase in NK following intraperitoneal infection with live Listeria monocytogenes (LM) was previously reported. Here, LM-induced NK cells were further characterized with respect to tumor target specificity and the expression of murine mast cell, mononuclear phagocyte, and lymphocyte differentiation antigens plus human NK-associated antigens. The M1/70-selected NK (Mac 1 NK) lysed Yac 1, RLmale 1, and WEHI 164.1, but not EL 4 or WTS cells. Immunoprecipitation with M1/70 demonstrated that Mac 1, the antigen recognized by M1/70, was present on NK and thioglycollate-elicited macrophages. Contaminating macrophages in the NK-enriched population did not account for the immunoprecipitated Mac 1. Mac 1 NK that lysed Yac 1 displayed Qa 5, LFA 1, asialo GM 1, Ly 5.1, and NK 1.2, but not Lyt 1, Lyt 2, Mac 2, Mac 3, or Mac 4. Thirty percent of these Mac 1 NK bore Thy 1.2. The presence of Thy 1.2 did not correlate with individual lytic efficiency or cell cycle. Antibodies to human NK antigens Leu 7, Leu 11a, and Leu 15 did not recognize LM-induced NK cells.
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PMID:Characterization of natural killer cells induced in the peritoneal exudates of mice infected with Listeria monocytogenes: a study of their tumor target specificity and their expression of murine differentiation antigens and human NK-associated antigens. 643 90

Intraperitoneal administration of zymosan and acetic acid induced a dose-dependent nociceptive writhing response in mice. Lavage of the peritoneal cavities with saline reduced the number of total resident peritoneal cells and caused a proportional decrease in the nociceptive responses induced by these stimuli. Furthermore, the specific reduction of the peritoneal mast cell population by intraperitoneal administration of compound 48/80 also reduced the nociceptive responses induced by zymosan and acetic acid. In contrast, enhancement of the peritoneal macrophage population by pretreatment of the cavities with thioglycollate caused an increase in the number of writhes induced by both stimuli. These data suggest that the nociceptive responses induced by zymosan and acetic acid are dependent upon the peritoneal resident macrophages and mast cells. These cells modulate the nociceptive response induced by zymosan and acetic acid via release of tumour necrosis factor alpha (TNF-alpha), interleukin 1beta and interleukin 8. This suggestion is supported by the following observations: (a) pretreatment of the peritoneal cavities with antisera against these cytokines reduced the nociceptive responses induced by these stimuli; (b) peritoneal cells harvested from cavities injected with zymosan or acetic acid released both interleukin 1beta and TNF-alpha; (c) although individual injection of TNF-alpha, interleukin 1beta or interleukin 8 did not induce the nociceptive effect, intraperitoneal injection of a mixture of these three recombinant cytokines caused a significant nociceptive writhing response. In conclusion, our results suggest that the nociceptive activity of zymosan and acetic acid in the writhing model is due to the release of TNF-alpha, interleukin 1beta and interleukin 8 by resident peritoneal macrophages and mast cells.
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PMID:Involvement of resident macrophages and mast cells in the writhing nociceptive response induced by zymosan and acetic acid in mice. 1063 69

Extravascular coagulation leading to fibrin deposition accompanies many immune and inflammatory responses. Although recognized by pathologists for decades, and probably pathologic under certain conditions, the physiologic functions of extravascular coagulation remain to be fully defined. This study demonstrates that thrombin can activate macrophage adhesion and prompt interleukin-6 (IL-6) and monocyte chemoattractant protein-1 (MCP-1) production in vivo. Peritoneal macrophages were elicited with thioglycollate (TG) and then activated in situ, either by intraperitoneal injection of lipopolysaccharide (LPS) or by injection of antigen into mice bearing antigen-primed T cells. Others previously established that such treatments stimulate macrophage adhesion to the mesothelial lining of the peritoneal cavity. The present study demonstrates that thrombin functions in this process, as macrophage adhesion was suppressed by Refludan, a highly specific thrombin antagonist, and induced by direct peritoneal administration of purified thrombin. Although recent studies established that protease activated receptor 1 (PAR-1) mediates some of thrombin's proinflammatory activities macrophage adhesion occurred normally in PAR-1-deficient mice. However, adhesion was suppressed in fibrin(ogen)-deficient mice, suggesting that fibrin formation stimulates macrophage adhesion in vivo. This study also suggests that fibrin regulates chemokine/cytokine production in vivo, as direct injection of thrombin stimulated peritoneal accumulation of IL-6 and MCP-1 in a fibrin(ogen)-dependent manner. Given that prior studies have clearly established inflammatory roles for PAR-1, thrombin probably has pleiotropic functions during inflammation, stimulating vasodilation and mast cell degranulation via PAR-1, and activating cytokine/chemokine production and macrophage adhesion via fibrin(ogen).
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PMID:Roles for thrombin and fibrin(ogen) in cytokine/chemokine production and macrophage adhesion in vivo. 1180 12

