Different diuresis-dependent excretions of urinary enzymes: N-acetyl-beta-D-glucosaminidase, alanine aminopeptidase, alkaline phosphatase, and gamma-glutamyltransferase.

1986 ◽  
Vol 32 (3) ◽  
pp. 529-532 ◽  
Author(s):  
K Jung ◽  
G Schulze ◽  
C Reinholdt
Keyword(s):  
Alkaline Phosphatase ◽  
Brush Border ◽  
Excretion Rate ◽  
Urine Flow ◽  
High Intake ◽  
Brush Border Enzymes ◽  
Urinary Creatinine ◽  
Gamma Glutamyltransferase ◽  
Alanine Aminopeptidase ◽  
Brush Border Enzyme

Abstract We studied how much of the lysosomal enzyme N-acetyl-beta-D-glucosaminidase (EC 3.2.1.30) and of the brush-border enzymes alanine aminopeptidase (EC 3.4.11.2), alkaline phosphatase (EC 3.1.3.1), and gamma-glutamyltransferase (EC 2.3.2.2) was excreted in urine over 8 h after a high intake of fluid (22 mL per kilogram of body weight). The hourly excretion of all four enzymes increased with the increasing urine flow rate. The excretion rate of the brush-border enzymes was more markedly influenced than that of N-acetyl-beta-D-glucosaminidase. By relating the enzyme excretion to urinary creatinine we could reduce the variability of brush-border enzyme output and could completely compensate for the effect of diuresis on the excretion of N-acetyl-beta-D-glucosaminidase.

Electrophoretic variants of alanine aminopeptidase, alkaline phosphatase, and gamma-glutamyltransferase in urine.

1984 ◽  
Vol 30 (6) ◽  
pp. 856-859 ◽  
Author(s):  
K Jung ◽  
U W Wischke
Keyword(s):  
Alkaline Phosphatase ◽  
Electrophoretic Mobility ◽  
Brush Border ◽  
Neuraminidase Treatment ◽  
Electrophoretic Variants ◽  
Brush Border Enzymes ◽  
Gamma Glutamyltransferase ◽  
Electrophoretic Mobilities ◽  
Alanine Aminopeptidase ◽  
Triton X

Abstract The three brush-border enzymes--alanine aminopeptidase (EC 3.4.11.2), alkaline phosphatase (EC 3.1.3.1), and gamma-glutamyltransferase (EC 2.3.2.2)--are present in the urine of healthy persons in two variants, a particulate form and a soluble one. They can be separated by electrophoresis in agarose gel and by ultracentrifugation. The particulate forms exhibit similar electrophoretic mobility, but the soluble forms of these brush-border enzymes differ in their electrophoretic mobilities. The enzyme components of the particulate activity can be mobilized by Triton X-100 and trypsin. The electrophoretic mobility of the soluble forms of alanine aminopeptidase and gamma-glutamyltransferase is slowed by neuraminidase treatment. Both forms of gamma-glutamyltransferase are influenced in their electrophoretic mobility by treatment with n-butanol/diisopropyl ether, showing their lipid dependence. These findings enhance our knowledge of the biochemical nature of brush-border enzymes in urine.

Diagnostic significance of some urinary enzymes for detecting acute rejection crises in renal-transplant recipients: alanine aminopeptidase, alkaline phosphatase, gamma-glutamyltransferase, N-acetyl-beta-D-glucosaminidase, and lysozyme.

