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1.
Environ Int ; 34(3): 412-9, 2008 Apr.
Article in English | MEDLINE | ID: mdl-17961649

ABSTRACT

The occurrence of the major components of the decabromodiphenyl ether (deca-BDE) flame retardant and other PBDEs was investigated in daily air particulate samples from 17th April to 20th May 2004 at a semi-rural site in north-west England. BDE-209 was found at between <0.49 and 100 pg m(-3) (median 13 pg m(-3)), and other higher-brominated PBDE congeners were also found, particularly the nona-BDEs (e.g. BDE-207: <0.042-79 pg m(-3), median 2.5 pg m(-3)). Deca- and nona-BDEs dominated the median particulate sample congener profile: 60% BDE-209, 16% BDE-207, 6% BDE-208 and 4% BDE-206. Nona-BDEs were greatly enriched, relative to BDE-209, compared to the deca-BDE commercial mixture, which may suggest degradation of BDE-209 between source and sampling site, or release from older deca-BDE commercial mixtures, which may have contained higher proportions of nona-BDEs. The highest PBDE concentrations occurred when air-masses passed over urban and industrial areas to the SSW-SW, though small local influences may also be seen. PBDE concentrations appear to have been influenced mainly by particle levels: 1-3 microm diameter particles for BDE-153, and 3-10 microm particles for BDEs with 7-10 Br atoms. BDE-153 may either be released from combustion sources, or re-condense onto small particles after emission, whereas BDE-209 and nona-BDEs appear to be associated with larger dust particles from industrial or domestic sources.


Subject(s)
Air Pollution , Particulate Matter/chemistry , Phenyl Ethers/analysis , Polybrominated Biphenyls/analysis , Air Movements , England , Environmental Monitoring , Flame Retardants/analysis , Halogenated Diphenyl Ethers
2.
Peptides ; 28(1): 153-62, 2007 Jan.
Article in English | MEDLINE | ID: mdl-17157962

ABSTRACT

Insect angiotensin converting enzyme (ACE) is a zinc metallopeptidase capable of inactivating a variety of small to medium size peptide hormones by cleavage of C-terminal dipeptides and dipeptideamides. High levels of ACE activity are found in the hemolymph and in reproductive tissues of insects, where the enzyme is considered to have an important role in the metabolism of bioactive peptides. Therefore, inhibiting ACE activity is expected to interfere with the peptidergic endocrine system and to have detrimental effects on growth, development and reproduction. We will review the studies showing that ACE inhibitors do indeed disrupt growth and reproduction in various insect species. We will also present some new genetic and pharmacological data that strengthens our conclusion that ACE should be considered as a potential target for the development of new insect growth regulators.


Subject(s)
Drug Design , Juvenile Hormones/pharmacology , Peptidyl-Dipeptidase A/metabolism , Angiotensin-Converting Enzyme Inhibitors/pharmacology , Animals , Female , Insecta/drug effects , Insecta/genetics , Insecta/growth & development , Male , Peptidyl-Dipeptidase A/genetics , Phylogeny , Reproduction/drug effects
3.
Crit Care Nurs Clin North Am ; 18(4): 469-79, ix, 2006 Dec.
Article in English | MEDLINE | ID: mdl-17118301

ABSTRACT

The Institute of Medicine identifies quality health care as care that is safe, time, effective, efficient, equitable, and patient centered. In the ICU, where patients who have complex, high-acuity are at increased risk of complications, morbidity, and mortality, promoting quality-focused case is especially important. This article describes several performance-improvement initiatives that were developed and implemented a Midwestern community hospital during a 4-year period. The initiatives to reduce catheter-associated blood stream infections, to identify early sepsis, and to promote evidence-based care.


Subject(s)
Critical Care/organization & administration , Infection Control/organization & administration , Outcome and Process Assessment, Health Care/organization & administration , Quality Assurance, Health Care/organization & administration , Total Quality Management/organization & administration , Benchmarking/organization & administration , Catheterization, Central Venous/adverse effects , Catheterization, Peripheral/adverse effects , Evidence-Based Medicine , Health Services Needs and Demand , Hospitals, Community , Humans , Midwestern United States , Nurse's Role , Nursing Evaluation Research , Nursing Records , Nursing Staff, Hospital/education , Nursing Staff, Hospital/organization & administration , Nursing Staff, Hospital/psychology , Personnel Turnover , Pneumonia, Ventilator-Associated/prevention & control , Practice Guidelines as Topic , Program Development , Program Evaluation , Sepsis/diagnosis , Sepsis/etiology , Sepsis/prevention & control
4.
Dev Biol ; 254(2): 238-47, 2003 Feb 15.
Article in English | MEDLINE | ID: mdl-12591244

ABSTRACT

The Angiotensin-converting enzyme (Ance) gene of Drosophila melanogaster is a homologue of mammalian angiotensin-converting enzyme (ACE), a peptidyl dipeptidase implicated in regulation of blood pressure and male fertility. In Drosophila, Ance protein is present in vesicular structures within spermatocytes and immature spermatids. It is also present within the lumen of the testis and the waste bag, and is associated with the surface of elongated spermatid bundles. Ance mRNA is found mainly in large primary spermatocytes and is not detectable in cyst cells. Testes lacking germ cells have reduced levels of ACE activity, and no Ance protein is detectable by immunocytochemistry, indicating that the germ cells are the major site of Ance synthesis. Ance mutant testes lack individualised sperm and have very few actin-based individualisation complexes. Spermatid nuclei undergo scattering along the cyst and have abnormal morphology, similar to other individualisation mutants. Mutant spermatids also have abnormal ultrastructure with grossly defective mitochondrial derivatives. The failure of Ance mutant testes to form individualisation complexes may be due to a failure in correct spermatid differentiation. Taken together, the expression pattern and mutant phenotype suggest that Ance is required for spermatid differentiation, probably through the processing of a regulatory peptide synthesised within the developing cyst.


Subject(s)
Drosophila Proteins/physiology , Metalloendopeptidases/physiology , Spermatogenesis , Animals , Drosophila melanogaster , Male , Metalloendopeptidases/analysis , Metalloendopeptidases/genetics , Mutation , Peptidyl-Dipeptidase A , Testis/enzymology
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