Carbamoyl phosphate synthetase (glutamine-hydrolyzing): increased activity in cancer cells.

Abstract

The specific activity of carbamoyl phosphate synthetase (glutamine-hydrolyzing), the first and rate-limiting enzyme of de novo uridine 5'-triphosphate biosynthesis, was increased in 13 transplantable hepatomas, particularly in the rapidly growing tumors (5.7- to 9.5-fold), and the rise was correlated with tumor growth rates. Thus, synthetase activity was linked with both hepatic neoplastic transformation and progression. Synthetase specific activity was so elevated in a transplantable sarcoma (18-fold) and a kidney adenocarcinoma (5-fold). The increased activity should enhance the capacity of the pathway and should confer selective advantages to cancer cells.

• Authors: T Aoki, G Weber
• Journal: Science (New York, N.Y.) (Science) Vol. 212 Issue 4493 Pg. 463-5 (Apr 24 1981) ISSN: 0036-8075 [Print] United States
• PMID: 7209543 (Publication Type: Journal Article, Research Support, U.S. Gov't, P.H.S.)

Chemical References

• Ligases
• Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing)

Topics

• Adenocarcinoma (enzymology)
• Animals
• Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing) (metabolism)
• Cell Differentiation
• Kidney Neoplasms
• Ligases (metabolism)
• Liver (enzymology)
• Liver Neoplasms, Experimental (enzymology, pathology)
• Liver Regeneration
• Neoplasm Transplantation
• Rats
• Sarcoma, Experimental (enzymology)