RAT PERITONEAL MACROPHAGES EXPRESS TWO DIFFERENT LECTIN-LIKE RECEPTORS ON THE CELL SURFACE

1981 ◽  
pp. 33-42
Author(s):  
Y. Nagamura ◽  
H. Kolb
Keyword(s):  
Cell Surface ◽  
Peritoneal Macrophages

scholarly journals Polymorphic glycoprotein-1 on mouse platelets: possible role of Pgp-1 and LFA-1 in antibody-dependent platelet cytotoxicity involving complement

Blood ◽  
1987 ◽  
Vol 69 (1) ◽  
pp. 211-218
Author(s):  
PJ McCaffery ◽  
AS Tan ◽  
MV Berridge
Keyword(s):  
Cell Surface ◽  
Peripheral Blood ◽  
Broad Band ◽  
Peritoneal Macrophages ◽  
Beta Subunits ◽  
Deficient Mouse ◽  
Antibody Dependent Cellular Cytotoxicity ◽  
Functional Studies ◽  
Immune Adherence

The presence of the Pgp-1 glycoprotein on mouse platelets is demonstrated by antibody-binding techniques, by immunoprecipitation, and by transblotting using the monoclonal antibody (MoAb) C71/26 against Pgp-1. C71/26 immunoprecipitates as a broad band of mol wt 87,000 to 100,000 as determined by radioiodination of the platelet cell surface and by the 3H-sodium borohydride labeling technique. Immunoblotting showed Pgp-1 expression on platelets to be quantitatively similar to its presence on macrophages and resolved platelet Pgp-1 into two bands of mol wt 87,000 and 97,000 whereas Pgp-1 on parasite-elicited peritoneal macrophages showed 82,000 and 87,000 mol wt species. Platelets and monocyte/macrophage cells from either peripheral blood or from the peritoneal cavity showed homogeneous binding of Pgp-1 antibody to greater than 97% of cells by flow cytometry. In contrast, lymphocytes from peripheral blood or from the spleen showed a heterogeneous binding pattern with 20% to 30% of cells being negative, and the majority weakly positive. In functional studies, MoAbs against CR1 and CR3 substantially inhibited platelet immune adherence, whereas C71/26 showed only marginal inhibitor. In contrast, C71/26 and other MoAbs against Pgp-1 inhibited platelet- dependent cytotoxicity of antibody-coated sheep erythrocytes in the presence of C5-deficient mouse plasma whereas M1/70 against CR3 showed no effect. In this assay, MoAbs against the alpha- and beta-subunits of leukocyte functional molecule LFA-1 also inhibited platelet cytotoxicity. These results show that the platelet cell surface moieties Pgp-1 and LFA-1 are involved in or closely associated with antibody-dependent cellular cytotoxicity by platelets.

Participation of concanavalin A binding sites in the interaction between Trypanosoma cruzi and macrophages

1983 ◽  
Vol 62 (1) ◽  
pp. 287-299
Author(s):  
M.N. Meirelles ◽  
A. Martinez-Palomo ◽  
T. Souto-Padron ◽  
W. De Souza
Keyword(s):  
Plasma Membrane ◽  
Cell Surface ◽  
Trypanosoma Cruzi ◽  
Uniform Distribution ◽  
Concanavalin A ◽  
Binding Sites ◽  
Peritoneal Macrophages ◽  
Untreated Mouse ◽  
Mouse Peritoneal Macrophages

Untreated mouse peritoneal macrophages as well as macrophages treated with concanavalin A (ConA) were incubated in the presence of untreated or ConA-treated epimastigotes and trypomastigotes of Trypanosoma cruzi. Treatment of epimastigotes or trypomastigotes with ConA increased or decreased their uptake by macrophages, respectively. Treatment of their macrophages with ConA reduced by 70% and increased by five times the ingestion of epimastigotes and trypomastigotes, respectively. These results are discussed in relation to previous studies on the mobility of ConA receptors in the membrane of the parasite. Using fluorescein- or ferritin-labelled ConA we observed that ConA binding sites located on the plasma membrane of macrophages are internalized during endocytosis of T. cruzi, and observed in association with the membrane of the endocytic vacuole. Vacuoles without parasites showed a uniform distribution of ConA binding sites, while these sites were distributed in patches in vacuoles containing parasites. These results, in association with others previously reported, suggest the involvement of glycoproteins and/or glycolipids localized on the cell surface of T. cruzi and macrophages during the T. cruzi-macrophage interaction.

The in vitro effect of Actinobacillus actinomycetemcomitans strain Y4 lipopolysaccharide on murine peritoneal macrophages

1983 ◽  
Vol 29 (11) ◽  
pp. 1552-1563 ◽  
Author(s):  
Kathleen A. Barker ◽  
S. C. Holt
Keyword(s):  
Cell Surface ◽  
Cell Activation ◽  
Cell Injury ◽  
Peritoneal Macrophages ◽  
Cell Ultrastructure ◽  
Actinobacillus Actinomycetemcomitans ◽  
Short Term ◽  
Murine Peritoneal Macrophage ◽  
Vitro Effect

Actinobacillus actinomycetemcomitans strain Y4 lipopolysaccharide (LPS) was examined for its in vitro effect on murine peritoneal macrophage morphology, viability, and lysosomal enzyme activity. Fifty micrograms of Y4 LPS per 106 macrophages resulted in macrophage activation, eliciting the release of acid phosphates (AcP), as well as the accumulation of intracellular AcP, without a loss in viability. There was also an increase in the number of organelles and cell-surface ruffles. One hundred or 250 μg of Y4 LPS caused flattening, rounding, and blebbing of the cell surface, as well as the release of large quantities of AcP and lactate dehydrogenase (LDH), within 5 min of exposure to the LPS. Alteration of cell ultrastructure occurred within 30 min, and extensive autophagocytosis by 24 h, indicative of cell injury. Short-term (less than 24 h) experiments appear necessary to distinguish between the effects of cell activation and cell death caused by A. actinomycetemcomitans Y4 LPS.

scholarly journals Is Percoll innocuous to cells?