1986 ◽  
Vol 32 (10) ◽  
pp. 1807-1811 ◽  
Author(s):  
K Jung ◽  
J Diego ◽  
V Strobelt ◽  
D Scholz ◽  
G Schreiber
Keyword(s):  
Alkaline Phosphatase ◽  
Renal Transplant ◽  
Acute Rejection ◽  
Renal Transplant Recipients ◽  
Transplant Recipients ◽  
Urinary Enzymes ◽  
Gamma Glutamyltransferase ◽  
Alanine Aminopeptidase ◽  
Group A ◽  
Group B

Abstract We compared the diagnostic validity of five urinary enzymes--alanine aminopeptidase (EC 3.4.11.2), alkaline phosphatase (EC 3.1.3.1), gamma-glutamyltransferase (EC 2.3.2.2), N-acetyl-beta-D-glucosaminidase (EC 3.2.1.30), and lysozyme (EC 3.2.1.17)--as indicators of acute rejection crises in renal-transplant recipients. In 82 patients (group A), the excretion of each of these five enzymes was measured daily from transplantation until discharge from hospital. In another 69 patients (group B), enzyme determinations were made when the patient came for regular checkups (about every four to eight weeks). We used an "activity ratio" (the activity measured at a particular time compared with the activity on the preceding determination) value of 1.5 as the decision point. In group A, use of this discrimination point for alanine aminopeptidase, gamma-glutamyltransferase, and N-acetyl-beta-D-glucosaminidase yielded a specificity and sensitivity of about 90%. In group B, only alanine aminopeptidase had a greater diagnostic sensitivity than creatinine alone. Evidently, measurement of alanine aminopeptidase can be a helpful indicator of acute rejection crises, when interpreted in combination with other available relevant clinical, biochemical, and immunological data.

Pattern of rat intestinal brush-border enzyme gene expression changes with epithelial growth state

1995 ◽  
Vol 269 (2) ◽  
pp. C385-C391 ◽  
Author(s):  
R. A. Hodin ◽  
S. M. Chamberlain ◽  
S. Meng
Keyword(s):  
Gene Expression ◽  
Alkaline Phosphatase ◽  
Brush Border ◽  
Longitudinal Axis ◽  
Mrna Levels ◽  
Intestinal Alkaline Phosphatase ◽  
Enzyme Gene ◽  
Growth State ◽  
Brush Border Enzyme ◽  
Epithelial Growth

Enterocyte growth and differentiation occur simultaneously within the epithelium, but little is known regarding any relationship between these two processes. Four rat models of small intestinal epithelial hypo- and hyperplasia (neonatal ontogeny, fasting/refeeding, hypo-/hyperthyroidism, and bombesin treatment) were used to study the regulation of enterocyte gene expression in relation to epithelial growth state. Mucosal scrapings, as well as crypt and villus cell populations, were subjected to Northern blot analyses using radiolabeled cDNA probes corresponding to lactase, intestinal alkaline phosphatase, villin, ornithine decarboxylase (ODC), and the actin control. In all four models, the hypoplastic (atrophic) condition is characterized by high levels of lactase and low levels of the 3.0-kb intestinal alkaline phosphatase mRNA, whereas under hyperplastic conditions this pattern is reversed. The changes in intestinal alkaline phosphatase and lactase are qualitatively similar along the longitudinal axis of the intestine and are proportional to the degree of hyperplasia, as verified by ODC mRNA levels. Furthermore, the crypt-villus axis of differentiation is maintained regardless of epithelial growth state. In conclusion, the pattern of brush-border enzyme gene expression changes as a function of epithelial growth state, indicating a previously unrecognized degree of plasticity to the state of enterocyte differentiation.

Presence of γ-glutamyltransferase in the renal microvascular compartment

1981 ◽  
Vol 59 (6) ◽  
pp. 383-386 ◽  
Author(s):  
P. D. Dass ◽  
R. P. Misra ◽  
T. C. Welbourne
Keyword(s):  
Alkaline Phosphatase ◽  
Phosphatase Activity ◽  
Density Gradient ◽  
Alkaline Phosphatase Activity ◽  
Brush Border ◽  
Sucrose Density Gradient ◽  
Isolated Glomeruli ◽  
Crude Homogenate ◽  
Brush Border Enzyme ◽  
Enzyme Alkaline Phosphatase

