scholarly journals Glucan receptor and zymosan-induced lysosomal enzyme secretion in macrophages

1995 ◽  
Vol 306 (3) ◽  
pp. 829-835 ◽  
Author(s):  
H Tapper ◽  
R Sundler
Keyword(s):  
Lysosomal Enzyme ◽  
Intracellular Signaling ◽  
Peritoneal Macrophages ◽  
Secretory Response ◽  
Enzyme Secretion ◽  
Cell Contact ◽  
Beta Glucan ◽  
High Particle ◽  
Mouse Peritoneal Macrophages ◽  
Multiple Interactions

A receptor for beta-glucan was in the present study shown to mediate binding of zymosan particles to resident mouse peritoneal macrophages. Lysosomal enzyme secretion in response to zymosan was maximal at a low particle/cell ratio, continuous for at least 3 h after particle/cell contact and inhibitable by soluble glucan. Latex particles of various size caused no selective secretory response, but at high particle/cell ratios were toxic. By use of a fluorescent ligand, the macrophage beta-glucan receptor was shown to be trypsin-sensitive, Ca2+/Mg(2+)-independent, recirculating and also present in an intracellular mobilizable pool. Binding of ligand to the beta-glucan receptor and inhibition of the lysosomal secretory response to zymosan were both more efficient with glucans of larger size, indicating that clustering of glucan receptors at the cell surface occurs. Such clustering could stabilize ligand binding by multiple interactions and possibly trigger intracellular signaling events on binding of zymosan particles.

scholarly journals Phagolysosome formation in normal and colchicine-treated macrophages.

1975 ◽  
Vol 142 (4) ◽  
pp. 903-913 ◽  
Author(s):  
E L Pesanti ◽  
S G Axline
Keyword(s):  
Acid Phosphatase ◽  
Lysosomal Enzyme ◽  
Peritoneal Macrophages ◽  
Cell Type ◽  
Inert Particles ◽  
Time Periods ◽  
Mouse Peritoneal Macrophages ◽  
Over Time

Intracellular lysosomal fusion has been evaluated in cultivated mouse peritoneal macrophages by measurement of transfer of acid phosphatase to polyvinyltoluene (PVT)-containing phagolysosomes. Enzyme transfer was found to be directly and significantly related to the uptake of PVT and to be independent of time allowed for phagolysosome formation over time periods of 15 min to 18 h. In addition, the extent of transfer of lysosomal enzyme to phagolysosomes was unaffected by treatment of the cells with 10(-6) M colchicine, a dose which eradicates morphologically identifiable microtubules in this cell type within 2 h. The data indicate that intracellular fusion of lysosomes with phagosomes in the macrophage does not require formed microtubules and suggest that fusion occurs promptly after interiorization of inert particles.

ANGPTL2 Promotes Inflammation via Integrin α5β1 in Chondrocytes

Cartilage ◽  
2019 ◽  
pp. 194760351987824 ◽  
Author(s):  
Mami Takano ◽  
Naoto Hirose ◽  
Chikako Sumi ◽  
Makoto Yanoshita ◽  
Sayuri Nishiyama ◽  
...  
Keyword(s):  
Real Time ◽  
Intracellular Signaling ◽  
Polymerase Chain Reaction Analysis ◽  
Peritoneal Macrophages ◽  
Inflammatory Factors ◽  
Related Factor ◽  
Rt Pcr ◽  
Integrin Α5β1 ◽  
Tnf Α ◽  
Mouse Peritoneal Macrophages