The initial phase of zymosan-induced peritonitis involves an increase of vascular permeability (peak at 30 min) that is correlated with high levels of vasoactive eicosanoids, namely, prostaglandins (PGI2 and PGE2) of cyclooxygenase-1 origin (as estimated by RT-PCR) and cysteinyl-leukotrienes. Previously, we showed that the increase of vascular permeability can be attributed only partially to mast cells and their histamine, as seen in mast cell-deficient WBB6F1-W/Wv mice. Thus we aimed to identify the major cellular source(s) that mediate vasopermeability, as well as particular vasoactive mediators operating in this model. For this purpose, some mice were selectively depleted of either peritoneal macrophages or mast cells, and/or they were treated with several pharmacologic inhibitors of cyclooxygenase- and lipoxygenase-metabolic pathways. More-over, macrophage-depleted mast cell-deficient WBB6F1-W/Wv mice and their controls (+/+) were used. The macrophage depletion always caused a profound decrease of both vascular permeability and lipid-mediator levels, which was particularly pronounced for leukotrienes, whereas the effects of mast-cell depletion were less severe. The macrophage/mast-cell co-mediation of vasopermeability was also revealed in thioglycolate-induced peritonitis, as well as the macrophage origin of cysteinyl-leukotrienes. Taken together, these findings demonstrate that the resident peritoneal macrophages are in fact the main contributors to the vasopermeability at the early stages of zymosan-induced peritonitis.
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PMID:Early vascular permeability in murine experimental peritonitis is co-mediated by resident peritoneal macrophages and mast cells: crucial involvement of macrophage-derived cysteinyl-leukotrienes. 1198 89

Spermadhesins are a group of (glyco)proteins from seminal fluid involved in various aspects of porcine fertilization. PSP-I/PSP-II, a heterodimer of glycosylated spermadhesins, is the major component of porcine seminal fluid. Its biological function remains, however, enigmatic. Using an in vitro chemotaxis assay, we showed that PSP-I/PSP-II and its isolated subunits induced migration of purified neutrophils. A possible proinflammatory activity of PSP-I/PSP-II induced upon injection of the spermadhesin heterodimer and its isolated subunits into the peritoneal cavity of rats was investigated. Lavage of peritoneal cavities, thioglycolate treatment, and mast cell depletion were done before spermadhesin administration, and neutrophil migration was evaluated 4 h after injections. Pharmacological modulation was also investigated. Resident cell depletion by lavage reduced the neutrophil migration induced by PSP-I/PSP-II and the PSP-II subunit but had no effect on that induced by isolated PSP-I. Both an increase of macrophage population by thioglycolate treatment and mast cell depletion potentiated the neutrophil migration induced by PSP-I/PSP-II and by PSP-II. The glucocorticoid dexamethasone but not indomethacin (cyclooxygenase inhibitor), MK886 (leukotriene inhibitor), and BN50739 (platelet activation factor [PAF] antagonist) inhibited neutrophil migration induced by PSP-I/PSP-II. Coincubation with mannose-6-phosphate (a PSP-II-specific ligand) inhibited neutrophil recruitment induced by PSP-II but did not alter the PSP-I activity. As a whole, the data suggested that enhancement of the neutrophil migration-inducing activity of PSP-I/PSP-II and PSP-II involved an indirect mechanism, i.e., via activation of resident cells, probably macrophages. On the other hand, PSP-I appeared to act directly on neutrophils. We hypothesize that the neutrophil migration-inducing effect displayed by PSP-II might be due to interaction of its lectin domain with cellular receptors and that neutrophil recruitment induced by PSP-I may involve protein-protein interactions.
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PMID:Spermadhesin PSP-I/PSP-II heterodimer and its isolated subunits induced neutrophil migration into the peritoneal cavity of rats. 1244 55