The association between the brush border enzyme alkaline phosphatase and γ-glutamyltransferase was determined by sucrose density gradient analysis of crude kidney homogenates, isolated glomeruli, and isolated microvessels. As previously established there is an overlap of these enzyme activities in the crude homogenate corresponding to a density of 1.17 g∙cm−3. In contrast, isolated glomeruli sedimented with a peak of 1.25 g∙cm−3 and exhibited γ-glutamyltransferase activity but little alkaline phosphatase activity; homogenizing isolated glomeruli shifted the fragments to a density coincident with that observed for the crude homogenate γ-glutamyltransferase peak. A second population of capillaries, isolated microvessels, were homogenized and analyzed on the sucrose density gradient. These fragments sedimented over the same range as crude homogenate γ-glutamyltransferase peak but were devoid of alkaline phosphatase activity and yet exhibited remarkable γ-glutamyltransferase activity. The results indicate homogenization of renal cortex results in a heterogenous collection of particles from both tubular and microvascular locations exhibiting γ-glutamyltransferase activity which overlap with the brush border alkaline phosphatase containing membranes. However, isolation of microvessels and glomeruli prior to homogenization allows separation of γ-glutamyltransferase from alkaline phosphatase activity; between 10 and 20% of the total homogenate γ-glutamyltransferase activity is estimated to be associated with the microvascular compartment.

The Effects of Prednisolone on the Rat Enterocyte at a Subcellular Level

1978 ◽  
Vol 55 (5) ◽  
pp. 435-443
Author(s):  
R. M. Batt ◽  
G. Wells ◽  
T. J. Peters
Keyword(s):  
Brush Border ◽  
Brush Border Membrane ◽  
Equilibrium Density ◽  
Proximal Jejunum ◽  
Brush Border Enzymes ◽  
Brush Borders ◽  
Brush Border Enzyme ◽  
Mitochondrial Malate Dehydrogenase ◽  
Subcellular Level ◽  
Isopycnic Centrifugation

1. Enterocytes, isolated from the proximal jejunum and distal ileum of normal and prednisolone-treated rats, were homogenized and fractionated by isopycnic centrifugation on sucrose density gradients. The distributions of marker enzymes for the principal subcellular organelles, RNA and protein were determined and related to the activities per enterocyte. 2. In enterocytes from the jejunum and ileum of prednisolone-treated animals the activities of particulate brush-border enzymes and of both soluble and mitochondrial malate dehydrogenase were increased compared with those of the control system. The equilibrium density of the brush borders was enhanced in the prednisolone-treated jejunum. The modal densities of the other organelles were unaltered by prednisolone administration. 3. There was a large increase in the total RNA content of enterocytes from the jejunum and ileum of prednisolone-treated animals. This was predominantly associated with a distinct particulate component, indicative of a proliferation of the rough endoplasmic reticulum and consistent with an enhanced rate of protein synthesis. 4. Studies of latent brush-border enzyme activities, the mechanical fragility of isolated brush borders and electron microscopy suggest that steroid administration results in no marked alterations in the gross conformation of the brush- border membrane or in the orientation of the enzymes within the membrane.

Normal limits of urinary excretion of eleven enzymes.

1976 ◽  
Vol 22 (10) ◽  
pp. 1567-1574 ◽  
Author(s):  
D Maruhn ◽  
I Fuchs ◽  
G Mues ◽  
K D Bock
Keyword(s):  
Alkaline Phosphatase ◽  
Lactate Dehydrogenase ◽  
Urinary Excretion ◽  
Gel Filtration ◽  
Reference Intervals ◽  
Creatinine Concentration ◽  
Urinary Creatinine ◽  
Gamma Glutamyltransferase ◽  
Normal Limits ◽  
Alpha Glucosidase

