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 isolation of plasma membrane from human peripheral blood monocytes is described. Monocytes were isolated by centrifugal elutriation, to eliminate an adherence step, thus minimizing functional and surface antigenic alterations to the cells. Monocytes were surface-labelled with a radiolabelled monoclonal antibody, 125I-WVH-1, and then disrupted by nitrogen cavitation. Membranes were separated according to equilibrium buoyant density by isopycnic centrifugation on a sucrose gradient. The subcellular membranes were localized using marker enzymes for the plasma membrane, 5'-nucleotidase and leucine 2-naphthylamidase (leucine aminopeptidase), and for intracellular membranes: galactosyltransferase (Golgi), arylsulfatase C (endoplasmic reticulum), monoamine oxidase (mitochondria), catalase (peroxisomes), beta-hexosaminidase and beta-glucuronidase (lysosomal vesicles) and lactate dehydrogenase (cytosol). The monoclonal antibody 125I-WVH-1 was shown to label the plasma membrane, as judged by known markers, and represents a highly specific trace label, applicable to the use of plasma membrane as an immunogen for monoclonal antibody production. The NAD-splitting enzyme, NAD+ nucleosidase, was detected and its presence on the plasma membrane was demonstrated. The subcellular localization of non-specific esterase in human mononuclear phagocytes is controversial. No evidence was found for alpha-naphthyl acetate esterase activity on the plasma membrane or in lysosomal vesicles. However, a membrane-bound esterase in fractions with properties similar to the smooth endoplasmic reticulum was detected.
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PMID:Isolation of plasma membrane from human blood monocytes. Subcellular fractionation and marker distribution. 397 89

Inflammatory responses to carrageenin in streptozotocin-induced diabetic rats proved to be characterized by low values of granuloma tissue (tissue) weight and granuloma pouch fluid (fluid) volume, high values of fluid beta-glucuronidase (beta-Gl) and leucine aminopeptidase (LAP), and furthermore by high values of fluid lipid peroxide (LPO) and lactate dehydrogenase (LDH) and low values of fluid proamidase. These results in such diabetic rats were similar to those in rats injected with high doses of carrageenin except tissue weight and fluid volume. On the basis of measurements of three basic parameters required for coordinated observation of the inflammatory system, namely lysosomal enzymes, LPO, and proamidase (related respectively to the inflammatory response sensu stricto, to tissue damage, and to tissue repair), it can be concluded that the diabetic rats show an inadequately adapted inflammatory response, with decreased granuloma formation and reduced exudation, to noxious agents. This is probably due to a low sensitivity of the inflamed tissue in diabetic rats to noxious stimuli or chemical mediators, leading to a delay in the normal defence reaction of enhanced granuloma formation and exudation, thus resulting in a prolonged inflammatory response with a delay in wound healing.
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PMID:Streptozotocin diabetes: prolonged inflammatory response with delay in granuloma formation. 400 73

Levels of three enzymes, leucine aminopeptidase (LAP), N-acetyl-beta-D-glucosaminidase (NAG), and beta-glucuronidase (BGA) were measured in the urine of patients receiving hematologically toxic doses of iproplatin (a) with or (b) without pretreatment hydration. The maximum post-treatment increases in the levels of each of the enzymes were compared between these two groups of patients. In addition, the maximum increases in urinary enzyme levels in iproplatin-treated patients were compared with those in patients treated with 40 mg/m2 cisplatin, a known nephrotoxic agent. Increases in LAP levels after cisplatin treatment in the periods studied are significantly higher than those after iproplatin treatment (P less than 0.05). No differences were found in the increases in BGA and NAG levels between iproplatin treatment and cisplatin treatment. No differences were found in the increases in levels of any of the enzymes between patients receiving iproplatin with pretreatment hydration and no prior hydration.
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PMID:Evaluation of the nephrotoxicity of iproplatin (CHIP) in comparison to cisplatin by the measurement of urinary enzymes. 405 65

