Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.2.1.31 (beta-glucuronidase)
7,680 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The activities and subcellular distribution of the following enzymes: NADH oxidase, alkaline phosphatase, beta-glucuronidase and ATPase, were assayed in human mononuclear and polymorphonuclear leucocytes and in particular the contamination and integrity of the mitochondrial fractions were evaluated with this new separation procedure. Results show that maximal contamination was found to be that from lysosomal beta-glucuronidase especially in polymorphonuclear leucocyte mitochondria fractions. Furthermore oligomycin-sensitive ATPase data suggest that mitochondria do not decrease in number or lose their integrity to a great extent. Controversial p-nitrophenyl-phosphatase activity was also found to be present in polymorphonuclear and mononuclear leucocytes granular-soluble fractions.
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PMID:Subcellular distribution of some specific enzymatic activities in human leucocytes. 644 64

Sheets or sections of mouse epidermis reacted by a histochemical method for the enzyme beta-glucuronidase display a subpopulation of dendritic cells which correspond in number and spacing to Langerhans cells demonstrated by reactivity for ATPase or Ia antigens. A similar staining pattern is seen in rat, rabbit, and guinea pig epidermis. In rhesus monkey and human skin, Langerhans cells appear to be reactive for beta-glucuronidase but, as keratinocytes are also reactive, Langerhans cells are not readily identifiable by this method. The thermal stability of beta-glucuronidase differs between strains of mice. Langerhans cells of Balb/C and C3H strains can thus be distinguished by appropriate pretreatment before incubation, a method of potential value for experimental investigations of the origin of Langerhans cells.
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PMID:Reactivity of epidermal Langerhans cells to a histochemical method for demonstration of beta-glucuronidase. 646 65

Histochemical techniques have been used to study the chemical composition of the oesophageal gland secretions of Orthocoelium scoliocoelium and Paramphistomum cervi. Results suggest that the secretions contain numerous enzymes, e.g., non-specific alkaline and acid phosphatases, ATPase, TPPase, esterase (Cathepsin C like), beta-galactosidase, beta-glucuronidase and N-acetyl-beta-glucosaminidase. The role of these enzymes in the digestion of food in these amphistomes is discussed. On the basis of histological and histochemical studies the caecal epithelium of the two amphistomes has been found to be syncytial bearing regularly arranged numerous, long but equal-sized and closely packed cylindrical microvilli. The role of various hydrolytic enzymes in well fed and starved flukes in relation to their gastrodermis and microvilli has also been discussed.
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PMID:Role of oesophageal glands in the digestive physiology of two rumen amphistomes Orthocoelium scoliocoelium and Paramphistomum cervi. 684 57

In this study, we have used a mouse monoclonal antibody to rat Ia (RT1-B or class II) antigens to demonstrate, by immunofluorescence on frozen sections, intensely Ia-positive dendritic cells in the interstitial connective tissues of every tissue we have examined (heart, liver, thyroid, pancreas, skin, kidney, ureter, and bladder) with the striking exception of brain. The characteristics of the interstitial dendritic cell found in heart were studied in detail, and this cell was shown to be negative for acid phosphatase, beta-glucuronidase, and ATPase activity, and certainly some and probably all of the cells were negative for nonspecific esterase activity. Experiments with colloidal carbon suggested that the cell was either poorly or not at all phagocytic. The cells were negative for surface immunoglobulin and the W3/13 antigen, but positive for the leukocyte common antigen and the SD (Class I) antigens of the major histocompatibility complex. The cell was shown to be of bone marrow origin, and either the cell itself, or more probably its precursor, was shown to be sensitive to irradiation and to cyclophosphamide. All strains tested--including the nude rat--had large numbers of interstitial dendritic cells. The widespread distribution, except in brain, of this cell, which resembles in every respect the dendritic cell described by Steinman et al. (4) in the spleen and lymph nodes of the mouse, is of interest, and the implications in this finding are discussed.
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PMID:Demonstration and characterization of Ia-positive dendritic cells in the interstitial connective tissues of rat heart and other tissues, but not brain. 694 85