Background Angiopoietin-like protein 2 (ANGPTL2) is a secreted molecule with numerous physiologic and pathologic functions, for example, in angiogenesis, hematopoiesis, and tumorigenesis. Although recent studies implicated ANGPTL2 in chronic inflammation in mouse peritoneal macrophages, human ligamentum flavum fibroblasts, and human retinal microvascular endothelial cells, the mechanism underlying ANGPTL2-associated inflammation in chondrocytes remains unclear. Therefore, it was investigated whether ANGPTL2 is expressed in or functions in chondrocytes. Methods Expression of ANGPTL2 and its receptor, integrin α5β1 were examined over time in ATDC5 cells using real-time RT-PCR (reverse transcription–polymerase chain reaction) analysis. ATDC5 cells were then incubated with or without ANGPTL2 for 3 hours, and expression of the IL-1β, TNF-α, COX-2, aggrecanase (ADAMTS)-5, matrix metalloproteinase (MMP)-3, and MMP-13 genes were examined using real-time RT-PCR. Additionally, phosphorylation of ERK, JNK, p38, Akt, and NF-κB was examined by western blotting. Furthermore, it was also investigated for the effect of anti-integrin α5β1 antibody on the expression of inflammatory markers and intracellular signaling pathways. Results ANGPTL2 induced the phosphorylation of all 3 MAPKs, Akt, and NF-κB and dramatically upregulated the expression of inflammation-related factor genes. Inhibiting the activation of integrin α5β1 suppressed these reactions. Conclusion ANGPTL2 may induce inflammatory factors by stimulating the integrin α5β1/MAPKs, Akt, and NF-κB signaling pathway.

scholarly journals Spontaneous lysosomal enzyme secretion by a murine macrophage-like cell line

1980 ◽  
Vol 190 (3) ◽  
pp. 847-850 ◽  
Author(s):  
W Jessup ◽  
R T Dean
Keyword(s):  
Cell Line ◽  
Lysosomal Enzyme ◽  
Peritoneal Macrophages ◽  
Enzyme Secretion ◽  
Murine Macrophage ◽  
Lysosomal Hydrolase

Lysosomal enzyme secretion by the murine macrophage-like cell line, P388D1, was compared with that of normal peritoneal macrophages. Unlike macrophages, lysosomal hydrolase secretion by P388D1 cells occurred spontaneously in vitro and was not further stimulated by the presentation of inflammatory agents such as zymosan and asbestos.

scholarly journals Secretion of lysosomal hydrolases by stimulated and nonstimulated macrophages.

1978 ◽  
Vol 148 (2) ◽  
pp. 435-450 ◽  
Author(s):  
J Schnyder ◽  
M Baggiolini
Keyword(s):  
Plasminogen Activator ◽  
Lysosomal Enzyme ◽  
Peritoneal Macrophages ◽  
Enzyme Secretion ◽  
Wall Material ◽  
Lysosomal Hydrolases ◽  
Intracellular Enzyme ◽  
Proteose Peptone ◽  
Peptone Medium

Peritoneal macrophages were obtained from untreated mice and from mice treated with thioglycollate medium (TA), proteose peptone medium (PP), or a suspension of streptococcus A cell wall material (SA). The biochemical and secretory properties of these cells in long term cultures (up to 2 wk) were compared. TA-elicited macrophages contained more protein, lactate dehydrogenase, lysosomal hydrolases, and in particular, more plasminogen activator than the other cells studied. All types of macrophages studied were found to release considerable amounts of lysosomal hydrolases (beta-glucuronidase, N-acetyl-beta-glucosaminidase, alpha-mannosidase, and acid phosphatase) into the medium. Release was independent of phagocytosis and must, therefore, be regarded as true secretion. In both elicited and nonelicited macrophages, the rates of lysosomal enzyme secretion were virtually identical in the presence and in the absence of serum, and they were not enhanced by increasing serum concentrations. Lysosomal enzyme secretion in macrophages appears to depend on protein synthesis, since it was blocked by low concentrations of cycloheximide which neither affected cell viability nor lowered the intracellular enzyme levels. The amounts of lysosomal hydrolases secreted were highest in TA-elicited macrophages. The rates of secretion of PP- or SA-elicited and of nonelicited macrophages were about one-fourth of that of the TA-elicited cells. This difference, although significant, is much smaller than that observed for the secretion of plasminogen activator which was 20-50 times higher in TA-elicited cells. Acid glycosidases were also found in the peritoneal lavage media used for cell harvesting from both treated and nontreated mice. This indicates that active secretion of lysosomal hydrolases may be an in vivo property of the macrophage.

scholarly journals The selective release of phospholipase A2 by resident mouse peritoneal macrophages

