The effect of local elevation of leukocyte cyclic AMP content on lysosomal enzyme release during acute inflammation in vivo

1977 ◽  
pp. 169-178
Author(s):  
D. A. Deporter
Keyword(s):  
Cyclic Amp ◽  
Lysosomal Enzyme ◽  
Acute Inflammation ◽  
Enzyme Release

Stobadine inhibits lysosomal enzyme release in vivo and in vitro

Life Sciences ◽  
1999 ◽  
Vol 65 (18-19) ◽  
pp. 1905-1907 ◽  
Author(s):  
Jana Navarová ◽  
Tatiana Mačičková ◽  
Katarina Horáková ◽  
Miroslava Urbančíková
Keyword(s):  
Lysosomal Enzyme ◽  
Enzyme Release

scholarly journals Bradykinin stimulates bone resorption and lysosomal-enzyme release in cultured mouse calvaria

1984 ◽  
Vol 219 (1) ◽  
pp. 329-332 ◽  
Author(s):  
G T Gustafson ◽  
U Lerner
Keyword(s):  
Bone Resorption ◽  
Bone Tissue ◽  
Lysosomal Enzyme ◽  
Enzyme Release ◽  
Newborn Mouse ◽  
Mouse Calvaria ◽  
Stable Calcium

The effect of bradykinin on bone resorption was studied in cultures of newborn-mouse calvaria. Bradykinin (0.03 microM, 1 microM) stimulated the release of 45Ca2+ from bones dissected out from mice prelabelled in vivo with 45Ca. Bradykinin (1 microM) also augmented the release of stable calcium (40Ca), Pi and the lysosomal enzyme beta-glucuronidase. The stimulatory effect of bradykinin on mineral mobilization and lysosmal -enzyme release could be blocked by indomethacin. It is speculated that concomitant generation of thrombin and bradykinin in areas of trauma and inflammation may induce resorption of nearby bone tissue.

Production of Peptides Inducing Chemotaxis and Lysosomal Enzyme Release in Human Neutrophils by Intestinal Bacteria in Vitro and in Vivo

1988 ◽  
Vol 23 (1) ◽  
pp. 121-128 ◽  
Author(s):  
V. S. Chadwick ◽  
D. M. Mellor ◽  
D. B. Myers ◽  
A. C. Selden ◽  
A. Keshavarzian ◽  
...  
Keyword(s):  
Lysosomal Enzyme ◽  
Intestinal Bacteria ◽  
Human Neutrophils ◽  
Enzyme Release

scholarly journals EVALUATION OF IN VITRO IMMUNOMODULATORY ACTIVITY OF AQUEOUS AND ETHANOLIC EXTRACT OF EULOPHIA NUDA LINDL

2018 ◽  
Vol 11 (11) ◽  
pp. 352 ◽  
Author(s):  
Vanita Kanase ◽  
Diptesh T Patil
Keyword(s):  
Lysosomal Enzyme ◽  
Stimulation Index ◽  
Ethanolic Extract ◽  
In Vivo Studies ◽  
Phagocytic Index ◽  
Immunomodulatory Activity ◽  
Myeloperoxidase Activity ◽  
Enzyme Release

Objective: The aim of this study was to evaluate the in vitro immunomodulatory activity of aqueous and ethanolic extract of dried tubers of Eulophia nuda.Methods: Effect of both the extracts was evaluated at various concentrations (832–6.5 μg/ml) for secretion of mediators such as nitric oxide (NO), superoxide, lysosomal enzyme, and myeloperoxidase activity of isolated murine peritoneal macrophages.Results: The extracts showed stimulation of NO, statistically significant at 832 μg/ml (SI 1.739) for ENA and at 832 μg/ml (stimulation index [SI] 1.662) for ENE; significant stimulation on lysosomal enzyme release for ENA at 832 μg/ml (SI 1.404) and ENE at 832 μg/ml (SI 1.513); myeloperoxidase activity was statistically significant for ENA at 832 μg/ml (SI 1.728) and ENE at 832 μg/ml (SI 1.770).Conclusion: In vitro phagocytic index showed significant results and thus proving the need for confirmation through in vivo studies.

scholarly journals HORMONAL CONTROL OF LYSOSOMAL ENZYME RELEASE FROM HUMAN NEUTROPHILS