Neuronal and glial localization of brain peptidases was investigated by means of the kainic acid (KA) lesion technique. Activities of 6 different peptidases were measured in the rat caudate-putamen (CP) and substantia nigra (SN) 2, 7 and 21 days after unilateral intra-CP injection with 2.5 micrograms of KA. As an indicator of KA lesion in CP, substance P content in both CP and SN was also determined. In addition, activities of the same peptidases in the primary and secondary glial cell cultures of fetal rats were measured and compared to those in CP homogenate. After the KA injection, prolyl endopeptidase (Pro-EP) activity was decreased in the lesioned CP and, to a lesser extent, in the ipsilateral SN. The activity of angiotensin-converting enzyme (ACE) in the lesioned CP was decreased with a complex time course, whereas a slow and progressive reduction was observed in the SN. Alanyl and leucyl aminopeptidase (Ala-AP and Leu-AP respectively) activities gave only small changes after the lesion; Ala-AP was decreased and Leu-AP was increased in the lesioned CP, while both were decreased in the SN. Dipeptidyl aminopeptidase (DAP) and arginyl endopeptidase (Arg-EP) activities were increased 5-fold in the CP 7 days after the KA injection. Their increases paralleled that of beta-glucuronidase, the lysosomal marker enzyme. Cultured glial cells contained only a trace amount of ACE activity. Ala-AP and Pro-EP activities were considerably lower in the glial culture cells than in the CP homogenate. In contrast, DAP and Arg-EP as well as lysosomal marker enzymes showed much higher activity in the former than in the latter. These results suggest that (1) Ala-AP and Pro-EP have large neuronal components, (2) ACE is preferencially localized in neurons and (3) DAP and Arg-EP are associated with glial lysosomal function. It is, therefore, concluded that at least a part of the brain peptidases are differentially localized in neurons and glia, and may be involved in specific neuronal or glial function.
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PMID:Brain peptidases: their possible neuronal and glial localization. 608 24

Histochemical techniques have been applied to the identification of cell types cultured from human endometrium. Previous work from this laboratory characterized two principal cell types found in cultures of endometrium: a mature epithelial cell and another cell which was classified as the endometrial stromal cell based on light and electron microscopy. In this report we compare the histochemical staining of endometrial tissue in frozen sections to that of cultured cells. These results confirm the epithelial and stromal nature of the respective cell types. Several markers were found that could distinguish between cells of epithelial and stromal origin. The enzymes alkaline phosphatase, gamma-glutamyltranspeptidase, peroxidase, and beta-glucuronidase were localized in glandular and surface epithelia in frozen sections and in colonies of epithelial cells in culture. Stroma in frozen sections and cultured stromal cells contained leucine aminopeptidase and fibronectin. Epithelia in sections and in culture could also be distinguished from cells of stromal origin by preferential binding of lotus and peanut lectin. Several other markers were found in both endometrial epithelium and stroma.
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PMID:Histochemical identification of cultured cells from human endometrium. 614 95

In porcine interareolar placental epithelia, the following enzymes were demonstrated by histochemical methods after 30, 58, 80, 100, and 110 d of pregnancy, respectively: beta-N-acetylhexosaminidase, beta-galactosidase, beta-glucuronidase, alpha-mannosidase, acid phosphatase, alkaline phosphatase, nonspecific esterases, cytochrome oxidase, 5-nucleotidase, leucine aminopeptidase, adenosine triphosphatase, diaphorases (NADH, NADPH), glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, succinate dehydrogenase, isocitrate dehydrogenase (NAD, NADP), beta-hydroxybutyrate dehydrogenase, glycero-3-phosphate dehydrogenase, NAD-glycero-3-phosphate dehydrogenase, glutamate dehydrogenase (NAD, NADP), lactate dehydrogenase. The results show that most of the enzyme activities remained almost unchanged during the period of investigation. Only G-6-PDH and 6-PGDH activities increased within the uterine epithelium and nonspecific esterase activity within uterine as well as chorionic epithelia during the 2nd half of pregnancy. Within chorionic and uterine epithelia, hydrolases but not dehydrogenases demonstrated a higher activity at the bases of chorionic villi as compared to the apices and flanks of the latter. The action and influence of the demonstrated enzymes on metabolism, energy transfer, secretory, and resorptive activities of chorionic and uterine epithelia are discussed.
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PMID:[Enzyme histochemical studies of the swine placenta. Histoptics of enzymes in interareolar placental epithelia]. 643 35

