Document Detail


Enzymes of creatine biosynthesis, arginine and methionine metabolism in normal and malignant cells.
MedLine Citation:
PMID:  19021765     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The creatine/creatine kinase system decreases drastically in sarcoma. In the present study, an investigation of catalytic activities, western blot and mRNA expression unambiguously demonstrates the prominent expression of the creatine-synthesizing enzymes l-arginine:glycine amidinotransferase and N-guanidinoacetate methyltransferase in sarcoma, Ehrlich ascites carcinoma and Sarcoma 180 cells, whereas both enzymes were virtually undetectable in normal muscle. Compared to that of normal animals, these enzymes remained unaffected in the kidney or liver of sarcoma-bearing mice. High activity and expression of mitochondrial arginase II in sarcoma indicated increased ornithine formation. Slightly or moderately higher levels of ornithine, guanidinoacetate and creatinine were observed in sarcoma compared to muscle. Despite the intrinsically low level of creatine in Ehrlich ascites carcinoma and Sarcoma 180 cells, these cells could significantly take up and release creatine, suggesting a functional creatine transport, as verified by measuring mRNA levels of creatine transporter. Transcript levels of arginase II, ornithine-decarboxylase, S-adenosyl-homocysteine hydrolase and methionine-synthase were significantly upregulated in sarcoma and in Ehrlich ascites carcinoma and Sarcoma 180 cells. Overall, the enzymes related to creatine and arginine/methionine metabolism were found to be significantly upregulated in malignant cells. However, the low levels of creatine kinase in the same malignant cells do not appear to be sufficient for the building up of an effective creatine/phosphocreatine pool. Instead of supporting creatine biosynthesis, l-arginine:glycine amidinotransferase and N-guanidinoacetate methyltransferase appear to be geared to support cancer cell metabolism in the direction of polyamine and methionine synthesis because both these compounds are in high demand in proliferating cancer cells.
Authors:
Soumen Bera; Theo Wallimann; Subhankar Ray; Manju Ray
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  The FEBS journal     Volume:  275     ISSN:  1742-4658     ISO Abbreviation:  FEBS J.     Publication Date:  2008 Dec 
Date Detail:
Created Date:  2008-11-21     Completed Date:  2009-01-27     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101229646     Medline TA:  FEBS J     Country:  England    
Other Details:
Languages:  eng     Pagination:  5899-909     Citation Subset:  IM    
Affiliation:
Department of Biological Chemistry, Indian Association for the Cultivation of Science, Jadavpur, Kolkata, India.
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MeSH Terms
Descriptor/Qualifier:
5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase / genetics
Adenosylhomocysteinase / genetics
Amidinotransferases / genetics,  metabolism
Animals
Arginase / genetics,  metabolism
Arginine / metabolism*
Carcinoma, Ehrlich Tumor / enzymology,  metabolism,  pathology
Cell Line, Tumor
Creatine / biosynthesis*,  blood,  metabolism
Creatinine / blood,  metabolism
Enzymes / genetics,  metabolism*
Female
Gene Expression Regulation, Neoplastic / genetics
Guanidinoacetate N-Methyltransferase / genetics,  metabolism
Kidney / enzymology,  metabolism
Liver / enzymology,  metabolism
Membrane Transport Proteins / genetics
Methionine / metabolism*
Mice
Muscle, Skeletal / enzymology,  metabolism
Neoplasms / enzymology*,  metabolism,  pathology
Ornithine / blood,  metabolism
Ornithine Decarboxylase / genetics
Sarcoma 180 / enzymology,  metabolism,  pathology
Chemical
Reg. No./Substance:
0/Enzymes; 0/Membrane Transport Proteins; 0/creatine transporter; 57-00-1/Creatine; 60-27-5/Creatinine; 63-68-3/Methionine; 7006-33-9/Ornithine; 74-79-3/Arginine; EC 2.1.1.13/5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase; EC 2.1.1.2/Guanidinoacetate N-Methyltransferase; EC 2.1.4.-/Amidinotransferases; EC 2.1.4.1/glycine amidinotransferase; EC 3.3.1.1/Adenosylhomocysteinase; EC 3.5.3.1/Arginase; EC 4.1.1.17/Ornithine Decarboxylase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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