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Describes a module in which students seek to gain an understanding of factors that interact in the ecological system of their school. Presents sample questions for use in reinforcing concepts and evaluating student learning, directions for four task activities, and topics for some of the remaining task activities. (RT)

The treatment of mental illness is often done on a trial-and-error basis and achieving therapeutic benefits from a medication is not always guaranteed. Pharmacogenomics explores the role of gene–gene interactions and interindividual responses to a drug and may be promising in the guidance of pharmacotherapeutic options. In the present study, the impact of pharmacogenomic testing in management of mental health medication was investigated. Participants were identified at a local outpatient mental health facility through convenience sampling. Retrospective chart review included medication history, adverse drug reactions, pharmacogenomic history, and demographic data including insurance coverage. Chart review focused on six months pre- and post-pharmacogenomic for a comparison with the patient serving as their own control. Results indicate a high incidence of alterations in two specific cytochrome enzymes, CYP2D6 and CYP2C19. In total, 82% of the sample had variations with CYP2D6, while 64% of individuals had variations with CYP2C19. In total, 91% of patients tested received Medicaid or Medicare. Post-pharmacogenomic testing, all patient drug regimens were modified, and all reported less adverse side effects. Moreover, advanced practice nurse providers educated patients about the availability of genetic testing, initiated testing and provided care based on findings. These results demonstrate the utility of genetic testing in the realm of mental health. Future directions involve further exploring the benefits of pharmacogenomic testing in this vulnerable population. [ABSTRACT FROM AUTHOR]

The Nucleotide Axis Hypothesis, defined and supported herein, proposes that ATP stimulates the release of vasoactive mediators from endothelium, including ATP itself. Here, we show rapid endothelium-dependent, agonist-stimulated ATP elaboration in coronary vessels of guinea pigs. Measurement of extracellular ADP metabolism in intact vessels results in the time- and substrate-dependent formation of ATP in the coronary perfusate in amounts greater than can be accounted for by release from endothelium alone. ATP formation by endothelial cells is saturable ([K.sub.M] = 38.5 [micro]mol/l, where [K.sub.M] is substrate concentration at which rate is half-maximal.) and trypsin-sensitive, membranes from [[Gamma]-.sup.32] P]ATP-labeled cells support ADP-dependent transphosphorylation by a 20-kDa protein, Western blots reveal the presence of a nucleoside diphosphate kinase (NDPK) of ~20 kDa in endothelial membranes, and analysis of NDPK antibody binding by flow cytometry is consistent with the presence of an ecto-NDPK on cardiac endothelial cells. Sequencing of the endothelial cell ecto-NDPK reveals a predicted amino acid sequence with 85% identity to human Nm23-H1 and consistent with a protein whose properties may confer membrane association as well as sites of regulation of activity. Our data underscore the potential importance of a nucleotide axis in cardiac blood vessels. release of vasoactive factors; ectoenzyme; ecto-Nm23

Angiostatin blocks tumor angiogenesis in vivo, almost certainly through its demonstrated ability to block endothelial cell migration and proliferation. Although the mechanism of angiostatin action remains unknown, identification of [F.sub.1]-[F.sub.0] ATP synthase as the major angiostatin-binding site on the endothelial cell surface suggests that ATP metabolism may play a role in the angiostatin response. Previous studies noting the presence of [F.sub.1] ATP synthase subunits on endothelial cells and certain cancer cells did not determine whether this enzyme was functional in ATP synthesis. We now demonstrate that all components of the [F.sub.1] ATP synthase catalytic core are present on the endothelial cell surface, where they colocalize into discrete punctate structures. The surfaceassociated enzyme is active in ATP synthesis as shown by dual-label TLC and bioluminescence assays. Both ATP synthase and ATPase activities of the enzyme are inhibited by angiostatin as well as by antibodies directed against the [Alpha]- and [Beta]-subunits of ATP synthase in cell-based and biochemical assays. Our data suggest that angiostatin inhibits vascularization by suppression of endothelialsurface ATP metabolism, which, in turn, may regulate vascular physiology by established mechanisms. We now have shown that antibodies directed against subunits of ATP synthase exhibit endothelial cell-inhibitory activities comparable to that of angiostatin, indicating that these antibodies function as angiostatin mimetics.