Eight compounds representing three classes of chemicals were evaluated for their toxic effects on normal neonatal human foreskin fibroblasts in vitro. A battery of toxicity assays was employed to measure the effects of the chemicals on cell viability, DNA synthesis, protein synthesis, DNA repair synthesis, cell ultrastructure, membrane-bound and soluble cytoplasmic proteins, and the activities of six enzymes: beta-glucuronidase, acid phosphatase, gamma-glutamyl transpeptidase, alkaline phosphatase, 5'mononucleotidase, and calcium-magnesium activated (Na+,K+)-dependent ATPase. The compounds evaluated included two antibiotics, each with a metabolic derivative-sulfamethazine (SMZ) and acetylsulfamethazine (ASZ), and carbadox (CBX) and desoxycarbadox (DCX); two anthelmintics-haloxon (HAL) and sansalid (SAN); and a steroid with a metabolic derivative, 17 alpha-estradiol (17-AE) and 17 alpha-estradiol-17-beta-D-glucoside (AE-G). Compounds with similar biological functions often elicited different patterns of response in the normal fibroblasts. For example, the two anthelmintics, HAL and SAN, were similar to each other in that they induced 50% relative cloning efficiencies (EC50) at approximately the same concentrations (HAL = 52 microgram/ml, SAN = 58 microgram/ml), and neither inhibited protein synthesis. They differed, however, in their effects of DNA synthesis. SAN did not inhibit DAN synthesis, while HAL was a profound inhibitor of DNA synthesis (98% inhibition after 4 h at 100 microgram/ml). Because the various toxicants elicited such a variety of response patterns as measured by a multiplicity of parameters, we conclude that similarities in survival responses of cells to closely related toxicants may arise frequently through toxic action at different sites within the cells.
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PMID:Multiparametric evaluation of the toxic responses of normal human cells treated in vitro with different classes of environmental toxicants. 713 84

The Arabidopsis thaliana (L.) Heynh. SUC2 gene encodes a plasma-membrane sucrose-H+ symporter. The DNA sequence of the SUC2 promoter has been determined. Using a translational fusion of this promoter to the N-terminus of beta-glucuronidase (GUS) and the GUS histochemical assay, the tissue specificity of the SUC2 promoter was studied in Arabidopsis plants transformed with this fusion construct. The SUC2 promoter directed expression of GUS activity with high specificity to the phloem of all green tissues of Arabidopsis such as rosette leaves, stems, and sepals. During leaf development the expression of SUC2-GUS activity was first seen in the tips of young rosette leaves. In older leaves and during their concomitant sink/source transition, expression proceeded from the tips to the bases of the leaves, indicating that expression of the SUC2 sucrose-H+ symporter is tightly coupled to the source-strength of Arabidopsis leaves. Expression of SUC2-GUS activity was also seen, however, in sink tissues such as roots and developing Arabidopsis pods, suggesting that the product of the SUC2 gene might not only be important for phloem loading, but also for phloem unloading. A possible regulatory effect of carbohydrates (glucose and sucrose) on the activity of the SUC2 promoter was studied and excluded, both in excised leaves and young seedlings of transgenic Arabidopsis plants. The overall pattern of SUC2-GUS expression correlated well with that of the Arabidopsis thaliana AHA3 plasma-membrane H(+)-ATPase which is also expressed in the phloem and most likely represents the primary pump generating the energy for secondary active transporters such as SUC2.
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PMID:The promoter of the Arabidopsis thaliana SUC2 sucrose-H+ symporter gene directs expression of beta-glucuronidase to the phloem: evidence for phloem loading and unloading by SUC2. 764 85

The plasma membrane H(+)-ATPases in Arabidopsis thaliana represent the largest family of cation translocating P-type ATPases identified in plants or animals. We report here seven new isoforms, which were identified by polymerase chain reaction (PCR) amplification of genomic DNA. Amplifications were performed with degenerate primers corresponding to two short conserved sequence motifs ("CSDK" and "GDGV") found in most P-type ATPases. A comparison was made of three CSDK-side primers, which were used either as totally degenerate mixtures or rendered less degenerate by substitution with deoxyinosine or fluorodeoxyuridine. Amplified genomic fragments were cloned, partially sequenced and shown to correspond to Arabidopsis genes by Southern blot analysis with gene-specific probes. One newly identified isoform, AHA10, was isolated as a cosmid clone and sequenced. The 5' and 3' ends of the gene were determined by comparison with the AHA10 cDNA sequence. AHA10 is the most divergent isoform characterized in the Arabidopsis family. AHA10 appears to be expressed primarily in developing seeds, as indicated by Northern blot analysis of AHA10 mRNA and by the analysis of transgenic plants expressing a beta-glucuronidase (GUS) reporter gene fused to an AHA10 promoter. Our results indicate that one function of this unusually large H(+)-ATPase gene family is to allow for expression of different isoforms in different cell types.
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PMID:The plasma membrane H(+)-ATPase gene family in Arabidopsis: genomic sequence of AHA10 which is expressed primarily in developing seeds. 796 26

