scholarly journals Characterization of brush borders purified in iso-osmotic medium and microvillar membranes subfractionated from mouse small intestine

1981 ◽  
Vol 196 (3) ◽  
pp. 669-673 ◽  
Author(s):  
M Fujita ◽  
H Ohta ◽  
T Uezato
Keyword(s):  
Alkaline Phosphatase ◽  
Brush Border ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gamma Glutamyl Transpeptidase ◽  
Electrophoretic Patterns ◽  
Mouse Small Intestine ◽  
Brush Borders ◽  
Typical Morphology ◽  
Glutamyl Transpeptidase

Brush borders free of nuclei were isolated by repeated homogenization and centrifugation in iso-osmotic medium. They showed typical morphology under electron microscopy. The mean recovery and enrichment of alkaline phosphatase activity in the brush-border fraction were 50% and 17.5-fold respectively. gamma-Glutamyl transpeptidase showed a close parallelism with alkaline phosphatase and sucrase in subcellular distribution. Microvillar membranes were purified from isolated brush borders; they showed a further enrichment for alkaline phosphatase and were composed of homogeneous vesicles. Both brush-border and microvillar-membrane preparations were analysed for contamination by basolateral and endoplasmic-reticular membranes. Sodium dodecyl sulphate/polyacrylamide-gel electrophoresis of the microvillar-membrane preparation in six different systems revealed approx. 40 components in the mol.wt. range 15 000-232 000. They were grouped into seven major classes on the basis of molecular weight and electrophoretic patterns.

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.

scholarly journals Developmental pattern of rat intestinal brush-border enzymic proteins along the villus–crypt axis

1979 ◽  
Vol 178 (2) ◽  
pp. 407-413 ◽  
Author(s):  
Patricia M. Simon ◽  
Michèle Kedinger ◽  
Francis Raul ◽  
Jacques F. Grenier ◽  
Katy Haffen
Keyword(s):  
Alkaline Phosphatase ◽  
Brush Border ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Protein Band ◽  
Band 3 ◽  
Developmental Pattern ◽  
Simultaneous Increase ◽  
Cell Compartments ◽  
Crypt Cells

At various postnatal stages, intestinal epithelial cells were isolated sequentially from villus tip to crypt base by successive EDTA treatments. According to the localization of marker enzymic activities, isolated cells were pooled into three cell compartments: villus (V), lower villus and upper crypt (VC) and crypt (C). Purified brush-border-membrane proteins were separated by 7.5%-polyacrylamide-gel electrophoresis in the presence of sodium dodecyl sulphate. Enzymic activities could be assigned to some protein bands: maltase/glucoamylase (protein band 3), sucrase–isomaltase (protein bands 3 and 6), lactase (protein band 5) and alkaline phosphatase (region of protein bands 8 and 9). The findings suggest the following. (1) Sucrase–isomaltase activities appeared in compartment C at 17 days with a simultaneous increase of the pre-existing protein band 3 and appearance of a well-defined protein band in position 6; the enzymic complex remained still present in the crypt cells until adulthood. From the day 21 onwards, sucrase–isomaltase was detected in compartments VC and V. (2) Lactase was only present in the three cell compartments until day 21; at this developmental stage its activity completely disappeared from compartment C, in spite of the persistence of a weak protein band. (3) Alkaline phosphatase activity could be detected as a single peak corresponding to protein band 9 in all three cell compartments until day 21; thereafter it was replaced by two peaks of activity showing a less precise correlation with the well-defined protein bands 8 and 9. In the crypt cells of the adult rat, however, the preweaning situation, which was regularly observed, is an unexpected phenomenon. (4) Maltase and glucoamylase did not display any marked qualitative or quantitative modifications either along the villus–crypt axis or during the period of postnatal development studied. Evidence is given from the present data that each brush-border enzyme investigated has a specific developmental pattern.

Regulation of brush-border enzyme activities and enterocyte migration rates in mouse small intestine

1992 ◽  
Vol 262 (6) ◽  
pp. G1047-G1059 ◽  
Author(s):  
R. P. Ferraris ◽  
S. A. Villenas ◽  
J. Diamond
Keyword(s):  
Cell Migration ◽  
Brush Border ◽  
Gamma Glutamyl Transpeptidase ◽  
Migration Rates ◽  
Protein Levels ◽  
Mouse Small Intestine ◽  
Rabbit Intestine ◽  
Brush Border Enzyme ◽  
Cell Fractions ◽  
Glutamyl Transpeptidase

We adapted the Weiser method, previously used to fractionate enterocytes of rat and rabbit intestine, to the much smaller intestine of mice. By histological, morphometric, enzymatic, histochemical, and immunocytochemical evidence, the method succeeded in removing mouse enterocytes sequentially along the crypt-villus axis while preserving cell viability and minimizing mixing among cell fractions. Activities of three brush-border enzymes [alkaline phosphatase (AP), sucrase, and gamma-glutamyl transpeptidase (GGP)] varied simultaneously with dietary substrate level, intestinal region, and position along the crypt-villus axis. All three enzymes proved to be stimulated by dietary substrate: sucrase by dietary sucrose, AP and GGP by dietary protein. We also studied cell migration rates and life-times by autoradiography and by our modified Weiser method. By both methods, injected [3H]thymidine after short times was virtually confined to crypt cells, whereas after 40-48 h it was distributed from the crypt over the whole villus except for the villus tip. Villus height decreased twofold from duodenum to ileum, parallel to the regional decrease in cell migration rates because the cell lifetime of 68 h was independent of region. When we varied dietary carbohydrate and protein levels reciprocally while maintaining protein above the maintenance level, both cell migration rate and cell lifetime proved independent of diet.

