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)

A significant portion of murine hepatocyte beta-glucuronidase is maintained within the endoplasmic reticulum (ER) by complex formation with the esterase active site of the protein egasyn. The carboxyl-terminal propeptide of the precursor form of glucuronidase appears important in localization of glucuronidase to the ER since a naturally occurring mutation in it is associated with decreased levels of ER glucuronidase. A sequence similarity was noted between the carboxyl-terminal propeptide and portions of the conserved sequences of the reactive site region of members of the serpin (serine proteinase inhibitor) superfamily. Also, previous studies had shown that a synthetic peptide, corresponding to the propeptide region, was a specific and potent inhibitor of the esterase activity of purified egasyn. Taken together, these results suggest that (a) the egasyn-glucuronidase system may use a novel mechanism related to that of serine proteinases and their inhibitors in complex formation and in subsequent localization of glucuronidase within the ER and that (b) a possible function of ER glucuronidase is to modulate the esterase activity of egasyn.
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PMID:The propeptide of beta-glucuronidase. Further evidence of its involvement in compartmentalization of beta-glucuronidase and sequence similarity with portions of the reactive site region of the serpin superfamily. 239 91

We previously showed that two polymorphonuclear neutrophil (PMN)-derived proteinases, namely cathepsin G (Cat. G) and elastase (HLE), acting in synergy activated nearby platelets in vitro. This cellular interaction could result in a pathology such as the adult respiratory distress syndrome (ARDS). Since elevated levels of tumor necrosis factor-alpha (TNF-alpha) and interleukin-8 (IL-8) were detected in these patients and therefore could be involved in this disease, we looked for their effects in the PMN-platelet cooperation system. Addition of IL-8 to mixed suspensions of PMN and platelets induced weak but significant platelet aggregations. Upon preincubation with TNF-alpha, aggregations triggered by IL-8 were significantly increased. The targets of these cytokines were not the platelets but the PMNs. This was shown by following beta-glucuronidase release and more interestingly by measuring the enzymatic activities of Cat. G and HLE in the supernatant. Inhibition of the platelet response upon addition of a serine proteinase inhibitor, eglin C, clearly demonstrated the involvement of these two enzymes. Taken together, these results constitute an additional argument for the role of the PMN-platelet interaction in ARDS.
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PMID:Synergism between interleukin-8 and tumor necrosis factor-alpha for neutrophil-mediated platelet activation. 788 Sep 76

Transcription analysis of a mustard (Sinapis alba L.) serine proteinase inhibitor gene revealed identical 5' termini of mRNAs synthesized during seed maturation and chemical or wounding induction. Polyadenylation of mRNAs on multiple or single sites differentiated gene expression, increasing the availability of stable mRNAs during seed maturation compared with chemical and wounding induction. Expression of the beta-glucuronidase (GUS)-encoding region of the UidA reporter gene, detected under the control of deleted segments of the region flanking on the 5' side the mit-2 gene, identified a stretch of about 520 bp essential for gene expression. The presence in this region of two ABRE motifs is relevant for plant response to gene induction. Expression of GUS was detectable under different induction stimuli in several organs such as seedlings and leaves and was active to varying extents in the vascular tissues and meristem.
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PMID:Analysis of mustard trypsin inhibitor-2 gene expression in response to developmental or environmental induction. 1134 44