Bleiweis, Arnold S. (The Pennsylvania State University, University Park), and Leonard N. Zimmerman. Properties of proteinase from Streptococcus faecalis var. liquefaciens. J. Bacteriol. 88:653-659. 1964.-The extracellular group D streptococcal proteinase is inactivated by chelating agents [ethylenediamine-tetraacetate (EDTA), o-phenanthroline, and 8-quinolinol] and mercaptans (cysteine, mercaptoethanol, and thioglycolate). The optimal inhibitory concentrations of EDTA (4 x 10(-4)m) and cysteine (2.5 x 10(-2)m) promote rapid loss of activity with 50% inactivation after 4 to 5 min. Enzyme inactivated by either EDTA or cysteine is reactivated about 80% by 4 x 10(-4)m Zn(++). Such reactivation of EDTA-treated enzyme is prevented completely by iodoacetate (5 x 10(-2)m) and of cysteine-treated enzyme by oxidizing conditions, which suggests that the zinc binding-site may be a thiol. High levels of zinc (10(-3)m) do not allow reactivation in either case, and actually inhibit native proteinase. Ca(++), Mg(++), Co(++), Fe(++), Cu(++), and Ni(++) do not reactivate cysteine-treated enzyme, but Mn(++) (10(-4) to 8 x 10(-4)m) allows 27% reversal. N(2)-held, cysteine-treated enzyme can be spontaneously reactivated if the substrate is flushed with O(2) during the assay; leakage of air or O(2) into the samples before assay leads to loss of reactivatability. Native proteinase does not lose activity after dialysis for 43 hr against 0.07 m phosphate buffer. It is concluded that the group D proteinase obtained from Streptococcus faecalis var. liquefaciens is probably a zinc metalloenzyme that is unlike the thiol-activated, group A streptococcal proteinase, but similar to the mammalian carboxypeptidase A.
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PMID:PROPERTIES OF PROTEINASE FROM STREPTOCOCCUS FAECALIS VAR. LIQUEFACIENS. 1420 3

PAL is a glucose/mannose-specific lectin isolated from Pisum arvense seeds. Previously, we demonstrated the capacity of other leguminous lectins to induce oedema formation and neutrophil stimulation. To investigate the potential pro-inflammatory activity of PAL, we have studied its ability to induce neutrophil migration into peritoneal cavities of rats and neutrophil chemotaxis in-vitro. The role of resident cells and sugar residues on PAL activity was analysed. PAL or saline (control) were administered intraperitoneally to rats, and total and differential leucocyte (macrophages, neutrophils and mast cells) counts were performed. The role of resident cells on the PAL effect was evaluated using three strategies: reducing the total resident cell population by lavage of rat cavities with saline; increasing macrophage population by treating animals with thioglycolate; and depleting mast cell population by subchronic treatment of rats with compound 48/80. PAL induced in-vitro and in-vivo neutrophil migration. In-vivo, PAL (50, 100, 200 and 300 microg) significantly (P < 0.05) and dose-dependently increased neutrophil migration by 600, 740, 900 and 940%, respectively, showing maximal effect 4 h after injection. PAL induced mononuclear cell migration. The neutrophil stimulatory effect of PAL was potentiated in animals treated with both thioglycolate and compound 48/ 80. The indirect lectin chemotactic effect was shown in rats injected with supernatant from cultured macrophages stimulated by PAL. In conclusion, PAL was shown to exhibit in-vivo and in-vitro proinflammatory activity. The in-vivo effect seemed to occur by a dual mechanism that was independent, but also dependent, on resident cells.
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PMID:Lectin of Pisum arvense seeds induces in-vivo and in-vitro neutrophil migration. 1580 94

Arum maculatum agglutinin (AMA) is a monocot lectin isolated from tubers of Arum maculatum L. (Araceae) which exhibits different specificity towards oligo-mannosidic-type and N-acetyllactosaminic-type glycans. We have investigated the effect of this lectin on the cells of the immune system. Models of neutrophil migration in vivo, neutrophil chemotaxis in vitro and macrophage cultures were used to study the lectin inflammatory activity. When administered into rat peritoneal cavities, AMA (80, 200 and 500 microg/mL/cavity) induced significant and dose-dependent neutrophil migration. This effect was inhibited by incubation with alpha-methyl-d-mannoside. A 83% depletion in the number of resident cells following peritoneal lavage did not reduce the AMA-induced neutrophil migration, as compared to sham animals (not washed). However, pre-treatment with 3% thioglycolate which increases the peritoneal macrophage population by 236%, enhanced the neutrophil migration induced by AMA (200 microg/mL/cavity) (119%, p < 0.05). Reduction of peritoneal mast cell population by chronic treatment of cavities with compound 48/80 did not modify AMA-induced neutrophil migration. The neutrophil chemotaxy assay in vitro shows that the lectin (300 microg/mL) induces neutrophil chemotaxy (368% p < 0.05) compared to RPMI. Finally, injection into peritoneal cavities of supernatants from macrophage cultures obtained after stimulation with AMA (300 microg/mL) enhanced neutrophil migration (110% p < 0.05). Summarizing, our data suggest that A. maculatum agglutinin presents pro-inflammatory activity, inducing neutrophil migration by two ways, one which is independent on resident cells and another one dependent on the presence of these cells.
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PMID:Pro-inflammatory effect of Arum maculatum lectin and role of resident cells. 1591 76


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