scholarly journals Some biological indicators relevant for the management of cholestasis in children

2015 ◽  
Vol 67 (4) ◽  
pp. 1421-1424
Author(s):  
Evelina Moraru ◽  
Ana Drochioi ◽  
Paula Popovici ◽  
Carmen Anton ◽  
Laura Bozomitu ◽  
...  
Keyword(s):  
Alkaline Phosphatase ◽  
Bile Flow ◽  
Serum Bilirubin ◽  
Biological Indicators ◽  
Aspartate Transaminase ◽  
Biological Parameters ◽  
Gamma Glutamyl Transpeptidase ◽  
Bile Formation ◽  
Diagnostic Protocol ◽  
Glutamyl Transpeptidase

Cholestasis is a multifactorial disorder with various biological, infectious, toxic, genetic and metabolic manifestations, its principal feature presented as reduced bile flow or abnormalities in bile formation. It has lately been accepted that some specific biological markers would shorten the period needed to establish a positive diagnosis, as currently it is necessary to navigate through a complex diagnostic protocol for this disorder. The purpose of this study was to establish some biological parameters and biomarkers useful for cholestasis management in children. Two hundred thirty-two children with cholestasis were selected, during a six-year study. The biological indicators followed were serum bilirubin, gamma-glutamyl transpeptidase, aspartate transaminase, alkaline phosphatase, lactate dehydrogenase, serum cholesterol and triglycerides. Our data showed that certain biological parameters are more often involved in the various forms of cholestasis, and the conclusions of this study could be useful in the early detection of cholestasis and appropriate disease management.

scholarly journals Assessment of liver enzymes in saliva and serum of Iraqi patients with chronic periodontitis disease

2020 ◽  
Vol 14 (1) ◽  
pp. 20-24
Author(s):  
Hussein SH. Ridha ◽  
Zahraa H.M. Kadri
Keyword(s):  
Alkaline Phosphatase ◽  
Chronic Periodontitis ◽  
Alanine Aminotransferase ◽  
Liver Enzymes ◽  
Serum Levels ◽  
Aspartate Transaminase ◽  
Gamma Glutamyl Transpeptidase ◽  
Serum Samples ◽  
Gamma Glutamyl ◽  
Glutamyl Transpeptidase

Objective: The present study aimed to assess of four liver enzymes, Alanine Aminotransferase (ALT), Aspartate Transaminase (AST), Alkaline Phosphatase (ALP) and Gamma-Glutamyl Transpeptidase (GGT). Material and Methods: Based on periodontal clinical parameters, sixty four patients with chronic periodontitis (CP) and twenty four controls were enrolled in the study. Saliva and serum samples were collected and Automated Chemistry Analyzer AU 480 was employed to assess levels of enzymes. Results: Compared to healthy controls, the levels of the four enzymes were significant increased in serum of patients, especially in the severe group while in the saliva a significant increase observed only in the level of AST. Moreover, Alanine Aminotransferase (ALT), Aspartate Transaminase (AST), Alkaline Phosphatase (ALP) and Gamma-Glutamyl Transpeptidase (GGT) the levels of these enzymes in serum were significantly higher than those in saliva. Conclusion: ALT, AST, ALP and GGT serum levels are suggested to be important indicators for disease progression as well as predict the liver health.  

Serum Gamma-Glutamyl Transpeptidase Activity as an Indicator of Disease of Liver, Pancreas, or Bone

1972 ◽  
Vol 18 (4) ◽  
pp. 358-362 ◽  
Author(s):  
Gifford Lum ◽  
S Raymond Gambino
Keyword(s):  
Alkaline Phosphatase ◽  
Liver Disease ◽  
Viral Hepatitis ◽  
Bone Disease ◽  
Leucine Aminopeptidase ◽  
Serum Alkaline Phosphatase ◽  
Metastatic Carcinoma ◽  
Gamma Glutamyl Transpeptidase ◽  
Serum Alkaline Phosphatase Activity ◽  
Glutamyl Transpeptidase

Abstract Serum γ-glutamyl transpeptidase (GGT), leucine aminopeptidase, alkaline phosphatase, alanine aminotransferase, and aspartate aminotransferase activities were assayed in controls and in patients with liver, pancreatic, or bone disease. GGT activity was above normal in all forms of liver disease studied (viral hepatitis, cirrhosis, cholecystitis, metastatic carcinoma to liver, pancreatic carcinoma, liver granuloma, and acute pancreatitis). GGT more sensitively indicated hepatic disease than did alkaline phosphatase, much more so than did leucine aminopeptidase. GGT was disproportionately more active in relation to the transaminases in cases of intraor extrahepatic biliary obstruction; the reverse was true in cases of viral hepatitis. GGT activity was normal in children, adolescents, and pregnant women, and in cases of bone disease and renal failure. Kinetic measurement of GGT activity offers a simple, sensitive, and direct means for distinguishing whether bone or liver is the source of increased serum alkaline phosphatase activity. Activity was highest in obstructive liver disease.

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