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Search indexed NASA NTRS and DOE OSTI research on propulsion, heat transfer, battery materials and energy systems. Follow report and document links to the original sources.

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At least 1,081 records · Page 60
All sourcesNASA NTRSDOE OSTI
DOE OSTI2019

The need for standardization of nuclear cardiology reporting and data system (NCAD-RADS): Learning from coronary artery disease (CAD), breast imaging (BI), liver imaging (LI), and prostate imaging (PI) RADS

Newer structured reporting manners, the reporting and data system (RADS), have made vast steps in improving standardized and structured reporting, allowing better communication between radiologists and referring providers. This has been implemented in several fields: breast (BI-RADS), lung (Lung-RADS), liver (LI-RADS), thyroid (TI-RADS), prostate (PI-RADS), and in cardiovascular radiology (CAD-RADS). The field of nuclear cardiology began its efforts of standardization years ago; however, a widespread standardized reporting structure has not yet been adopted. Such an approach in nuclear cardiology, the nuclear cardiology reporting and data system (NCAD-RADS), will assist radiologists and treating clinicians in conveying and understanding reports and determining the appropriate next steps in management. By linking explicit findings to defined recommendations, patients will receive more consistent and appropriate care.

62 RADIOLOGY AND NUCLEAR MEDICINE↗
DOE OSTI2014

Crystal structure of cathepsin A, a novel target for the treatment of cardiovascular diseases

Graphical abstract: - Highlights: • The structures of active cathepsin A and the inactive precursor are very similar. • The only major difference is the absence of a 40 residue activation domain. • The termini of the active catalytic core are held together by a disulfide bond. • Compound 1 reacts with the catalytic Ser150, building a tetrahedral intermediate. • Compound 2 is cleaved by the enzyme and a fragment remained bound. - Abstract: The lysosomal serine carboxypeptidase cathepsin A is involved in the breakdown of peptide hormones like endothelin and bradykinin. Recent pharmacological studies with cathepsin A inhibitors in rodents showed a remarkable reduction in cardiac hypertrophy and atrial fibrillation, making cathepsin A a promising target for the treatment of heart failure. Here we describe the crystal structures of activated cathepsin A without inhibitor and with two compounds that mimic the tetrahedral intermediate and the reaction product, respectively. The structure of activated cathepsin A turned out to be very similar to the structure of the inactive precursor. The only difference was the removal of a 40 residue activation domain, partially due to proteolytic removal of the activation peptide, and partially by an order–disorder transition of the peptides flanking the removed activation peptide. The termini of the catalytic core are held together by the Cys253–Cys303 disulfide bond, just before and after the activation domain. One of the compounds we soaked in our crystals reacted covalently with the catalytic Ser150 and formed a tetrahedral intermediate. The other compound got cleaved by the enzyme and a fragment, resembling one of the natural reaction products, was found in the active site. These studies establish cathepsin A as a classical serine proteinase with a well-defined oxyanion hole. The carboxylate group of the cleavage product is bound by a hydrogen-bonding network involving one aspartate and two glutamate side chains. This network can only form if at least half of the carboxylate groups involved are protonated, which explains the acidic pH optimum of the enzyme.

60 APPLIED LIFE SCIENCES↗
DOE OSTI2018

Spermidine ameliorates non-alcoholic fatty liver disease through regulating lipid metabolism via AMPK

Highlights: • Spermidine ameliorates high-fat diet-induced body weight increase. • Spermidine improves glucose tolerance and insulin sensitivity. • Spermidine ameliorates high-fat diet-induced hepatic steatosis. • Spermidine inhibits the expression of lipogenic genes dependent on AMPK. In this study, treatment of high-fat diet-induced obesity (DIO) C57BL/6J mice with spermidine decreased body weight and subcutaneous and visceral fat content, reversed the apparent hepatosteatosis, and reduced hepatic intracellular and serum triglyceride and total cholesterol concentrations. Moreover, spermidine treatment improved glucose tolerance and insulin sensitivity in DIO mice. The mechanism studies indicated that spermidine indeed increased the phosphorylation of hepatic AMP-activated protein kinase (AMPK), and inhibited the expression of lipogenic genes in vivo and in vitro. Moreover, these spermidine-mediated molecular effects were also abolished by compound C, an inhibitor of AMPK, in primary hepatocytes. In summary, spermidine protected against DIO-induced hepatosteatosis by decreasing lipogenic genes expression through an AMPK-mediated mechanism.

60 APPLIED LIFE SCIENCES↗