A Novel Ecdysone Receptor Mediates Steroid-Regulated Developmental Events during the Mid-Third Instar of Drosophila

The larval salivary gland of Drosophila melanogaster synthesizes and secretes glue glycoproteins that cement developing animals to a solid surface during metamorphosis. The steroid hormone 20-hydroxyecdysone (20E) is an essential signaling molecule that modulates most of the physiological functions of the larval gland. At the end of larval development, it is known that 20E—signaling through a nuclear receptor heterodimer consisting of EcR and USP—induces the early and late puffing cascade of the polytene chromosomes and causes the exocytosis of stored glue granules into the lumen of the gland. It has also been reported that an earlier pulse of hormone induces the temporally and spatially specific transcriptional activation of the glue genes; however, the receptor responsible for triggering this response has not been characterized. Here we show that the coordinated expression of the glue genes midway through the third instar is mediated by 20E acting to induce genes of the Broad Complex (BRC) through a receptor that is not an EcR/USP heterodimer. This result is novel because it demonstrates for the first time that at least some 20E-mediated, mid-larval, developmental responses are controlled by an uncharacterized receptor that does not contain an RXR-like component

ACC/AHA 2002 guideline update for exercise testing: Summary article. A report of the American College of Cardiology/American Heart Association Task Force on Practice Guidelines (Committee to update the 1997 exercise testing guidelines)

"The American College of Cardiology (ACC)/American Heart Association (AHA) Task Force on Practice Guidelines regularly reviews existing guidelines to determine when an update or full revision is needed. This process gives priority to areas where major changes in text, and particularly recommendations, are mentioned on the basis of new understanding or evidence. Minor changes in verbiage and references are discouraged. The ACC/AHA guidelines for exercise testing that were published in 1997 have now been updated. The full-text guidelines incorporating the updated material are available on the Internet (www.acc.org or www.americanheart.org) in both a version that shows the changes in the 1997 guidelines in strike-over (deleted text) and highlighting (new text) and a “clean” version that fully incorporates the changes. This article describes the 10 major areas of change reflected in the update in a format that we hope can be read and understood as a stand-alone document. The table of contents from the full-length guideline (see next page) indicates the location of these changes. Interested readers are referred to the full-length Internet version to completely understand the context of these changes. All new references appear in boldface type; all original references appear in normal type.

ACC/AHA 2002 Guideline Update for Exercise Testing: Summary Article: A Report of the American College of Cardiology/American Heart Association Task Force on Practice Guidelines (Committee to Update the 1997 Exercise Testing Guidelines)

The American College of Cardiology (ACC)/American Heart Association (AHA) Task Force on Practice Guidelines regularly reviews existing guidelines to determine when an update or full revision is needed. This process gives priority to areas where major changes in text, and particularly recommendations, are mentioned on the basis of new understanding or evidence. Minor changes in verbiage and references are discouraged. The ACC/AHA guidelines for exercise testing that were published in 1997 have now been updated. The full-text guidelines incorporating the updated material are available on the Internet (www.acc.org or www.americanheart.org) in both a version that shows the changes in the 1997 guidelines in strike-over (deleted text) and highlighting (new text) and a “clean” version that fully incorporates the changes. This article describes the 10 major areas of change reflected in the update in a format that we hope can be read and understood as a stand-alone document. The table of contents from the full-length guideline (see next page) indicates the location of these changes. Interested readers are referred to the full-length Internet version to completely understand the context of these changes. All new references appear in boldface type; all original references appear in normal type

The LYR Factors SDHAF1 and SDHAF3 Mediate Maturation of the Iron-Sulfur Subunit of Succinate Dehydrogenase

Disorders arising from impaired assembly of succinate dehydrogenase (SDH) result in a myriad of pathologies, consistent with its unique role in linking the citric acid cycle and electron transport chain. In spite of this critical function, however, only a few factors are known to be required for SDH assembly and function. We show here that two factors, Sdh6 (SDHAF1) and Sdh7 (SDHAF3), mediate maturation of the FeS cluster SDH subunit (Sdh2/SDHB). Yeast and Drosophila lacking SDHAF3 are impaired in SDH activity with reduced levels of Sdh2. Drosophila lacking the Sdh7 ortholog SDHAF3 are hypersensitive to oxidative stress and exhibit muscular and neuronal dysfunction. Yeast studies revealed that Sdh6 and Sdh7 act together to promote Sdh2 maturation by binding to a Sdh1/Sdh2 intermediate, protecting it from the deleterious effects of oxidants. These studies in yeast and Drosophila raise the possibility that SDHAF3 mutations may be associated with idiopathic SDH-associated diseases. [Display omitted] •SDH maturation is dependent on two Sdh2-specific assembly factors•Yeast cells lacking SDHAF1 and SDHAF3 are sensitive to endogenous oxidants•Drosophila lacking SDHAF3 exhibit muscular and neuronal dysfunction Na et al. show that maturation of the iron-sulfur cluster subunit (sdh2) of mitochondrial succinate dehydrogenase (which links the TCA cycle to the electron transport chain) is dependent on the assembly factors Sdh6 (SDHAF1) and Sdh7 (SDHAF3). These factors shield the sdh2 complex against endogenous oxidants during assembly

Modular Zwitterion-Functionalized Poly(Isopropyl Methacrylate) Polymers for Hosting Luminescent Lead-Halide Perovskite Nanocrystals

Inorganic lead-halide perovskite nanocrystals (NCs) are an exciting class of luminescent materials with high defect tolerance and broad spectral tunability, but such NCs are vulnerable to degradation under ambient conditions. Here, we report a class of modular zwitterion-functionalized isopropyl methacrylate polymers designed to stabilize a wide variety of perovskite NCs of different compositions, while also enabling processing in green solvents. Specifically, we report polymers in which the zwitterion spacing is tuned to accommodate the different lattice parameters of CsPb(Cl1-xBrx)3 and CsPbI3 NCs, and we report partially fluorinated polymers prepared to accommodate the needs of infrared-emitting NCs. We show that as-synthesized CsPbBr3, CsPbI3, and Yb3+:CsPbCl3 NCs are easily transferred into these zwitterionic polymers via a simple ligand-exchange procedure. These NC/polymer composites were then cast into thin films that showed substantially improved photoluminescence (PL) and stability compared with more conventional NC/polymer films. Specifically, CsPbBr3 and CsPbI3 NCs in films of their appropriately designed polymers had PL quantum yields of ~90% and ~80%, respectively. PL quantum yields decreased under continuous illumination, but self-healed completely after dark storage. We also found that all the NC compositions studied here maintain their PL quantum yields in NC/polymer composite films even after 1 year of ambient storage. These encouraging results demonstrate the utility of such modular zwitterion-functionalized polymers for hosting specific perovskite NCs, potentially opening avenues for robust new photonic applications of this important class of NCs

Glue Genes are Induced by 20E in Cultured Glands.

<p>Mid-L3 animals were torn in half and incubated with ethanol as a control (A), or with 20E at a final concentration of 10⁻⁸ M (B). The induction of glue proteins in the salivary glands was detected by the expression of a <i>GFP</i>-tagged <i>Sgs3</i> gene (<i>glueGRN</i>). Note that the positions of the salivary glands in (A) are outlined with dashed lines. The fluorescence detected in the pharynx (arrowheads) is non-specific and was used to standardize photographic exposures. Both photographs were taken at the same magnification indicated by the bar in A.</p