Abstract Urinary excretion of lactate dehydrogenase, hydroxybutyrate dehydrogenase, gamma-glutamyltransferase, alkaline phosphatase, arylsulphatase A, alpha-glucosidase, beta-galactosidase, trehalase, N-acetyl-beta-glucosaminidase, beta-glucuronidase, and leucinearylamidase was studies in a carefully selected group of 100 healthy subjects, 50 women and 50 men. Enzyme activities were assayed in 3-h morning samples after gel filtration of the urine. Activities were related to time volume, and to urinary creatinine concentration. Several transforming functions had to be applied to enzyme output data to obtain an approximation to gaussian frequency distribution. Men showed a significantly higher excretion of gamma-glutamyltransferase, alpha-glucosidase, trehalase, N-acetyl-beta-glucosaminidase,beta-glucuronidase, and leucine arylamidase activity than did women if enzyme activity was related to urinary time volume. Women excreted more lactate dehydrogenase, hydroxybutyrate dehydrogenase, gamma-glutamyltransferase, alkaline phosphatase, alpha-glucosidase, trehalase, and N-acetyl-beta-glucosaminidase activity than did men, if urinary creatinine was used as the basis of reference. Reference intervals were calculated as 2.5 and 97.5 percentiles for both sexes.

scholarly journals Plasma lipopolysaccharide level and enterocyte brush border enzymes in gnotobiotic piglets infected with Salmonella typhimurium

2012 ◽  
Vol 47 (No. 10 - 11) ◽  
pp. 289-294
Author(s):  
I. Trebichavský ◽  
H. Kozáková ◽  
IŠplíchal
Keyword(s):  
Alkaline Phosphatase ◽  
Brush Border ◽  
Virulent Strain ◽  
Systemic Infection ◽  
Gamma Glutamyl Transpeptidase ◽  
Brush Border Enzymes ◽  
Dipeptidylpeptidase Iv ◽  
Glutamyl Transpeptidase ◽  
Rough Mutant ◽  
Gnotobiotic Piglets

Gnotobiotic piglets were orally infected either with the virulent LT2 strain or the non-pathogenic SF1591 rough mutant of Salmonella enterica serotype Typhimurium. They were sacrificed 6 or 24 h after the infection. All piglets infected for 24 h developed systemic infection with an increase of plasma lipopolysaccharide. Infection with the virulent strain caused a significant decrease (P < 0.001) of gamma-glutamyl transpeptidase (GGT) activity in the enterocyte brush border of both the jejunum and ileum, infection with the rough mutant caused a decrease of GGT activity in the ileum only. The activities of other brush border enzymes (lactase, sucrase, glucoamylase, alkaline phosphatase and dipeptidylpeptidase IV) did not change significantly after infection.

Effects of genetic strain and holding facility on the characteristics of alkaline phosphatase and brush border enzymes in silver perch (Bidyanus bidyanus)

2007 ◽  
Vol 38 (4) ◽  
pp. 361-372 ◽  
Author(s):  
Yaniv Hakim ◽  
Stuart J Rowland ◽  
Jeff A Guy ◽  
Charles Mifsud ◽  
Zehava Uni ◽  
...  
Keyword(s):  
Alkaline Phosphatase ◽  
Brush Border ◽  
Brush Border Enzymes ◽  
Genetic Strain

scholarly journals Evaluation of Met-Val-Lys as a Renal Brush Border Enzyme-Cleavable Linker to Reduce Kidney Uptake of 68Ga-Labeled DOTA-Conjugated Peptides and Peptidomimetics

Molecules ◽  
2020 ◽  
Vol 25 (17) ◽  
pp. 3854 ◽  
Author(s):  
Shreya Bendre ◽  
Zhengxing Zhang ◽  
Hsiou-Ting Kuo ◽  
Julie Rousseau ◽  
Chengcheng Zhang ◽  
...  
Keyword(s):  
Brush Border ◽  
Ex Vivo ◽  
Neutral Endopeptidase ◽  
Amide Bond ◽  
Detection Sensitivity ◽  
Brush Border Enzymes ◽  
Positron Emission ◽  
Brush Border Enzyme ◽  
Renal Brush Border