Enzymatic characterization of 48 Aeromonas hydrophila complex isolates from various sources was determined with the API ZYM system (Analytab Products, Plainview, N.Y.). All isolates lacked valine and cystine aminopeptidases, chymotrypsin, alpha-mannosidase, alpha-fucosidase, alpha-galactosidase, and beta-glucuronidase but possessed caprylate esterase-lipase, leucine aminopeptidase, acid phosphatase, phosphoamidase, and N-acetyl-beta-glucosidase. Variability was found in the presence of alkaline phosphatase, butyrate esterase, myristate lipase, trypsin, beta-galactosidase, alpha-glucosidase, and beta-glucosidase. No significant differences were evident among the enzymatic profiles of isolates from various sources.
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PMID:Enzymatic characterization of Aeromonas hydrophila complex by the API ZYM system. 681 46

282 human prostatic fluid samples have been investigated for their pH value, zinc, and citrate concentration and their acid phosphatase, leucine aminopeptidase, diamine oxidase, and beta-glucuronidase activities. The results have been analysed in terms of the clinical status of the patients. Significant differences between patient categories were found with all but diamine oxidase and beta-glucuronidase. These differences were mainly found between men with apparently healthy prostates and prostatitis patients; the pH being raised and the acid phosphatase, leucine aminopeptidase, zinc and citrate being reduced. The diagnostic value of these parameters was evaluated, each could be used to classify correctly 90% of patients from these 2 groups. Zinc, citrate and leucine aminopeptidase showed no age relationship and were better than acid phosphatase and pH in discriminating between BPH and prostatitis. Evidence was also found for a return of normal secretory function sometime after an episode of prostatitis. Zinc and citrate are likely to be the most useful parameters for clinical evaluation.
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PMID:The response of seven prostatic fluid components to prostatic disease. 717 28

Synovial membrane obtained from the patients, in number of twenty one, suffering from the rheumatoid arthritis of classical type, was surveyed from the stand-point of enzyme histochemistry concentrating on lysosomal enzyme. Examined enzymes were leucine aminopeptidase, acid phosphatase and beta-glucuronidase. The activities of respective enzymes were compared with clinical and pathological activities of disease in each cases. It has been known that these lysosomal enzymes indicate high activity not only in chemical analysis of synovial membrane, but also histochemical observation. The origin of these enzymes, however, has not yet been determined as being derived of the synovial tissue or inflammatory cells. In the present investigation, it has been clarified that the enzyme activities were well localized at lining cell layer, but no activation of enzyme in the inflammatory cells in tissue. Therefore, it is suggested that lysosomal enzyme activity may be one of the factors which act on the destructive process in the rheumatoid arthritis.
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PMID:[Histochemical study of lysosomal enzymes in the synovial membrane of the rheumatoid arthritis (author's transl)]. 739 24

An epidemiologic study of Pasteurella haemolytica serovar 1 (Ph1) in market-stressed feeder calves from 7 farms in eastern Tennessee was conducted. The nasal mucus of each calf was cultured sequentially at the farm of origin (day 0), at an auction market (day 133), and at a feedyard in Texas (days 141, 148, 155, and 169). Of the 103 calves tested, 77 were culture-positive, including 1 on day 0, 1 on day 133, 20 on day 141, 57 on day 148, 50 on day 155, and 14 on day 169. From the 143 Ph1 isolates, 20 enzyme profiles were determined by use of a commercial enzyme system that detects 19 enzymatic reactions; 4 antimicrobial susceptibility profiles were obtained, using the disk-diffusion method, which evaluated susceptibility to 11 antibacterial drugs. All isolates were positive for acid phosphatase and alkaline phosphatase, but were negative for alpha-galactosidase, alpha-mannosidase, beta-glucosidase, beta-glucuronidase, cystine aminopeptidase, N-acetyl-beta-glucosaminidase, and trypsin. Other positive enzyme reactions included: leucine aminopeptidase, 140 Ph1 isolates; phosphohydrolase, 90 isolates; alpha-fucosidase, 63 isolates; esterase (C4), 59 isolates; valine aminopeptidase, 30 isolates; esterase lipase (C8), 24 isolates; beta-galactosidase, 2 isolates; and alpha-glucosidase, chymotrypsin and lipase (C14), 1 isolate each. Thirty-four Ph1 profiles were identified, using combined enzyme and antimicrobial susceptibility profiles. The data indicate that the strains isolated during the feedyard period may have been determined more by farm of origin (P < or = 0.001) than by habitation with calves from other farms while in the feedyard.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Identification of Pasteurella haemolytica A1 isolates from market-stressed feeder calves by use of enzyme and antimicrobial susceptibility profiles. 842 78


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