1981 ◽  
Vol 200 (2) ◽  
pp. 441-444 ◽  
Author(s):  
P D Wightman ◽  
M E Dahlgren ◽  
P Davies ◽  
R J Bonney
Keyword(s):  
Phospholipase A2 ◽  
Phospholipase C ◽  
Lysosomal Enzyme ◽  
Enzyme Activities ◽  
Lysosomal Enzymes ◽  
Culture Medium ◽  
Peritoneal Macrophages ◽  
Cellular Activity ◽  
Mouse Peritoneal Macrophages ◽  
Phospholipase A2 Activity

Resident mouse peritoneal macrophages have three phospholipase activities: a phospholipase A2 active at pH 4.5, a Ca2+-dependent phospholipase A2 active at pH 8.5 and a phosphatidylinositol-specific phospholipase C activity. When macrophages are exposed to zymosan in culture, the cellular activity of pH-4.5 phospholipase A2 is diminished in a manner dependent on zymosan concentration and time of exposure, whereas the cellular activities of pH-8.5 phospholipase A2 and phospholipase C remain unchanged. The depletion of pH-4.5 phospholipase A2 activity from the cell is paralleled by a quantitative recovery of this activity in the culture medium in a manner similar to the cellular depletion and extracellular recovery of two lysosomal enzymes. This release is specifically elicited by an inflammatory substance such as zymosan, since macrophages incubated with 6 micrometer latex spheres retain pH-4.5 phospholipase A2 activity and lysosomal enzyme activities intracellularly.

scholarly journals Primary amines induce selective release of lysosomal enzymes from mouse macrophages

1980 ◽  
Vol 188 (3) ◽  
pp. 933-936 ◽  
Author(s):  
D W Riches ◽  
D R Stanworth
Keyword(s):  
Chain Length ◽  
Lysosomal Enzyme ◽  
Lysosomal Enzymes ◽  
Peritoneal Macrophages ◽  
Primary Amines ◽  
Aliphatic Chain ◽  
Enzyme Release ◽  
Mouse Macrophages ◽  
Aliphatic Diamines ◽  
Mouse Peritoneal Macrophages

Cultured mouse peritoneal macrophages were found to release substantial amounts of lysosomal beta-glucuronidase and beta-glactosidase activites when exposed to millimolar concentrations of various primary aliphatic monoamines. With methylamine, ethylamine, propylamine and butylamine, lysosomal enzyme release was selective, but further increases in the aliphatic chain length resulted in the compounds becoming lytic. By contrast, structurally related primary aliphatic diamines proved to be inactive at inducing both selective and lytic lysosomal-enzyme discharge.

scholarly journals Trypanosoma cruzi: the immunological induction of macrophage plasminogen activator requires thymus-derived lymphocytes.

1977 ◽  
Vol 146 (1) ◽  
pp. 172-183 ◽  
Author(s):  
N Nogueira ◽  
S Gordon ◽  
Z Cohn
Keyword(s):  
Trypanosoma Cruzi ◽  
Spleen Cell ◽  
Plasminogen Activator ◽  
Peritoneal Macrophages ◽  
Enzyme Secretion ◽  
Cell Populations ◽  
Spleen Cells ◽  
Trypanocidal Activity ◽  
Mouse Peritoneal Macrophages

In this article we describe methods in which unstimulated mouse peritoneal macrophages were induced to secrete high livels of plasminogen activator under in vitro conditions. The exposure of sensitized peritoneal or spleen cell populations from Trypanosoma cruzi-infected animals to either viable or heat-killed trypanosomes lead to the release of an inducing factor(s). Maximal levels of plasminogen activator secretion are achieved by the incubation of such factors (s) with unstimulated macrophages for 48 h. A significant increase in enzyme secretion was already observed after a 24 h incubation. The production of the inducing factor(s) by sensitized cells was immunologically specific and unrelated antigens did not stimulate the production of the factor(s) by sensitized peritoneal or spleen cell populations. The inducing factor(s) was produced by nylon-wool-fractionated spleen and peritoneal cells which had been depleted of marcrophages. Pretreatment of sensitized spleen cells with anti-theta serum and C abolished the production of the activating factor(s). The active supernatant fluids were able to induce secretion of macrophage plasminogen activator across H-2 barriers. Attempts to induce trypanocidal activity in unstimulated macrophages have not been successful.

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