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Jennifer Menzies,
Laura A Magee,
Jing Li,
Ying C MacNab,
Ruihua Yin, Heather Stuart,
Brandon Baraty,
Elaine Lam,
Trevor Hamilton,
Shoo K Lee,
Peter von Dadelszen
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ABSTRACT: To assess the incidence of combined adverse maternal and perinatal outcomes in women with preeclampsia before and after introducing standardized assessment and surveillance.
This study was a preintervention (retrospective) compared with a postintervention (prospective) cohort comparison in a single-tertiary, perinatal unit that included women admitted to hospital with preeclampsia. We interrogated an existing retrospective 24-month database and then introduced the guidelines, assessing the incidence of the combined adverse maternal and perinatal outcomes for 41 months (September 2003 through February 2007). Tests of organ (dys)function were performed at least as often as on the day of admission, admission day +1, every Monday and Thursday, day of delivery, and delivery day +1. All data were checked for errors. The combined maternal outcome was maternal death or one or more of hepatic failure, hematoma, or rupture, Glasgow coma score of less than 13, stroke, at least two seizures, cortical blindness, need for positive inotrope support, myocardial infarction, infusion of any third antihypertensive, renal dialysis, renal transplantation, at least 50% FIO(2) for greater than 1 hour, intubation, or transfusion of at least 10 units of blood products. The combined perinatal outcome was perinatal or infant mortality, bronchopulmonary dysplasia, necrotizing enterocolitis, grade III/IV intraventricular hemorrhage, cystic periventricular leukomalacia, or stage 3-5 retinopathy of prematurity.
Two hundred ninety-five and 405 women were in the preintervention and postintervention cohorts, respectively. The incidence of adverse maternal outcome fell (5.1% to 0.7%; Fisher P<.001; odds ratio 0.14, 95% confidence interval 0.04-0.49). Perinatal outcomes did not change.
Standardized surveillance of women with preeclampsia was associated with reduced maternal risk.
Obstetrics and Gynecology 07/2007; 110(1):121-7. · 4.73 Impact Factor
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ABSTRACT: The pseudopodial protrusions of Moloney sarcoma virus (MSV)-Madin-Darby canine kidney (MDCK)-invasive (INV) variant cells were purified on 1-microm pore polycarbonate filters that selectively allow passage of the pseudopodial domains but not the cell body. The purified pseudopodial fraction contains phosphotyrosinated proteins, including Met and FAK, and various signaling proteins, including Raf1, MEK1, ERK2, PKBalpha (Akt1), GSK3alpha, GSK3beta, Rb, and Stat3. Pseudopodial proteins identified by liquid chromatography tandem mass spectrometry included actin and actin-regulatory proteins (ERM, calpain, filamin, myosin, Sra-1, and IQGAP1), tubulin, vimentin, adhesion proteins (vinculin, talin, and beta1 integrin), glycolytic enzymes, proteins associated with protein translation, RNA translocation, and ubiquitin-mediated protein degradation, as well as protein chaperones (HSP90 and HSC70) and signaling proteins (RhoGDI and ROCK). Inhibitors of MEK1 (U0126) and HSP90 (geldanamycin) significantly reduced MSV-MDCK-INV cell motility and pseudopod expression, and geldanamycin treatment inhibited Met phosphorylation and induced the expression of actin stress fibers. ROCK inhibition did not inhibit cell motility but transformed the pseudopodial protrusions of MSV-MDCK-INV cells into extended lamellipodia. Dominant negative Rho disrupted pseudopod expression and, in serum-starved cells, L-alpha-lysophosphatidic acid (oleoyl) activation of Rho induced pseudopodial protrusions or, in the presence of the ROCK inhibitor, extended lamellipodia. RNA was localized to the actin-rich pseudopodial domains of MSV-MDCK-INV cells, but the extent of colocalization with dense actin ruffles was reduced in the extended lamellipodia formed upon ROCK inhibition. Rho/ROCK activation in epithelial tumor cells therefore regulates RNA translocation to a pseudopodial domain that contains proteins involved in signaling, cytoskeleton remodeling, cell adhesion, glycolysis, and protein translation and degradation.
Journal of Biological Chemistry 09/2005; 280(34):30564-73. · 4.77 Impact Factor
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[show abstract]
[hide abstract]
ABSTRACT: The pseudopodial protrusions of Moloney sarcoma virus (MSV)-Madin-Darby canine kidney (MDCK)-invasive (INV) variant cells
were purified on 1-μm pore polycarbonate filters that selectively allow passage of the pseudopodial domains but not the cell
body. The purified pseudopodial fraction contains phosphotyrosinated proteins, including Met and FAK, and various signaling
proteins, including Raf1, MEK1, ERK2, PKBα (Akt1), GSK3α, GSK3β, Rb, and Stat3. Pseudopodial proteins identified by liquid
chromatography tandem mass spectrometry included actin and actin-regulatory proteins (ERM, calpain, filamin, myosin, Sra-1,
and IQGAP1), tubulin, vimentin, adhesion proteins (vinculin, talin, and β1 integrin), glycolytic enzymes, proteins associated
with protein translation, RNA translocation, and ubiquitin-mediated protein degradation, as well as protein chaperones (HSP90
and HSC70) and signaling proteins (RhoGDI and ROCK). Inhibitors of MEK1 (U0126) and HSP90 (geldanamycin) significantly reduced
MSV-MDCK-INV cell motility and pseudopod expression, and geldanamycin treatment inhibited Met phosphorylation and induced
the expression of actin stress fibers. ROCK inhibition did not inhibit cell motility but transformed the pseudopodial protrusions
of MSV-MDCK-INV cells into extended lamellipodia. Dominant negative Rho disrupted pseudopod expression and, in serum-starved
cells, l-α-lysophosphatidic acid (oleoyl) activation of Rho induced pseudopodial protrusions or, in the presence of the ROCK inhibitor,
extended lamellipodia. RNA was localized to the actin-rich pseudopodial domains of MSV-MDCK-INV cells, but the extent of colocalization
with dense actin ruffles was reduced in the extended lamellipodia formed upon ROCK inhibition. Rho/ROCK activation in epithelial
tumor cells therefore regulates RNA translocation to a pseudopodial domain that contains proteins involved in signaling, cytoskeleton
remodeling, cell adhesion, glycolysis, and protein translation and degradation.
Journal of Biological Chemistry 08/2005; 280(34):30564-30573. · 4.77 Impact Factor