High kidney uptake is a common feature of peptide-based radiopharmaceuticals, leading to reduced detection sensitivity for lesions adjacent to kidneys and lower maximum tolerated therapeutic dose. In this study, we evaluated if the Met-Val-Lys (MVK) linker could be used to lower kidney uptake of 68Ga-labeled DOTA-conjugated peptides and peptidomimetics. A model compound, [68Ga]Ga-DOTA-AmBz-MVK(Ac)-OH (AmBz: aminomethylbenzoyl), and its derivative, [68Ga]Ga-DOTA-AmBz-MVK(HTK01166)-OH, coupled with the PSMA (prostate-specific membrane antigen)-targeting motif of the previously reported HTK01166 were synthesized and evaluated to determine if they could be recognized and cleaved by the renal brush border enzymes. Additionally, positron emission tomography (PET) imaging, ex vivo biodistribution and in vivo stability studies were conducted in mice to evaluate their pharmacokinetics. [68Ga]Ga-DOTA-AmBz-MVK(Ac)-OH was effectively cleaved specifically by neutral endopeptidase (NEP) of renal brush border enzymes at the Met-Val amide bond, and the radio-metabolite [68Ga]Ga-DOTA-AmBz-Met-OH was rapidly excreted via the renal pathway with minimal kidney retention. [68Ga]Ga-DOTA-AmBz-MVK(HTK01166)-OH retained its PSMA-targeting capability and was also cleaved by NEP, although less effectively when compared to [68Ga]Ga-DOTA-AmBz-MVK(Ac)-OH. The kidney uptake of [68Ga]Ga-DOTA-AmBz-MVK(HTK01166)-OH was 30% less compared to that of [68Ga]Ga-HTK01166. Our data demonstrated that derivatives of [68Ga]Ga-DOTA-AmBz-MVK-OH can be cleaved specifically by NEP, and therefore, MVK can be a promising cleavable linker for use to reduce kidney uptake of radiolabeled DOTA-conjugated peptides and peptidomimetics.

Biochemical and ultrastructural investigation of the effect of Stelazine (trifluoperazine) on Hymenolepis diminuta (Cestoda)

Parasitology ◽  
1987 ◽  
Vol 94 (1) ◽  
pp. 135-149 ◽  
Author(s):  
Jayne B. Hipkiss ◽  
A. Skinner ◽  
C. J. Branford White
Keyword(s):  
Alkaline Phosphatase ◽  
Connective Tissue ◽  
Brush Border ◽  
Incubation Medium ◽  
Hymenolepis Diminuta ◽  
Minimal Effect ◽  
Cellular Organization ◽  
Brush Border Enzymes ◽  
Ultrastructural Appearance

SUMMARYThe effects of the phenothiazine, Stelazine, on Hymenolepis diminuta were investigated. The cestode was incubated for 10 min at 37 °C with 1 mM trifluoperazine, in the presence and absence of Ca2+. Assay of brush border enzymes showed that drug treatment lowered the activities of alkaline phosphatase, Ca2+-ATP'ase, 5′-nucleotidase and type 1 phosphodiesterase. This occurred in parallel with a significant reduction in tegumental protein. Under these conditions gross changes in ultrastructural appearance and cellular organization were observed. There was a lack of ordered microtriches and the distal cytoplasm was absent. Glycogen granules were scattered throughout the cytoplasm within the subtegumental layer. The connective tissue also appeared to be in some disarray. The effects of Stelazine appeared to be dependent on time and were significantly increased when Ca2+ was included in the incubation medium. Incubation with the less hydrophobic phenothiazine trifluoperazine sulphoxide had minimal effect on the integrity of the cestode. The results reported here support the premise that certain phenothiazines may be considered as potential cestocidal agents.

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