Investigation on phosphate dependent glutaminase (EC 3.5.1.2) activity in host tissues of EAC-bearing mice and response of liver EC 3.5.1.2 on Cu-ATP therapy

• Published in: Cancer letters Vol. 58; no. 1; pp. 151 - 153
• Main Authors: Pal, S., Nayak, K.K., Maity, P.
• Format: Journal Article
• Language: English
• Published: Shannon Elsevier Ireland Ltd 14.06.1991; Elsevier
• Subjects: Adenosine Triphosphate - therapeutic use; Animals; Biological and medical sciences; Brain - enzymology; Carcinoma, Ehrlich Tumor - drug therapy; Carcinoma, Ehrlich Tumor - enzymology; Carcinoma, Ehrlich Tumor - pathology; Cell Division - drug effects; copper-ATP complex; Cu-ATP therapy; Ehrlich ascites tumor; glutaminase; Glutaminase - analysis; Glutaminase - antagonists & inhibitors; Kidney - enzymology; Liver - drug effects; Liver - enzymology; Medical sciences; Mice; mouse liver; Spleen - enzymology; Tumors; glutaminase; Ehrlich ascites tumor; Cu-ATP therapy; mouse liver; copper-ATP complex; Pathophysiology; Enzyme; Rodentia; Glutaminase; Vertebrata; Mammalia; Cell line; Enzymatic activity; Mouse; Copper; ATP; Tumor cell
• ISSN: 0304-3835; 1872-7980
• DOI: 10.1016/0304-3835(91)90038-J

Phosphate-dependent glutaminase activity in spleen, kidney, brain and liver is increased after tumor cell inoculation and this activity gradually increases with the progression of the tumor. The increase in enzyme activity in the liver is significant. Studies of the response of liver glutaminase after Cu-ATP treatment reveals that Cu-ATP is capable of reducing the high glutaminase level in subjects with malignant tumors to the normal level.