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Genetics, structure, function, mode of actions and role in cancer development of CYP17.

Abstract
Most prostate and breast cancers are hormone dependent. The inhibition of steroid 17α-hydroxylase/17,20- lyase (CYP17), which is a crucial enzyme for steroid hormone biosynthesis, is widely used to treat androgen-dependent prostate cancer (PC). CYP17 has dual enzymatic activity: 17alpha-hydroxylase activity (utilizing delta4- C21 steroids as substrates) and the 17,20-lyase activity (using delta5- C21 steroids as substrates). The steroid biosynthetic pathway is directed to either the production of corticosteroids or sex hormones depending on the activity of CYP17. In this review, the current information on the genetics, molecular structure, substrate specificity and inhibitors of CYP17 is analyzed and discussed.
AuthorsTatyana A Sushko, Andrei A Gilep, Sergey A Usanov
JournalAnti-cancer agents in medicinal chemistry (Anticancer Agents Med Chem) Vol. 14 Issue 1 Pg. 66-76 (Jan 2014) ISSN: 1875-5992 [Electronic] Netherlands
PMID24007292 (Publication Type: Journal Article)
Chemical References
  • Adrenal Cortex Hormones
  • Androgens
  • Carcinogens, Environmental
  • Xenobiotics
  • Cytochromes b5
  • Steroid 17-alpha-Hydroxylase
Topics
  • Adrenal Cortex Hormones (biosynthesis)
  • Androgens (biosynthesis)
  • Breast Neoplasms (metabolism)
  • Carcinogenesis (drug effects, metabolism)
  • Carcinogens, Environmental (metabolism, toxicity)
  • Cytochromes b5 (metabolism)
  • Female
  • Humans
  • Male
  • Neoplasms, Hormone-Dependent (metabolism)
  • Prostatic Neoplasms (metabolism)
  • Protein Conformation
  • Steroid 17-alpha-Hydroxylase (antagonists & inhibitors, genetics, metabolism)
  • Substrate Specificity
  • Xenobiotics (metabolism, toxicity)

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