1982 ◽  
Vol 202 (3) ◽  
pp. 795-797 ◽  
Author(s):  
J S Wakefield ◽  
J S J Gale ◽  
M V Berridge ◽  
T W Jordan ◽  
H C Ford
Keyword(s):  
Cell Surface ◽  
Leydig Cells ◽  
Density Gradient Centrifugation ◽  
Gradient Centrifugation ◽  
Peritoneal Macrophages ◽  
Isolated Rat Liver ◽  
Subcellular Organelles ◽  
Large Numbers ◽  
Gradient Medium ◽  
Isolated Rat

Peritoneal macrophages from mice, isolated rat liver Kupffer cells and rat testis Leydig cells ingested large numbers of Percoll particles, a gradient medium widely used for separation of cells and subcellular organelles by density-gradient centrifugation. A decrease in the percentage of macrophages adhering to plastic also occurred after exposure of the cells to Percoll, even at 4 degrees C, a temperature at which Percoll was not ingested. The effect of Percoll on macrophage adherence may involve a loose association between the density medium and the cell surface. Other cell-surface-related phenomena may also be affected by prior exposure of cells to Percoll.

scholarly journals Protein kinase activity associated with the surface of guinea pig macrophages.

1978 ◽  
Vol 148 (4) ◽  
pp. 1099-1104 ◽  
Author(s):  
E Remold-O'Donnell
Keyword(s):  
Protein Kinase ◽  
Cell Surface ◽  
Guinea Pig ◽  
Outer Surface ◽  
Inorganic Phosphate ◽  
Kinase Activity ◽  
Peritoneal Macrophages ◽  
Protein Kinase Activity ◽  
Associated Proteins ◽  
Phosphate Donor

Protein kinase activity has been detected associated with the outer surface of guinea pig peritoneal macrophages. Macrophages incubated with [gamma-32P]ATP incorporated 32P-phosphate into cell-associated proteins. Inorganic phosphate did not compete, nor could inorganic [32P]phosphate substitute as the phosphate donor, demonstrating that transfer of phosphate from ATP to protein is direct and extracellular. The macrophage-associated protein kinase was also shown to phosphorylate added acceptor protein (histone) and to be tightly associated with the cell surface. Thus, a new ectoenzyme, a protein kinase, has been detected in macrophages.

scholarly journals Post-transcriptional regulation of syndecan-1 expression by cAMP in peritoneal macrophages

1993 ◽  
Vol 122 (4) ◽  
pp. 941-950 ◽  
Author(s):  
C Yeaman ◽  
AC Rapraeger
Keyword(s):  
Cell Surface ◽  
Heparan Sulfate ◽  
Mrna Translation ◽  
Peritoneal Macrophages ◽  
Distinct Pattern ◽  
Intracellular Camp ◽  
Growth Factor Signaling ◽  
Blood Monocytes ◽  
Dibutyryl Camp ◽  
Stored Mrna

Syndecan-1 is a cell surface heparan sulfate proteoglycan that is proposed to serve in cell-cell adhesion, cell-matrix anchorage, and growth factor signaling. Its expression is temporally and spatially regulated during epithelial-mesenchymal interactions in many developing tissues. In some cases, this regulation appears to be achieved at the level of transcription. However, induction of syndecan-1 expression in the embryonic kidney mesenchyme is suggested to occur at the level of mRNA translation (Vainio, S., M. Jalkanen, M. Bernfield, and L. Saxén. 1992. Dev. Biol. 152:221-232). To identify a system in which the regulatory mechanisms controlling syndecan-1 expression can be studied, cells of the monocyte-macrophage lineage, which regulate the expression of many cell surface receptors, were screened for syndecan-1 expression. The syndecan-1 gene is active in blood monocytes as well as resident and thioglycollate-elicited mouse peritoneal macrophages, but expression of the proteoglycan is regulated at two levels. First, elicited macrophages accumulate nine-fold more syndecan-1 mRNA than do resident macrophages or circulating blood monocytes. Another member of the syndecan family of proteoglycans, syndecan-4, shows a distinct pattern of expression, suggesting that this regulation is specific for syndecan-1. Second, utilization of the mRNA for syndecan-1 production encounters a post-transcriptional block in the elicited macrophages that can be overcome by triggering agents such as E-type prostaglandins or dibutyryl cAMP, which raise intracellular cAMP levels. Dibutyryl cAMP does not induce syndecan-1 expression in resident peritoneal macrophages, which lack a pool of stored mRNA. This suggests that this agent promotes the post-transcriptional utilization of stored syndecan-1 mRNA. The induced proteoglycan appears at the cell surface as a integral of 100-kD heparan sulfate-rich isoform of syndecan-1. This suggests that a cAMP-dependent post-transcriptional control mechanism may be present in a variety of tissues when syndecan-1 expression is regulated.

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