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Tidal wetlands can be a substantial sink of greenhouse gases, which can be offset by variable methane (CH 4 ) emissions under certain environmental conditions and anthropogenic interventions. Land managers and policymakers need maps of tidal wetland CH 4 properties to make restoration decisions and inventory greenhouse gases. However, there is a mismatch in spatial scale between point-based sampling of porewater CH 4 concentration and its predictors, and the coarser resolution mapping products used to upscale these data. We sampled porewater CH 4 concentrations, salinity, sulfate (SO 4 2- ), ammonium (NH 4 + ), and total Fe using a spatially stratified sampling at 27 tidal wetlands in the United States. We measured porewater CH 4 concentrations across four orders of magnitude (0.05 to 852.9 μM). The relative contribution of spatial scale to variance in CH 4 was highest between- and within-sites. Porewater CH 4 concentration was best explained by SO 4 2- concentration with segmented linear regression (p < 0.01, R 2  = 0.54) indicating lesser sensitivity of CH 4 to SO 4 2- below 0.62 mM SO 4 2- . Salinity was a significant proxy for CH 4 concentration, because it was highly correlated with SO 4 2- (p < 0.01, R 2  = 0.909). However, salinity was less predictive of CH 4 with segmented linear regression (p < 0.01, R 2  = 0.319) relative to SO 4 2- . Neither NH 4 + , total Fe, nor relative tidal elevation correlated significantly with porewater CH 4 ; however, NH 4 + was positively and significantly correlated with SO 4 2- after detrending CH 4 for its relationship with SO 4 2- (p < 0.01, R 2  = 0.194). Future sampling should focus on within- and between-site environmental gradients to accurately map CH 4 variation. Mapping salinity at sub-watershed scales has some potential for mapping SO 4 2- , and by proxy, constraining spatial variation in porewater CH 4 concentrations. Additional work is needed to explain site-level deviations from the salinity-sulfate relationship and elucidate other predictors of methanogenesis. This work demonstrates a unique approach to remote team science and the potential to strengthen collaborative research networks., Competing Interests: Declaration of competing interest Erika L. Koontz, James R. Holmquist reports financial support was provided by NASA. Sarah M. Parker, Alice E. Stearns, Brian J. Roberts, Patricia Y. Oikawa, J. Patrick Megonigal reports financial support was provided by NASA. J. Patrick Megonigal, Amanda C. Spivak reports was provided by National Science Foundation. James R. Holmquist reports was provided by US Department of Energy. Andre S. Rovai, Robert R. Twilley reports was provided by US Army Engineer Research and Development Center. Amanda C. Spivak reports was provided by US Coastal Research Program. If there are other authors, they declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 The Authors. Published by Elsevier B.V. All rights reserved.)

Louisiana estuaries are important habitats in the northern Gulf of Mexico, a region undergoing significant and sustained human- and climate-driven changes. This paper synthesizes data collected over multiple years from four Louisiana estuaries - Breton Sound, Terrebonne Bay, the Atchafalaya River Delta Estuary, and Vermilion Bay - to characterize trends in phytoplankton biomass, community composition, and the environmental factors influencing them. Results highlight similarities in timing and composition of maximum chlorophyll, with salinity variability often explaining biomass trends. Distinct drivers for biomass versus community structure were observed in all four estuarine systems. Systems shared a lack of significant correlation between river discharge and overall phytoplankton biomass, while discharge was important for understanding community composition. Temperature was a significant explanatory variable for both biomass and community composition in only one system. These results provide a regional view of phytoplankton dynamics in Louisiana estuaries critical to understanding and predicting the effects of ongoing change., (Copyright © 2022 The Authors. Published by Elsevier Ltd.. All rights reserved.)

Coxsackievirus B3 (CVB3) infection of C57Bl/6 mice shows a sex bias with males developing more severe cardiac inflammation than females because males develop a Th1 inflammatory response, whereas females develop a Th2 response. Since their discovery, Toll-like receptors have been shown to play an important role in the development of the immune response against harmful pathogens. To assess the role of TLRs in coxsackievirus-induced myocarditis wild type and Toll-like receptor 2-/- male and female mice were infected and assessed for viral replication, myocarditis, helper T-cell generation, and regulatory T-cell generation. TLR2-/- mice show reduced Th1 expression compared to controls. Treatment of wild type mice with either Pam3CSK4 (TLR2) or LPS (TLR4) specific TLR agonists resulted in increased Th1 expression in male and female mice and a decrease in FoxP3+ regulatory T-cells in male mice. The suppression of T regulatory cells by TLR signaling in males but not females correlates with the increased myocarditis susceptibility of the males., (Copyright © 2012 Elsevier Inc. All rights reserved.)

Plakophilins (Pkp-1, -2, and -3) comprise a family of armadillo repeat-containing proteins first identified as desmosomal plaque components, in which they link desmoplakin to the desmosomal cadherins. In addition to their role in desmosomal cell-cell adhesion, Pkps also localize to the nucleus, where they perform unknown functions. Of the three Pkps, Pkp-1 is most readily detected in the nucleus, where it is localized to the nucleoplasm. Pkp chimeras containing the Pkp-1 head domain and Pkp-3 armadillo repeat domain were localized to the nucleus in A431 cells, whereas Pkp chimeras containing the Pkp-3 head domain and Pkp-1 armadillo repeat domain localized to the desmosome and the cytosol. DNAse I digestion of chromatin in cultured cells results in loss of nuclear Pkp-1, suggesting that Pkp-1 associates specifically with nuclear components. In addition, in vitro assays revealed that the amino-terminal head domains of Pkps-1 and -2 were sufficient to bind single-stranded DNA. Induction of DNA damage induced a partial redistribution of Pkp-1 protein to the nucleolus, and depletion of Pkp-1 resulted in increased survival in response to DNA damage. These data suggest that in addition to mediating desmosome assembly, the nuclear pool of Pkp can influence cell survival by interactions with DNA.

