scholarly journals Immunohistochemical study of .GAMMA.-glutamyl transpeptidase with monoclonal antibodies. I Preparation and characteristics of monoclonal antibodies to .GAMMA.-glutamyl transpeptidase.

1986 ◽  
Vol 19 (5) ◽  
pp. 589-600 ◽  
Author(s):  
KENJIRO YASUDA ◽  
SHUJI YAMASHITA ◽  
SADAKAZU AISO ◽  
MASAHIDE SHIOZAWA ◽  
TOSHIKO KOMATSU
Keyword(s):  
Monoclonal Antibodies ◽  
Immunohistochemical Study ◽  
Gamma Glutamyl Transpeptidase ◽  
Gamma Glutamyl ◽  
Glutamyl Transpeptidase

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 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 Localization of Gamma-Glutamyl Transpeptidase in the Proliferative State of Liver An Enzyme Histochemical and Immunohistochemical Study

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

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
Keyword(s):  
Monoclonal Antibody ◽  
Immunohistochemical Study ◽  
Islet Cells ◽  
Human Kidney ◽  
Immunoperoxidase Technique ◽  
Human Pancreas ◽  
Gamma Glutamyl Transpeptidase ◽  
Gamma Glutamyl ◽  
Glutamyl Transpeptidase ◽  
Centroacinar Cells

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.

Relationship Between Gamma-glutamyl Transpeptidase Activity and Inflammatory Response in Lichen Planus

2018 ◽  
Vol 69 (3) ◽  
pp. 739-743 ◽  
Author(s):  
Madalina Irina Mitran ◽  
Ilinca Nicolae ◽  
Corina Daniela Ene ◽  
Cristina Iulia Mitran ◽  
Clara Matei ◽  
...  
Keyword(s):  
Inflammatory Response ◽  
Lichen Planus ◽  
Inflammatory Process ◽  
Molecular Mechanisms ◽  
Functional Adaptation ◽  
Physical Factors ◽  
Inflammatory Disorder ◽  
Gamma Glutamyl Transpeptidase ◽  
Gamma Glutamyl ◽  
Glutamyl Transpeptidase

Chemicals used in the manufacture of synthetic fibers have been associated with undesirable side effects such as itching or skin lesions and it seems that they are involved in the induction of pathological processes such as oxidative stress and inflammation. Lichen planus (LP) can be regarded as an inflammatory disorder, chemical and physical factors playing an important role in the perpetuation of the inflammatory process. Gamma-glutamyl transpeptidase (GGT) plays an important role in the preservation of skin architecture and modulation of skin inflammation. In this study, we found that GGT activity is increased in LP patients with mild inflammation, whilst GGT is inactivated under conditions of severe inflammation. Therefore, GGT is involved in the inflammatory process, but there is no a positive correlation between its activity and the intensity of the inflammatory response. This functional adaptation of the enzyme may be due to down-regulation of its synthesis under free radical overload conditions. Understanding the molecular mechanisms involved in the modulation of intracellular redox homeostasis is an important step in the pharmacological management of patients with LP.

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