Sexually transmitted diseases during pregnancy in Louisiana, 2007-2009: high-risk populations and adverse newborn outcomes.

BACKGROUND: The aims of the study were to determine the prevalence of sexually transmitted diseases during pregnancy (STDs/P) in Louisiana, the association of maternal characteristics with STDs/P, and the association of STDs/P with low birth weight and preterm birth. METHODS: STDs surveillance data from 2006-2009 were linked with 2007-2009 birth certificate data. The linked data were used for analyses. The data were limited to infections of chlamydia, gonorrhea, and syphilis during pregnancy. Logistic regression was applied to evaluate associations. RESULTS: The prevalence of chlamydia, gonorrhea, and syphilis during pregnancy was 5.5%, 1.6%, and 0.3%, respectively, among women who had a live birth between 2007 and 2009. Maternal race, ethnicity, age, education, marital status, and Medicaid paid for delivery were associated with STDs/P (p-value < .05). Only infection with gonorrhea during pregnancy was associated with preterm birth [adjusted OR: 1.20 (CI95%: 1.08-1.33)]. CONCLUSIONS: The prevalence of STDs/P in Louisiana remains high. Low-educated, young, black, single, and economically disadvantaged mothers were at high risk for STDs during pregnancy. Women diagnosed with gonorrhea during pregnancy were more likely to experience preterm birth.

Conversion of human 5-lipoxygenase to a 15-lipoxygenase by a point mutation to mimic phosphorylation at Serine-663.

The enzyme 5-lipoxygenase (5-LOX) initiates biosynthesis of the proinflammatory leukotriene lipid mediators and, together with 15-LOX, is also required for synthesis of the anti-inflammatory lipoxins. The catalytic activity of 5-LOX is regulated through multiple mechanisms, including Ca(2+)-targeted membrane binding and phosphorylation at specific serine residues. To investigate the consequences of phosphorylation at S663, we mutated the residue to the phosphorylation mimic Asp, providing a homogenous preparation suitable for catalytic and structural studies. The S663D enzyme exhibits robust 15-LOX activity, as determined by spectrophotometric and HPLC analyses, with only traces of 5-LOX activity remaining; synthesis of the anti-inflammatory lipoxin A(4) from arachidonic acid is also detected. The crystal structure of the S663D mutant in the absence and presence of arachidonic acid (in the context of the previously reported Stable-5-LOX) reveals substantial remodeling of helices that define the active site so that the once fully encapsulated catalytic machinery is solvent accessible. Our results suggest that phosphorylation of 5-LOX at S663 could not only down-regulate leukotriene synthesis but also stimulate lipoxin production in inflammatory cells that do not express 15-LOX, thus redirecting lipid mediator biosynthesis to the production of proresolving mediators of inflammation.

The structure of human 5-lipoxygenase.

The synthesis of both proinflammatory leukotrienes and anti-inflammatory lipoxins requires the enzyme 5-lipoxygenase (5-LOX). 5-LOX activity is short-lived, apparently in part because of an intrinsic instability of the enzyme. We identified a 5-LOX-specific destabilizing sequence that is involved in orienting the carboxyl terminus, which binds the catalytic iron. Here, we report the crystal structure at 2.4 angstrom resolution of human 5-LOX stabilized by replacement of this sequence.