The Role of Gamma-Glutamyl Transpeptidase in Glutamine Metabolism by Cultured Human Kidney Cells1

2015 ◽  
pp. 191-199 ◽  
Author(s):  
Itzhak Nissim ◽  
Beatrice States ◽  
Ilana Nissim ◽  
Marc Yudkoff
Keyword(s):  
Human Kidney ◽  
Glutamine Metabolism ◽  
Gamma Glutamyl Transpeptidase ◽  
Gamma Glutamyl ◽  
Glutamyl Transpeptidase

Absence of a role of gamma-glutamyl transpeptidase in the transport of amino acids by rat renal brushborder membrane vesicles

1984 ◽  
Vol 80 (2) ◽  
pp. 167-173 ◽  
Author(s):  
Betty Y. L. Hsu ◽  
John W. Foreman ◽  
Susan M. Corcoran ◽  
Kristina Ginkinger ◽  
Stanton Segal
Keyword(s):  
Amino Acids ◽  
Membrane Vesicles ◽  
Gamma Glutamyl Transpeptidase ◽  
Gamma Glutamyl ◽  
Glutamyl Transpeptidase

scholarly journals A monoclonal antibody against human kidney gamma-glutamyl transpeptidase: preparation, immunochemical, and immunohistochemical characterization.

1989 ◽  
Vol 37 (7) ◽  
pp. 1053-1061 ◽  
Author(s):  
M Shiozawa ◽  
S Yamashita ◽  
S Aiso ◽  
K Yasuda
Keyword(s):  
Monoclonal Antibody ◽  
Immunohistochemical Study ◽  
Basolateral Membrane ◽  
Human Kidney ◽  
Normal Liver ◽  
Gamma Glutamyl Transpeptidase ◽  
Gamma Glutamyl ◽  
Human Organs ◽  
Human Enzyme ◽  
Glutamyl Transpeptidase

To perform immunohistochemical study of the distribution of gamma-glutamyl transpeptidase in human organs, a highly specific antibody against the human enzyme is required. We prepared monoclonal antibody against gamma-glutamyl transpeptidase from human kidney, using the hybridoma technique. The antibody was of the IgG1 type and the light chain belonged to the kappa class. The antibody reacted specifically with the 63 KD heavy subunit of the enzyme. Examination of the specificity of the antibody performed by immunohistochemical staining of human kidney sections revealed that the antigen was localized on the brush border and along the basolateral membrane of the epithelial cells of both the convoluted and the straight portions of the proximal tubule. This antibody was also reactive in several human organs other than kidney, including epididymis, prostate, seminal vesicle, pancreas, and normal liver, and in human hepatoma. These findings indicate the existence of an antigenic determinant common to human kidney and other organs. The monoclonal antibody did not crossreact with mouse, rat, guinea pig, rabbit, or pig kidney.

scholarly journals Studies on gamma-glutamyl transpeptidase in human and rabbit erythrocytes

Blood ◽  
1976 ◽  
Vol 47 (4) ◽  
pp. 645-650 ◽  
Author(s):  
SK Srivastava ◽  
YC Awasthi ◽  
SP Miller ◽  
A Yoshida ◽  
E Beutler
Keyword(s):  
Amino Acids ◽  
Human Kidney ◽  
Ringer Solution ◽  
Proximal Tubules ◽  
Red Cell ◽  
Gamma Glutamyl Transpeptidase ◽  
Gamma Glutamyl ◽  
Red Cell Membranes ◽  
Glutamyl Transpeptidase ◽  
Human Red Cells

Abstract Gamma-glutamyl transpeptidase transfers the gamma-glutamyl moiety of glutathione to a variety of acceptor amino acids. Through the operation of the gamma-glutamyl-cyclotransferase cycle, this enzyme has been implicated in the transport of amino acids into cells, especially the cells of the proximal tubules of kidney. It has been reported to be present in rabbit erythrocytes. However, using white cell-free preparations, we have not been able to demonstrate the presence of gamma-glutamyl transpeptidase in human or rabbit erythrocytes either by measuring the utilization of GSH or by following the formation of the product. 14C-L-methionine was used as acceptor amino acid, and the formation of gamma-glutamyl-14C-L-methionine was followed. Using similar conditions, we have been able to demonstrate the presence of gamma-glutamyl transpeptidase in human and rabbit leukocytes and in human kidney. In contrast to a previous report, we were unable to find the accumulation of 5-oxoproline, an intermediate of the gamma-glutamyl- cyclotransferase pathway in human red cells incubated in Krebs-Ringer solution. Immunologic studies demonstrated that human red cell membranes contained no protein antigenically similar to kidney gamma- glutamyl transpeptidase. Thus our studies indicated that in human and rabbit erythrocytes, the gamma-glutamyl transpeptidase-cyclotransferase pathway was not operative.

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