scholarly journals Distribution of gamma-glutamyl transpeptidase in human pancreas: immunohistochemical study with a monoclonal antibody.

1990 ◽  
Vol 38 (3) ◽  
pp. 339-350 ◽  
Author(s):  
K Yasuda ◽  
M Shiozawa ◽  
S Aiso ◽  
S Taniguchi ◽  
S Yamashita

We studied in detail the distribution pattern of gamma-glutamyl transpeptidase (gamma-GT) in human pancreas, using the immunoperoxidase technique and a monoclonal antibody to human kidney gamma-GT. Positive reaction was confined exclusively to the luminal surface of the centroacinar cells and the epithelia of the intercalated, intralobular, and interlobular ducts. The immunoreaction was stronger in the intercalated and intralobular ducts than in the interlobular ducts. The acinar cells did not show any reaction. The islets of Langerhans were heavily surrounded by the ducts, and normal islet cells showed no reaction. The course of the ducts, from the acinar lumina to the interlobular ducts, was delineated by using reaction sites positive for gamma-GT as markers. The courses of the ducts, which comprise the pathway for pancreatic juice, were found to vary widely in their connections with each other, especially between the intralobular and interlobular ducts. At least three separate routes could be identified.

1989 ◽  
Vol 37 (7) ◽  
pp. 1053-1061 ◽  
Author(s):  
M Shiozawa ◽  
S Yamashita ◽  
S Aiso ◽  
K Yasuda

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.


Blood ◽  
1976 ◽  
Vol 47 (4) ◽  
pp. 645-650 ◽  
Author(s):  
SK Srivastava ◽  
YC Awasthi ◽  
SP Miller ◽  
A Yoshida ◽  
E Beutler

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.


1986 ◽  
Vol 63 (4) ◽  
pp. 209-221 ◽  
Author(s):  
Masahide SHIOZAWA ◽  
Sadakazu AISO ◽  
Osamu HOSHIAI ◽  
Hiromu TAHARA ◽  
Shuji YAMASHITA ◽  
...  

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