Enzymic imbalance in serine metabolism in human colon carcinoma and rat sarcoma

K. Snell, Y. Natsumeda, J. N. Eble, J. L. Glover, G. Weber

Research output: Contribution to journalArticle

94 Scopus citations

Abstract

The activities of 3-phosphoglycerate dehydrogenase, an enzyme of serine biosynthesis, and serine hydroxymethyltransferase, serine dehydratase and serine aminotransferase, which are competing enzymes of serine utilization, were assayed in human colon carcinomas from patients and in transplantable rat sarcomas. Serine dehydratase and serine aminotransferase activities were absent, whereas 3-phosphoglycerate dehydrogenase and serine hydroxymethyltransferase activities were markedly increased in both tumour types. Serine hydroxymethyltransferase catalyses the formation of glycine and methylene tetrahydrofolate which are important precursors for nucleotide biosynthesis. The observed enzymic imbalance in these tumours ensures that an increased capacity for the synthesis of serine is coupled to its utilisation for nucleotide biosynthesis as a part of the biochemical commitment to cellular replication in cancer cells. That this pattern is found in sarcomas and carcinomas, and in tumours of human and rodent origin, signifies its universal importance for the biochemistry of the cancer cell and singles it out as a potential target site for anti-cancer chemotherapy.

Original languageEnglish (US)
Pages (from-to)87-90
Number of pages4
JournalBritish Journal of Cancer
Volume57
Issue number1
DOIs
StatePublished - Jan 1988

ASJC Scopus subject areas

  • Oncology
  • Cancer Research

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