HOMEPRODUCTSCOMPANYCONTACTFAQResearchDictionaryPharmaSign Up FREE or Login

Detoxification of cyclophosphamide by human aldehyde dehydrogenase isozymes.

Abstract
In in vitro studies, no turnover of aldophosphamide and mafosfamide was observed with the tumor-specific aldehyde dehydrogenase 3 isozyme (ALDH3) isolated from human stomach mucosa as well as from lung (A549) and pharynx (UMSCC2) carcinoma cell lines. Only the human liver cytosolic ALDH preparation (ALDH1) showed any significant oxidation of aldophosphamide and mafosfamide.
AuthorsU von Eitzen, D Meier-Tackmann, D P Agarwal, H W Goedde
JournalCancer letters (Cancer Lett) Vol. 76 Issue 1 Pg. 45-9 (Jan 15 1994) ISSN: 0304-3835 [Print] Ireland
PMID8124665 (Publication Type: Journal Article)
Chemical References
  • Isoenzymes
  • Phosphoramide Mustards
  • aldophosphamide
  • Cyclophosphamide
  • Aldehyde Dehydrogenase
Topics
  • Adenocarcinoma (enzymology)
  • Aldehyde Dehydrogenase (isolation & purification, metabolism)
  • Cyclophosphamide (pharmacokinetics)
  • Gastric Mucosa (enzymology)
  • Humans
  • Inactivation, Metabolic
  • Isoelectric Focusing
  • Isoenzymes (isolation & purification, metabolism)
  • Liver (enzymology)
  • Lung Neoplasms (enzymology)
  • Oxidation-Reduction
  • Pharyngeal Neoplasms (enzymology)
  • Phosphoramide Mustards (metabolism)
  • Substrate Specificity
  • Tumor Cells, Cultured

Join CureHunter, for free Research Interface BASIC access!

Take advantage of free CureHunter research engine access to explore the best drug and treatment options for any disease. Find out why thousands of doctors, pharma researchers and patient activists around the world use CureHunter every day.
Realize the full power of the drug-disease research graph!


Choose Username:
Email:
Password:
Verify Password:
Enter Code Shown: