Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.2.1.31 (beta-glucuronidase)
 7,680 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We have studied the effects of prostaglandin E1 (PGE1) on the release of lysosomal enzymes such as beta-glucuronidase in leukocyte (beta-GL) and granulocyte elastase (GEL) in 52 patients for major abdominal surgery. All patients were divided into two groups; the PG group (24 patients) and the control group (28 patients). The patients of the PG group received PGE1 continuously at the rate of 0.03 to 0.1 micrograms.kg-1.min-1 during surgery. Plasma levels of GEL and beta-GL, which are known to be the indicators of tissue destruction, were measured during and after surgery. The GEL/granulocyte ratio in the PG group was significantly smaller than that of the control group during surgery. The rate of change of beta-GL was significantly depressed in the PG group compared to that of the control group. These findings suggest that the administration of PGE1 during major abdominal surgery inhibits the release of lysosomal enzymes, and this prevents tissue injury during and after surgery.
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PMID:[The effects of prostaglandin E1 on the release of beta-glucuronidase in leukocyte and granulocyte elastase in patients for major abdominal surgery]. 851 50

Polymorphonuclear cells (PMN) are the dominating inflammatory cell population in acute tissue injury and contribute to host-defence mechanisms by formation and release of chemical mediators. The aim of the present study was to investigate whether chemoattractant-induced PMN stimulation can be synergistically antagonized by vasodilatory prostaglandins and nitric oxide (NO), both being formed by the vasculature in inflamed areas. PGE1 (10 nM-10 microM) inhibited concentration-dependently formyl-methionyl-leucyl-phenylalanine (fMLP)-induced beta-glucuronidase and oxygen radical (O2.) release from human PMN. The NO donor linsidomine (100 microM) was ineffective, but significantly enhanced PGE1 effects on oxygen radical generation and enzyme release. The non-selective phosphodiesterase inhibitor 3-isobutyl-l-methylxanthine (IBMX) (0.5 mM) potentiated PGE1 effects on all parameters measured. The combination linsidomine (100 microM) plus IBMX (0.5 mM) did not additionally reduce beta-glucuronidase release, but abolished fMLP-stimulated O2. generation. There was a stimulation of cAMP formation by PGE1 but not by linsidomine, both in the absence and presence of IBMX. It is concluded that the effects of linsidomine on PMN function and its synergism with PGE1 are not tightly correlated with total cAMP accumulation. Alternatively, the inhibition of O2. generation by linsidomine may be related to its ability to modulate the activation of the NADPH oxidase system or to scavenge free oxygen radicals.
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PMID:Synergistic inhibition of human polymorphonuclear function by prostaglandin E1 and linsidomine. 886 34

3-(5'-Hydroxymethyl-2'-furyl)-1-benzyl indazole (YC-1), a novel type of soluble guanylyl cyclase (sGC) activator, is useful in investigating the signaling of cGMP and may provide a new approach for treating cardiovascular diseases. Herein, YC-1 was demonstrated to inhibit the generation of superoxide anion (O2-) and the release of beta-glucuronidase release, to diminish the membrane-associated p47phox and to accelerate resequestration of cytosolic calcium in formyl-l-methionyl-l-leucyl-l-phenylalanine-activated human neutrophils. YC-1 not only directly promoted sGC activity and cGMP formation but also dramatically potentiated sodium nitroprusside-induced sGC activity and cGMP formation in human neutrophils. However, the synergistic increase in the amount of cGMP was inconsistent with its cellular response. Moreover, neither an sGC inhibitor nor protein kinase G inhibitors reversed the inhibitory effect of YC-1. Interestingly, YC-1 also increased the cAMP concentration and protein kinase (PK)A activity. The inhibitory effect of YC-1 was significantly enhanced by prostaglandin (PG)E1 and isoproterenol, and almost abolished by PKA inhibitors. These results show that cAMP, but not cGMP, mediates the YC-1-induced inhibition of human neutrophils. YC-1 increased the PGE1- and forskolin-induced but not 3-isobutyl-1-methylxanthine-produced cAMP formation, suggesting inhibition of phosphodiesterase. These findings thus reveal novel mechanism-mediated anti-inflammatory properties of YC-1 in human neutrophils, which can influence the progression of cardiovascular disease. cAMP, but not cGMP, plays an important role in the regulation of respiratory burst and degranulation in human neutrophils.
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PMID:Soluble guanylyl cyclase activator YC-1 inhibits human neutrophil functions through a cGMP-independent but cAMP-dependent pathway. 1464 72


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