S. Gentiraimondi et al., LOW AROMATASE-ACTIVITY IN MICROSOMES FROM COMPLETE HYDATIDIFORM MOLE, The Journal of clinical endocrinology and metabolism, 76(1), 1993, pp. 108-111
The complete hydatidiform mole (CHM) is characterized by the presence
of aberrant placenta, with hyperplasia of cyto- and syncytiotrophoblas
ts and the absence of maternal genetic information. Steroidogenesis in
this condition is, thus, of special interest. In this study we invest
igated the kinetic parameters of aromatase in microsomes from CHM comp
ared with those in normal early placenta (NEP). The enzyme activity wa
s determined by measuring the conversion of [H-3] testosterone to [H-3
]estradiol plus [H-3]estrone. The K(m) value for testosterone was 33 n
mol/L in CHM and 17 nmol/L in NEP of similar gestational ages. Aminogl
utethimide, a nonsteroideal inhibitor, decreased in a dose-dependent m
anner and with the same potency the aromatization of testosterone in b
oth tissues (ID50, 2 vs. 1 mumol/L in CHM and NEP, respectively). Thes
e results suggest that the enzymes from the two sources are kineticall
y similar. However, the enzyme efficiency, expressed as the maximum ve
locity/K(m) ratio, was 17-fold lower in CHM than in NEP tissue (1.22/3
3 vs. 10.68/17 min/mg . mL). These findings suggest that in molar preg
nancy the decreased capacity of trophoblast tissue for the formation o
f estrogen could increase the testosterone concentration inside the mo
lar vesicle, which, in turn, as we previously reported, inhibits proge
sterone formation. All of these data could provide an explanation for
the low circulating level of progesterone, which may directly or indir
ectly affect the spontaneous expulsion of this aberrant tissue in the
second trimester of pregnancy.