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Squalene epoxidase, oxido-squalene cyclase and cholesterol biosynthesis in normal and tumoral mucosa of the human gastro-intestinal tract. Evidence of post-HHG CoA regulation.

Abstract
Cholesterol biosynthesis was evaluated in different parts of the human gastro-intestinal tract by incorporation of labelled acetic or mevalonic acid into non-saponifiable metabolites and also by measuring squalene epoxidase activity, oxido=squalene cyclase activity and dihydrolanosterol demethylation rate. With respect to rat liver, whole cholesterol biosynthesis was generally low and we found an anatomic localization of activity towards the end of the gastro-intestinal tract. The results of analysis of mevalonic acid metabolites implied the existence of post-HMG CoA regulation. A comparison with the corresponding dat obtained from homologous cancerous tissues (inthe case of high cholesterogenic activity) did not show a greater activity in the tumor, in spite of higher levels of epoxidase concentration.
AuthorsC Tabacik, S Aliau, M Astruc, A C De Paulet
JournalBiochimica et biophysica acta (Biochim Biophys Acta) Vol. 666 Issue 3 Pg. 433-41 (Dec 23 1981) ISSN: 0006-3002 [Print] Netherlands
PMID6173065 (Publication Type: Journal Article)
Chemical References
  • Acetates
  • Glutarates
  • Cholesterol
  • Meglutol
  • Peroxidases
  • Oxygenases
  • Squalene Monooxygenase
  • Isomerases
  • Intramolecular Transferases
  • lanosterol synthase
  • Acetic Acid
Topics
  • Acetates (metabolism)
  • Acetic Acid
  • Adult
  • Aged
  • Animals
  • Cholesterol (biosynthesis)
  • Female
  • Gastric Mucosa (metabolism)
  • Gastrointestinal Neoplasms (metabolism)
  • Glutarates (metabolism)
  • Humans
  • Intestinal Mucosa (metabolism)
  • Intestine, Small (metabolism)
  • Intramolecular Transferases
  • Isomerases (metabolism)
  • Liver (metabolism)
  • Meglutol (metabolism)
  • Microsomes (metabolism)
  • Middle Aged
  • Oxygenases (metabolism)
  • Peroxidases (metabolism)
  • Placenta (metabolism)
  • Pregnancy
  • Rats
  • Squalene Monooxygenase

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