scholarly journals Monoclonal antibodies against rat kidney γ-glutamyl transpeptidase show species and tissue specificity

1986 ◽  
Vol 238 (3) ◽  
pp. 913-917 ◽  
Author(s):  
J A Green ◽  
N D Cook ◽  
M M Manson
Keyword(s):  
Monoclonal Antibodies ◽  
Brush Border ◽  
Tissue Specificity ◽  
Rat Kidney ◽  
Gamma Glutamyl Transpeptidase ◽  
Brush Border Membranes ◽  
Adult Rat ◽  
Foetal Rat ◽  
Epithelial Tumours ◽  
Glutamyl Transpeptidase

Monoclonal antibodies have been raised against rat kidney gamma-glutamyl transpeptidase (GGT). All five antibodies immunoprecipitate enzyme activity from solubilized kidney brush-border membranes, but not from hepatocellular carcinoma membranes. Three of the antibodies react immunohistochemically with brush-border membranes in sections of adult rat kidney, but none of the antibodies cross-react with sections of guinea-pig, mouse or marmoset kidney or with untreated or carcinogen-treated rat liver. The antibodies do not recognize GGT in foetal-rat kidney and react poorly with kidney from 2-year-old rat. They do react with tubules trapped within mesenchymal kidney tumours induced by dimethylnitrosamine, but epithelial tumours, which are GGT-positive (although much less so than normal kidney), are not immunoreactive.

Inhibition of the hydrolytic and transpeptidase activities of rat kidney gamma-glutamyl transpeptidase by specific monoclonal antibodies

1999 ◽  
Vol 260 (3) ◽  
pp. 844-854 ◽  
Author(s):  
Evgenia Bluvshtein ◽  
George A. Glass ◽  
Gloria Volohonsky ◽  
Margalit Yaakubowitz ◽  
Ella Harness ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Rat Kidney ◽  
Gamma Glutamyl Transpeptidase ◽  
Gamma Glutamyl ◽  
Glutamyl Transpeptidase

scholarly journals Tissue- and developmental-stage-specific methylation in the two kidney promoters of the rat γ-glutamyl transpeptidase gene

1992 ◽  
Vol 287 (3) ◽  
pp. 691-694 ◽  
Author(s):  
J H Baik ◽  
S Siegrist ◽  
G Giuili ◽  
O Lahuna ◽  
F Bulle ◽  
...  
Keyword(s):  
Dna Methylation ◽  
Developmental Stage ◽  
Rat Liver ◽  
Kidney Development ◽  
Rat Kidney ◽  
Liver Development ◽  
Gamma Glutamyl Transpeptidase ◽  
Site Specific ◽  
Adult Rat ◽  
Glutamyl Transpeptidase

We have investigated, using DNA methylation patterning, the site-specific methylation of promoters I and II of the rat gamma-glutamyl transpeptidase gene. This analysis was done in fetal, newborn and adult rat kidney, in which promoters I and II are progressively active during development, as well as in rat liver, which never expresses mRNAs from these two promoters. During kidney development, a progressive demethylation occurs in the promoter I and II region, specially at the level of the most proximal MspI site of promoter II. A progressive reorganization of the methylated sites within the 5′ end of the gene also occurs during liver development.

Enzymatic and transport characteristics of isolated snake renal brush-border membranes

1988 ◽  
Vol 255 (1) ◽  
pp. R52-R60 ◽  
Author(s):  
S. Benyajati ◽  
W. H. Dantzler
Keyword(s):  
Brush Border ◽  
Transport Systems ◽  
Disulfonic Acid ◽  
Thamnophis Sirtalis ◽  
Organic Solutes ◽  
Gamma Glutamyl Transpeptidase ◽  
Brush Border Membranes ◽  
Brush Border Enzyme ◽  
Glutamyl Transpeptidase ◽  
Filtration Technique

