Women with preeclampsia have increased serum levels of pregnancy-associated plasma protein A (PAPP-A), inhibin A, activin A and soluble E-selectin.

OBJECTIVE: Poor placentation in early pregnancy is thought to lead to an excessive maternal systemic inflammatory response, which causes the maternal syndrome of preeclampsia. The aims of this retrospective study were to confirm old reports of increased blood levels of pregnancy-associated plasma protein A (PAPP-A) in preeclampsia and how its levels correlate with the levels of other placental and endothelial proteins that are reported to be elevated in preeclampsia. METHODS: Nineteen women with preeclampsia symptoms were matched with 19 normal pregnant controls for gestational age, maternal age, and parity. PAPP-A, placental pregnancy-specific beta1-glycoprotein (SP1), inhibin A, activin A, and sE-selectin were measured in serum using specific ELISAs. RESULTS: Maternal serum levels of PAPP-A, inhibin A, activin A and sE-selectin were increased in women with preeclampsia (mean 157.7 vs. 76.85 mIU/mL, p=0.005; 3.08 vs. 1.51 ng/mL, p=0.002, 32.36 vs. 3.77 ng/mL, p<0.001 and 62.15 vs. 46.37 ng/mL, p=0.02 respectively), compared to controls. Serum levels of SP1 were not altered in preeclampsia. PAPP-A (r=0.636, p<0.01) had a positive correlation with sE-selectin in patients with preeclampsia. Serum inhibin A and activin A had a significant positive correlation with each other in preeclampsia. CONCLUSIONS: Raised levels of PAPP-A in preeclampsia confirm earlier reports. Activin A showed the highest increase over the controls and is thus likely to be a better serum marker for this pathology than the other markers that were tested.

Follistatin-related protein (FSRP): a new member of the follistatin gene family.

The identification and characterization of follistatin related protein (FSRP) suggests that the follistatin (FS) gene family may actually contain two sub-families. The first includes FS and FSRP by virtue of their high degree of structural homology and comparable activin-binding activity, while the second sub-family contains extracellular matrix proteins that possess one or more 10-cysteine FS domains, but do not bind activin or related TGF-beta family members. Characterization of FSRP indicates that it binds activin with similar affinity and selectivity as FS, but does not bind heparin. Furthermore, although FSRP inhibits activin-mediated gene transcription in heterologous assays, FSRP is much less active than FS in the rat pituitary bioassay. When overexpressed in transgenic mice, FSRP may lead to interruption of follicular development and fertility in females but appears to have only a modest effect on males. These results suggest that FSRP is a structural, but not necessarily a functional homologue of FS.