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)

Little information is available on the effect produced by antiepileptic drugs on the serum beta-glucuronidase activity. According to recent findings, beta-glucuronidase serum levels are increased in patients with epilepsy just before the beginning of seizures and remain increased during several weeks; this it is suggested that determination of this enzyme could be important in the provision and the treatment of seizures. The purpose of the present study attempts to understand these changes. Our study was carried out on 49 adult healthy subjects and 48 adult epileptic patients receiving anticonvulsant therapies. Serum beta-glucuronidase activity was determined by a simplified procedure employing phenolphtalein glucuronic acid as substrate. The mean +/- SEM of serum beta-glucuronidase activity in treated patients (40.93 +/- 5.01 MSU/ml) was significantly higher than those of the healthy subjects (25.04 +/- 3.40 MSU/ml). In conclusion, the relationship between changes in serum enzyme activity, seizures and anticonvulsant therapies suggests that the determination of serum beta-glucuronidase activity presents a weak interest in predicting or treating seizures.
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PMID:[Serum beta-glucuronidase activity in patients with epilepsy]. 235 28

Human PMN release lysosomal enzymes (beta-glucuronidase, acid phosphatase) when exposed to immune complexes, but do not release cytoplasmic LDH. The cells remain viable, and failure of LDH to appear in supernatants is not due to selective absorption or inactivation. Release of enzymes is not due to platelet contamination and is only partially enhanced by fresh serum. The selective release of lysosomal enzymes after uptake of complexes resembles that induced by inert particles of zymosan, and can be distinguished from the concurrent release of all enzymes after cell death induced by membrane-lytic crystals of MSU. Uptake of complexes, zymosan, or MSU particles is accompanied by concomitant increases in C-1 oxidation of glucose. Although MSU-induced damage can be retarded by the presence of Tris buffer, immune complexes and zymosan selectively release lysosomal hydrolases in the presence or absence of Tris buffer. Agents which elevate the level, within cells, of cAMP (PGE(1), theophylline, 2-CA) and cAMP itself inhibit the selective extrusion of acid hydrolases from leukocytes without affecting the viability of cells. Leukocytes may respond to immune particles by regurgitating a portion of their lysosomal hydrolases during phagocytosis.
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PMID:Mechanisms of lysosomal enzyme release from leukocytes exposed to immune complexes and other particles. 1986 63