In an experimental model of liver cirrhosis, marked increases in ER proteasome content in rat livers were observed 5 h after acute i.p. injection of the hepatotoxicant CCl4. To confirm the role of CYP2E1 in mediating protein misfolding/damage in the ER via its metabolism of CCl4, 293T cells stably transfected with human CYP2E1 were exposed to CCl4 and cell ER fractions assessed for ubiquitination. Increases in ER ubiquitin conjugates were noted in CYP2E1/293T cells treated with CCl4 and not in controls, suggesting these effects are CYP2E1 specific. Finally, the role of CYP2E1 in ER homeostasis was investigated by examining the unfolded protein response (UPR). When exposed to CCl4, CYP2E1/293T cells but not 293T or CYP1A2/293T cells showed rapid induction of the UPR-inducible ER chaperone BiP. Collectively, the data presented suggest that CYP2E1 is capable of inducing significant ER protein damage and stress via its catalytic activation of pro-oxidants.

The molecular mechanism of cytochrome P4502E1 (CYP2E1) inhibition by a synthetic compound, YH439, was studied. In rats treated with YH439, N-nitrosodimethylamine demethylase activity and the amount of immunoreactive CYP2E1 were rapidly decreased in time- and dose-dependent manners. Within 2 h after a single dose of YH439 (150 mg/kg), the CYP2E1-catalyzed activity in uninduced rats was decreased by about 30% and by 43% at 24 h after YH439 injection. YH439 treatment also reduced the elevation of CYP2E1 enzyme activity in starved (induced) animals by 34%. More profound inhibition of CYP2E1 protein levels was observed by immunoblot analysis. The level of CYP2E1 catalytic activity and immunoreactive protein remained suppressed for at least 48 h and returned to normal level at 72 h after YH439 treatment. The levels of immunoreactive CYP2B1/2 protein and catalytic activity were moderately increased while little change was observed in the levels of NADPH-dependent P450 oxidoreductase activity and its protein after treatment with YH439. Unlike competitive inhibitors of CYP2E1, YH439 rapidly (within 2 h) decreased the level of CYP2E1 mRNA, while malotilate, a structural analog of YH439, slightly suppressed its level. Nuclear run-on transcription analyses at 2, 4, and 8 h post-YH439 administration revealed that the inhibition of CYP2E1 by YH439 is at the level of transcription, indicating that YH439 is a new class of CYP2E1 inhibitor. Our data demonstrate that YH439 is a powerful inhibitor of CYP2E1 expression and is thus potentially useful as a pharmacological tool to study CYP2E1 function as well as a potential therapeutic agent.

Controversy exists as to whether the induction of CYP2E1 by ethanol occurs via increased protein synthesis or protein stabilization. To address these issues in vivo, we chronically administered ethanol to rats and determined levels of immunoreactive CYP2E1 in liver, kidney, brain and upper gastro-intestinal tract (GI). Our data shows that chronic ethanol administration induces hepatic (5-6-fold over pair-fed controls) and extra-hepatic CYP2E1, an effect which is strikingly absent 12 hours after ethanol withdrawal. No changes in CYP2E1 mRNA were observed at any time, suggesting these changes are mainly post-translational at a blood ethanol concentration of 0.15% w/v. Our experimental data indicates that CYP2E1 possesses a half-life of 6 hours or less in the liver and is rapidly degraded following the removal of ethanol. This pattern of CYP2E1 turnover was also observed in other tissues, suggestive of a similar mode of regulation.

Multiplicity of hepatic microsomal coenzyme A ligases catalyzing acyl-CoA thioester formation is an important factor for consideration in relation to the metabolism of xenobiotic carboxylic acids. In this study the kinetic characteristics of rat hepatic microsomal nafenopin-CoA ligase were studied and compared with those of long-chain fatty acid (palmitoyl) CoA ligase. The high affinity component of palmitoyl-CoA formation was inhibited by nafenopin (Ki 53 microM) and ciprofibrate (Ki 1000 microM). Analagous to palmitoyl-CoA, nafenopin-CoA formation was catalyzed by an apparent high affinity low capacity isoform (Km 6 +/- 2.5 microM, Vmax 0.33 +/- 0.12 nmol/mg per min) which was inhibited competitively by palmitic acid (mean Ki 1.7 microM, n = 5) and R-ibuprofen (mean Ki 10.8 microM, n = 5) whilst ciprofibrate and clofibric acid were ineffective as inhibitors. The intrinsic metabolic clearance of nafenopin to nafenopin-CoA (Vmax/Km 0.057 +/- 0.011 nmol/mg/min/ +/- M) was similar to that reported recently for the formation of ibuprofenyl-CoA by rat liver microsomes. Evidence of both a substantial difference between the Km and Ki for nafenopin and lack of commonality with regard to xenobiotic inhibitors suggests that the high affinity microsomal nafenopin-CoA and long-chain fatty acid-CoA ligases are kinetically distinct. Thus until the current 'long-chain like' xenobiotic-CoA ligases are fully characterised in terms of substrate specificity, inhibitor profile, etc, it will be impossible to rationalize (and possibly predict) the metabolism and hence toxicity of xenobiotic carboxylic acids forming acyl-CoA thioester intermediates.