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)

Blood phagocytes of the dogfish Mustelus canis attack oocytes of the sea urchin Arbacia punctulata, first provoking a surrogate fertilization response and then killing the eggs. To test the hypothesis that secretion of lysosomal contents is critical in this model of phagocyte-mediated cell injury, we studied effects of agents that modify lysosomal enzyme secretion. Inhibitors of membrane transport (>0.1 mM) inhibited postphagocytic secretion of lysosomal beta-glucuronidase from dogfish phagocytes: phloretin > ethacrynate > furosemide > 4-acetamido-4'-isothiocyanostilbene-2,2'-disulfonic acid >> pyridoxal phosphate > ouabain. The same order of activity was found for inhibition by these agents of killing of Arbacia eggs by phagocytes. Cell activation (fertilization response) and cytotoxicity were quantitated both morphologically and by measurements of enzyme (beta-glucuronidase, catalase) release. The agents neither inhibited fertilization responses of eggs to calcium ionophore A23187 nor impaired their viability. Vital staining demonstrated that ethacrynate prevented phagocytes from degranulating upon contact with zymosan particles. The data not only suggest that agents primarily known for their capacity to inhibit membrane transport systems can inhibit lysosomal enzyme secretion from phagocytes but also support the hypothesis that secretion of lysosomal contents mediates activation and killing of target cells in phagocyte-mediated tissue injury.
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PMID:Inhibitors of membrane transport reduce lysosomal enzyme secretion from dogfish phagocytes and their killing of sea urchin eggs. 37 88

Chloramphenicol a potent inhibitor of bacterial and some mammalian cell protein synthesis, was administered i.p. to a group of mice for 6 consecutive days. Another group of animals was treated similarly with thiamphenicol and a third group served as control. The effects of the two antibiotics on the activity of some liver enzymes; the two pyridoxal 5-phosphate dependent enzymes, kynurenine hydrolase and kynurenine amino-transferase; pyridoxal phosphokinase; beta-glucuronidase and acid ribonuclease were determined. Chloramphenicol and thiamphenicol decreased significantly the activities of kynurenine hydrolase, beta-glucuronidase and acid ribonuclease and both drugs increased the activity of pyridoxal phosphokinase significantly. Their effect on kynurenine amino-transferase was different, chloramphenicol decreased while thiamphenicol increased the enzyme activity. Results are discussed and possible explanations suggested.
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PMID:In vivo effect of chloramphenicol and thiamphenicol on some enzymes of normal mouse liver. 705 51