Brush-border membranes (BBM) of proximal tubules were isolated from the kidney of the garter snake (Thamnophis sirtalis) by a procedure involving hypotonic lysis, Ca precipitation, and differential centrifugation. The isolated membranes were enriched 15-fold in brush-border enzyme activities (alkaline phosphatase, gamma-glutamyl transpeptidase) compared with whole kidney homogenates and were substantially free of other contaminating membranes. The yield of the BBM preparation was 40%. The BBM vesicular transport of several organic solutes was characterized by a rapid filtration technique at 25 degrees C. D-glucose, p-aminohippurate (PAH), and urate entered the same osmotically active space (2-3 microliter/mg protein) and binding was minimal (less than 20% for PAH). An uptake overshoot for 3-O-methyl-D-glucose (20 microM) by reptilian BBM was observed only in the presence of an inwardly directed NaCl gradient and was abolished by 0.1 mM phlorizin. Reptilian BBM exhibited Na-gradient-stimulated uptake of PAH (90 microM) with an overshoot that was inhibited by other organic acids and by 4-acetamido-4'-isothiocyanostilbene-2, 2'-disulfonic acid (SITS). In contrast, urate uptake (30 microM) appeared to be Na independent and not appreciably affected by other organic anions or SITS. The presence of specific transport systems for organic solutes in the isolated membrane preparation distinctly characterizes the BBM of reptilian kidney.

Protein-lipid interactions in human small intestinal brush-border membranes

1989 ◽  
Vol 257 (5) ◽  
pp. G809-G817
Author(s):  
P. K. Dudeja ◽  
J. M. Harig ◽  
K. Ramaswamy ◽  
T. A. Brasitus
Keyword(s):  
Lipid Composition ◽  
Brush Border ◽  
Gamma Glutamyl Transpeptidase ◽  
Lipid Interactions ◽  
Gamma Glutamyl ◽  
Brush Border Membranes ◽  
Lipid Fluidity ◽  
Intestinal Brush Border ◽  
Small Intestinal ◽  
Glutamyl Transpeptidase

Brush-border membranes prepared from proximal and distal human small intestine were characterized with respect to lipid fluidity, lipid composition, and protein-lipid interactions. Steady-state fluorescence polarization and differential polarized phase fluorometry revealed that the "static" and "dynamic" rotational components of fluidity (assessed by r infinity values of 1,6-diphenyl-1,3,5-hexatriene and r values of 12-anthroylstearate, respectively) were greater in the distal membranes compared with their proximal counterparts. The lipid fluidity of distal brush-border membranes was also greater as measured by excimer/monomer fluorescence ratio intensities of pyrene decanoate. A lower molar ratio of cholesterol/phospholipid in the distal membranes was responsible for these regional fluidity differences. Lipid thermotropic transitions were detected at 26-28 degrees C using 1,6-diphenyl-1,3,5-hexatriene in proximal and distal membranes. Arrhenius plots of p-nitrophenylphosphatase and gamma-glutamyl transpeptidase activities demonstrated breakpoints in the vicinity of the lipid thermotropic transition temperatures (28-30 degrees C), whereas maltase and sucrase yielded a single activity slope over the range of 10-40 degrees C. Moreover, 50 mM benzyl alcohol fluidized proximal brush-border membranes and increased p-nitrophenylphosphatase activity in this membrane. This agent also shifted the phase transition temperature of the membrane and breakpoint temperature of this enzymatic activity from approximately 28 degrees C to 19 degrees C. These findings demonstrate that differences in human small intestinal brush-border membrane lipid fluidity and lipid composition exist between proximal and distal regions of this organ. Furthermore, alterations in fluidity and/or lipid composition modulate p-nitrophenylphosphatase and gamma-glutamyl transpeptidase but not sucrase or maltase activities in these membranes.

Binding of lysozyme to brush border membranes of rat kidney

1983 ◽  
Vol 732 (2) ◽  
pp. 372-376 ◽  
Author(s):  
Gabriele Beyer ◽  
Folkert Bode ◽  
Karl Baumann
Keyword(s):  
Brush Border ◽  
Rat Kidney ◽  
Brush Border Membranes

The binding and degradation of insulin by brush-border membranes from rat kidney

1982 ◽  
Vol 10 (4) ◽  
pp. 220-220
Author(s):  
J. HYWEL THOMAS ◽  
PHILIP G. DAVEY ◽  
CHRISTOPHER D. G. JENKINS ◽  
DESPINA K. PAPACHRISTODOULOU
Keyword(s):  
Brush Border ◽  
Rat Kidney ◽  
Brush Border Membranes
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