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J. Biol. Chem., Vol. 262, Issue 6, 2787-2793, 02, 1987
K Nagata, T Matsunaga, J Gillette, HV Gelboin and FJ Gonzalez
A P-450, designated P-450a, with high testosterone 7 alpha-hydroxylase
activity was purified from rat liver microsomes. Specific polyclonal
antibody against this P-450 was used to screen a lambda gt11 expression
cDNA library and a 1687-base pair cDNA was isolated and sequenced. The
deduced protein had 492 amino acids, a calculated Mr of 56,016, and it
shared 51 and 45% amino acid similarities to P-450e and P-450f,
respectively. Regions of similarity were distributed in distinct areas of
high and low similarity along the P-450a primary sequence. P-450a cDNA was
introduced into yeast cells using the expression vector pAAH5, and the
resultant yeast microsomes contained both a protein of identical
electrophoretic mobility to that of rat P-450a and testosterone 7
alpha-hydroxylase activity. These results confirm enzyme reconstitution
data and antibody inhibition data that P-450a possesses testosterone 7
alpha-hydroxylase activity. The antibody and cDNA probes were used to
examine the mechanism of regulation of P-450a by inducers and during
development. P-450a and its mRNA were present at low level in newborn rats
and increased to maximal level at 1 week of age in both males and females.
At age 12 weeks, however, the P-450a level decreased in males but remained
elevated in females. Concomitant with the decrease in P-450a in adult males
was an increase in level of another immunologically related P-450. In adult
male rats, P-450a was induced almost 5-fold by administration of
3-methylcholanthrene and this induction was the result of an increase in
its mRNA. These results establish testosterone 7 alpha-hydroxylase as a
member of the P-450e gene family that is developmentally regulated,
sex-dependent, and markedly inducible by 3-methylcholanthrene.
Rat testosterone 7 alpha-hydroxylase. Isolation, sequence, and expression of cDNA and its developmental regulation and induction by 3- methylcholanthrene
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