1974 ◽  
Vol 139 (6) ◽  
pp. 1395-1414 ◽  
Author(s):  
L. J. Ignarro ◽  
T. F. Lint ◽  
W. J. George
Keyword(s):  
Cyclic Amp ◽  
Cyclic Gmp ◽  
Lysosomal Enzyme ◽  
Lysosomal Enzymes ◽  
Hormonal Control ◽  
Human Neutrophils ◽  
Cell Contact ◽  
Enzyme Release ◽  
Lactate Dehydrogenase Activity ◽  
Particle Uptake

The purpose of this investigation was to examine the effects of autonomic neurohormones, cyclic nucleotides, and related agents on the immunologic discharge of lysosomal enzymes from, and phagocytosis by, purified human neutrophils. In order to discern the possible intracellular mechanisms by which certain neurohormones influence neutrophil function, the concentrations of cyclic AMP and cyclic GMP in neutrophils were assessed during cell contact with phagocytizable particles and autonomic agents. The model system employed for study was the interaction of purified human neutrophils with rheumatoid arthritic (RA) serum-treated zymosan particles at 37°C in a neutral, balanced salt solution containing glucose. Neutrophils ingested the particles and discharged ß-glucuronidase but not lactate dehydrogenase activity during 30 min of incubation. Treatment of zymosan particles with RA serum was more effective than treatment with normal serum with regard to the extent of both particle uptake and lysosomal enzyme release. During contact of neutrophils with RA serum-treated zymosan particles epinephrine, isoproterenol, and cyclic AMP inhibited both particle ingestion and ß-glucuronidase discharge. These actions of epinephrine were associated with a concomitant elevation of cyclic AMP levels. In contrast to the actions of catecholamines and cyclic AMP, acetylcholine and cyclic GMP accelerated lysosomal enzyme release without affecting particle uptake. The actions of acetylcholine were associated with a concomitant elevation of cyclic GMP levels. Increases in neutrophil levels of cyclic GMP but not of cyclic AMP were associated also with the discharge of ß-glucuronidase provoked by particles in the absence of added cholinergic agents. The data suggest that the immunologic release of lysosomal enzymes from human neutrophils can be regulated by autonomic neurohormones, perhaps via the selective formation of appropriate nucleotides.

scholarly journals Regulation of macrophage lysosomal enzyme secretion: role of arachidonate metabolites, divalent cations and cyclic AMP

1980 ◽  
Vol 44 (1) ◽  
pp. 299-315
Author(s):  
R.M. McMillan ◽  
D.E. Macintyre ◽  
J.E. Beesley ◽  
J.L. Gordon
Keyword(s):  
Cyclic Amp ◽  
Lysosomal Enzyme ◽  
Lysosomal Enzymes ◽  
Divalent Cations ◽  
Cell Types ◽  
Enzyme Secretion ◽  
Ionophore A23187 ◽  
Enzyme Release ◽  
Arachidonate Metabolites

We have investigated the role in macrophage lysosomal enzyme release of arachidonate metabolites, extracellular divalent cations and cyclic AMP (cAMP) which modulate secretion in other cell types. Lysosomal enzyme secretion induced by zymosan was accompanied by release of malondialdehyde (MDA), which is derived from arachidonic acid via prostaglandin synthase. Blockade of MDA formation, by aspirin or indomethacin, was associated with only a small inhibitory effect on lysosomal enzyme release by zymosan: arachidonate metabolites thus play only a minor role in mediating macrophage lysosomal enzyme release. Zymosan-induced secretion of lysosomal enzymes from macrophages did not require extracellular magnesium or calcium although release was enhanced by magnesium and inhibited by calcium. These effects may be related to an influence of the ions on phagocytosis. Elevation of intracellular divalent cation concentrations, by ionophore A23187, induced release of lysosomal enzymes but this was a result of cell lysis. Adenylate cyclase stimulants and dibutyryl cAMP produced slight inhibition of zymosan-induced lysosomal enzyme release. Aminophylline and papaverine caused more marked inhibition but their effects may be due to actions independent of phosphodiesterase inhibition. Our data indicate that arachidonate metabolites and cAMP do not play a major role in regulating zymosan-induced enzyme release from macrophages. Extracellular calcium and magnesium may modulate secretion but the role of intracellular divalent cations remains to be established. We conclude that macrophage lysosomal enzyme secretion is controlled by regulatory mechanisms different from those which control similar degranulation processes in other cell types.

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