A proton-pumping ATPase is present in the plasma membrane of plant cells where it sustains transport-related functions. This enzyme is encoded by a family of genes that shows signs of both transcriptional and post-transcriptional regulation. The regulation of pma1, one of the Nicotiana plumbaginifolia H+-ATPase genes, was characterized with the help of the beta-glucuronidase (gusA) receptor gene in transgenic plants. pma1 is active in the root epidermis, the stem cortex, and guard cells. This activity depends on developmental and growth conditions. For instance, pma1 activity in guard cells was strongly enhanced when the plant material (young seedlings or mature leaves) was incubated in liquid growth medium. pma1 is also expressed in several tissues of the reproductive organs where active transport is thought to occur but where scarcely any ATPase activity has been identified, namely in the tapetum, the pollen, the transmitting tissue, and the ovules. Several pma genes have a long 5'untranslated region (leader sequence) containing an upstream open reading frame (URF). Analysis of translational and transcriptional fusions with gusA in transgenic plants suggests that the pma1 leader sequence might activate translation of the main open reading frame, even though the URF is translated by a large majority of the scanning ribosomes. As confirmation, transient expression experiments showed that the pma1 leader causes a fourfold post-transcriptional increase of main open reading frame expression. Deletion of the URF by site-directed mutagenesis stimulated the main open reading frame translation 2.7-fold in an in vitro translational assay. These results are consistent with a regulatory mechanism involving translation reinitiation. Altogether, they suggest a fine, multilevel regulation of H+-ATPase activity in the plant.
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PMID:A plant plasma membrane proton-ATPase gene is regulated by development and environment and shows signs of a translational regulation. 799 72

The mitochondrial F1-ATPase beta subunit (ATPase-beta) of Nicotiana plumbaginifolia is nucleus-encoded as a precursor containing an NH2-terminal extension. By sequencing the mature N. tabacum ATPase-beta, we determined the length of the presequence, viz. 54 residues. To define the essential regions of this presequence, we produced a series of 3' deletions in the sequence coding for the 90 NH2-terminal residues of ATPase-beta. The truncated sequences were fused with the chloramphenicol acetyl transferase (cat) and beta-glucuronidase (gus) genes and introduced into tobacco plants. From the observed distribution of CAT and GUS activity in the plant cells, we conclude that the first 23 amino-acid residues of ATPase-beta remain capable of specifically targeting reporter proteins into mitochondria. Immunodetection in transgenic plants and in vitro import experiments with various CAT fusion proteins show that the precursors are processed at the expected cleavage site but also at a cryptic site located in the linker region between the presequence and the first methionine of native CAT.
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PMID:Truncated presequences of mitochondrial F1-ATPase beta subunit from Nicotiana plumbaginifolia transport CAT and GUS proteins into mitochondria of transgenic tobacco. 815 82

More than 11 different P-type H(+)-ATPases have been identified in Arabidopsis by DNA cloning. The subcellular localization for individual members of this proton pump family has not been previously determined. We show by membrane fractionation and immunocytology that a subfamily of immunologically related P-type H(+)-ATPases, including isoforms AHA2 and AHA3, are primarily localized to the plasma membrane. To verify that AHA2 and AHA3 are both targeted to the plasma membrane, we added epitope tags to their C-terminal ends and expressed them in transgenic plants. Both tagged isoforms localized to the plasma membrane, as indicated by aqueous two-phase partitioning and sucrose density gradients. In contrast, a truncated AHA2 (residues 1-193) did not, indicating that the first two transmembrane domains alone are not sufficient for plasma membrane localization. Two epitope tags were evaluated: c-myc, a short, 11-amino acid sequence, and beta-glucuronidase (GUS), a 68-kD protein. The c-myc tag is recommended for its sensitivity and specific immunodetection. GUS worked well as an epitope tag when transgenes were expressed at relatively high levels (e.g. with AHA2-GUS944); however, evidence suggests that GUS activity may be inhibited when a GUS domain is tethered to an H(+)-ATPase complex. Nevertheless, the apparent ability to localize a GUS protein to the plasma membrane indicates that a P-type H(+)-ATPase can be used as a delivery vehicle to target large, soluble proteins to the plasma membrane.
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PMID:Targeting of two Arabidopsis H(+)-ATPase isoforms to the plasma membrane. 888 93


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