Placental Protein (placental + protein)

Distribution by Scientific Domains


Selected Abstracts


PP13 stability in first trimester maternal serum and whole blood

PRENATAL DIAGNOSIS, Issue 6 2010
N. J. Cowans
Abstract Background Maternal serum placental protein 13 (PP13) has been proposed as a marker for prenatal screening of pre-eclampsia (PE) and other adverse pregnancy outcomes. This study aims to examine the stability of PP13 at different routine temperatures. Methods Maternal serum pools and whole blood samples were stored at ,30 °C', room temperature or refrigerator temperature. Further, serum pools were also subjected to repeated freeze,thaw cycles. PP13 was measured at set time points using an AutoDELFIAź research assay. Results Levels of PP13 are stable, defined as less than 10% change in concentration, in serum for 17.4 h at ,30 °C', 3.4 days at room temperature and for at least 34 days at refrigerator temperature. PP13 concentration is not altered following three ,20 °C to room temperature freeze,thaw cycles. PP13 is stable in whole blood for at least 3 days at all three temperatures studied. Conclusions PP13 is a suitably stable molecule and can be treated under routine laboratory and normal transport temperatures. Copyright © 2010 John Wiley & Sons, Ltd. [source]


Maternal serum placental protein 13 at 11,13 weeks of gestation in preeclampsia

PRENATAL DIAGNOSIS, Issue 12 2009
Ranjit Akolekar
Abstract Objective To examine the potential value of maternal serum concentration of placental protein 13 (PP13) at 11,13 weeks' gestation in screening for preeclampsia (PE). Methods Serum PP13, PAPP-A and uterine artery pulsatility index (PI) were determined in a case,control study of 208 cases that developed PE including 48 that required delivery before 34 weeks (early-PE) and 416 unaffected controls. Results Serum PP13 levels, expressed as multiples of the median (MoM) in the unaffected group, were significantly reduced in early-PE (0.83 MoM) but not in late-PE (0.96 MoM). In both early- and late-PE serum PAPP-A (0.55 and 0.84 MoM) was reduced and uterine artery PI (1.61 and 1.25 MoM) was increased. In PE pregnancies there was a significant association between serum PP13 and both uterine artery PI and serum PAPP-A (p < 0.0001 for both). Logistic regression analysis demonstrated that serum PP13 did not improve significantly the prediction of early-PE provided by a combination of maternal factors, uterine artery PI and PAPP-A. Conclusion PP13 is implicated in the pathogenesis of impaired placentation and subsequent development of early-PE but measurement of this placental product is unlikely to be useful in screening for the disease at 11,13 weeks. Copyright © 2009 John Wiley & Sons, Ltd. [source]


ADAM12-s in coelomic fluid and maternal serum in early pregnancy

PRENATAL DIAGNOSIS, Issue 13 2006
George Makrydimas
Abstract Objectives ADAM12-s is a placental protein. In early pregnancy, reduced maternal levels of ADAM12-s have been reported in association with foetal trisomy 21 or 18 and in cases that subsequently develop pre-eclampsia and foetal growth restriction. The aim of this study is to investigate the distribution of ADAM12-s in early pregnancy by comparing its concentration in maternal serum, amniotic fluid and coelomic fluid. Methods Coelomic fluid was obtained by coelocentesis from 13 singleton pregnancies with live foetuses at 6.9,9.3 weeks of gestation. Maternal serum was also obtained in all cases and in six cases amniotic fluid was also obtained. The concentration of ADAM12-s was measured by dissociation enhanced lanthanide fluoro-immunoassay. Results The median concentration of ADAM12-s in maternal serum was 132.7 (range 33.8,254.5) ng/mL and in coelomic fluid it was 10.5 (range 1.3,15.8) ng/mL; there were no detectable levels in five of the six amniotic fluid samples. The concentration of maternal serum ADAM12-s increased significantly with gestation (r = 0.862, p < 0.0001). There was no significant association between coelomic fluid ADAM12-s and either gestation (r = 0.255, p = 0.401) or maternal serum ADAM12-s (r = 0.302, p = 0.316). Conclusion The distribution of ADAM12-s in maternal serum and the early embryonic fluid compartments is consistent with its syncytiotrophoblastic origin. Copyright © 2006 John Wiley & Sons, Ltd. [source]


A cloning and expression analysis of pregnancy-associated glycoproteins expressed in trophoblasts of the white-tail deer placenta,

MOLECULAR REPRODUCTION & DEVELOPMENT, Issue 11 2007
Gretchen A. Brandt
Abstract The pregnancy-associated glycoproteins (PAGs) are placental proteins that have been cloned from swine, sheep, goats, and cattle, but never from animals within the Cervidae family. The goal of this work was to characterize PAGs in white-tailed deer. Placenta and uterine tissues were collected from pregnant does at days 85 and 90 of pregnancy. RNA from cotyledons was used to amplify deer PAGs by RT-PCR. Ten distinct cDNAs were cloned and sequenced. Some normally conserved amino acids comprising the catalytic site were found to be altered in deer PAGs 4, 5, and 8; another PAG, (PAG-9) was a splice variant that lacked exon 7. In each case, these mutations would likely preclude proteolytic activity for these proteins. A phylogenetic analysis revealed that most of the deer PAGs fell within the ancient PAG grouping. The remainder fell within the more modern (BNC-specific) PAG group. Western blotting was performed with anti-PAG antibodies and this analysis revealed that deer PAGs comprise a heterogeneous group based on different antigenicities and electrophoretic mobilities. Immunohistochemistry and in situ hybridization revealed some unique localization patterns of PAGs in the deer placentome compared to those in other ruminants. Most notably, deer PAGs 4 and 5, which according to the phylogeny, are "ancient PAGs," were expected to be present in all trophoblasts; instead, they were localized to the BNC. Although many of the PAGs identified here are very similar to those in Bovidae, some are clearly distinct in their expression pattern and probably possess functional roles unique to cervid reproduction. Mol. Reprod. Dev. 74: 1355,1362, 2007. © 2007 Wiley-Liss, Inc. [source]