Biochemical properties of cytochrome P-450 in relation to steroid oxygenation.

نویسندگان

  • M J Coon
  • K Inouye
چکیده

The P-450 cytochromes have been characterized biochemically in recent years as a family of monooxygenases that reductively activate molecular oxygen for insertion into steroids and other physiologically occurring lipids. Many of these enzymes are also known to bind and oxygenate a host of foreign compounds, including alcohol, drugs, pesticides, anesthetics, and mutagens. Some of the poorly understood variations in congenital adrenal hyperplasia may represent nutritional effects on the P-450 oxygenase systems or the ability of xenobiotics to interfere with normal steroid metabolism by these versatile cytochromes.

برای دانلود رایگان متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Distinct forms of cytochrome P-450 are responsible for 6 beta-hydroxylation of bile acids and of neutral steroids.

Cytochrome P-450-dependent 6 beta-hydroxylation of bile acids in rat liver contributes to the synthesis of the quantitatively important pool of 6-hydroxylated bile acids, as well as to the detoxification of hydrophobic bile acids. The lithocholic acid 6 beta-hydroxylation reaction was investigated and compared with androstenedione 6 beta-hydroxylation. Differential responses of these two activi...

متن کامل

Cytochrome P-450 isozymes and monooxygenase activity in aquatic animals.

The roles of different forms of cytochrome P-450 in activation and deactivation of toxic chemicals, synthesis and breakdown of steroid hormones, and other functions, indicate the significance of these enzymes. Monooxygenase systems have been studied in species from several phyla of aquatic organisms. However, cytochrome P-450, the dominant catalyst in xenobiotic monooxygenase activity, is best ...

متن کامل

Involvement of Cytochrome P-450 in n-Butyl Nitrite-Induced Hepatocyte Cytotoxicity

      Addition of n-butyl nitrite to isolated rat hepatocytes caused an immediate glutathione depletion followed by an inhibition of mitochondrial respiration, inhi- bition of glycolysis and ATP depletion. At cytotoxic butyl nitrite concentrations, lipid  peroxidation  occurred  before  the  plasma  membrane  was  disrupted. Cytochrome P-450 inhibitors inhibited peroxynitrite formation and prev...

متن کامل

High affinity binding of substrate and effector ligands to testicular microsomal cytochrome P-450.

The binding characteristics of substrate and effector ligands to testicular microsomal cytochrome P-450 (17 alpha-hydroxylase/C17-20 lyase) have been investigated by difference spectroscopy. Steroid products and their analogs induce oxygen-mediated damage of microsomal P-450 activities of cultured Leydig cells, whereas testosterone acetate protects P-450 from this damage [1]. Progesterone and 1...

متن کامل

Zonation of hepatic cytochrome P-450 expression and regulation.

The CYP genes encode enzymes of the cytochrome P-450 superfamily. Cytochrome P-450 (CYP) enzymes are expressed mainly in the liver and are active in mono-oxygenation and hydroxylation of various xenobiotics, including drugs and alcohols, as well as that of endogenous compounds such as steroids, bile acids, prostaglandins, leukotrienes and biogenic amines. In the liver the CYP enzymes are consti...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

عنوان ژورنال:
  • Annals of the New York Academy of Sciences

دوره 458  شماره 

صفحات  -

تاریخ انتشار 1985