Enhancing the quality of life and preserving independence for target needs populations through integration of assistive technology devices.

Telehealth Test Bed-Quality of Life Studies is a research study investigating, testing, evaluating, and demonstrating technologies that have the potential to improve the quality of life for target populations, such as warriors in transition, veterans, individuals with physical and mental disabilities, and adults age 65 and older, who may require assistive technology devices to aid in maintaining or improving their quality of life. Thousands of soldiers who fought in Operation Iraqi Freedom and Operation Enduring Freedom have been wounded in action or have sustained injuries from noncombat accidents. Many of these injuries affecting military populations, as well as the general public, have resulted in amputations, traumatic brain injuries, and other physical or mental impairments. Depending on the severity of the injury, assistive technologies may be temporarily needed, or as a long-term solution, to regain and maintain normal daily functions. Saint Francis University's Center of Excellence for Remote and Medically Under-Served Areas developed an evaluation matrix comparing assistive technologies to identify devices that will improve or maintain the quality of life for these target populations. The integration of telehealth and telerehabilitation applications into patients' daily lives was examined to help improve home rehabilitation via access to healthcare specialties in rural and medically underserved settings. Researchers identified and tested assistive technology devices to be included in a self-sufficient living environment. The continuation of this research involves recruiting individuals to test and evaluate the functions of these commercially available technologies and to complete data collection surveys and questionnaires. The results are useful in selecting devices that will enhance or extend the quality of life of the target populations.

Full-length estrogen receptor alpha and its ligand-binding domain adopt different conformations upon binding ligand.

The binding of ligand to a nuclear receptor causes conformational changes that can result in coactivator or corepressor recruitment and subsequent regulation of transcription. Several peptides have previously been identified that bind to the liganded estrogen receptor (ER). One interacting peptide, pepalphaII, was used in the present studies to assess the ability of ligands to induce spatial changes within both the full-length human estrogen receptor alpha (ER-alpha) and a truncated receptor containing the ligand-binding domain (LBD). pepalphaII interacted weakly with the full-length estrogen receptor alpha in the presence of both agonists and antagonists. In contrast, the interaction of pepalphaII with the truncated receptor containing the ligand-binding domain was strongly induced by antagonists and only weakly induced by agonists. Thus, the same ligand can induce different spatial configurations of the full-length and ligand-binding domain of estrogen receptor alpha as measured by pepalphaII affinity. Crystal structures of nuclear hormone receptors solved to date have used ligand-binding domains and therefore may not accurately predict surface interaction domains present in the liganded full-length receptor. Furthermore, the ability of a ligand to induce a strong interaction of pepalphaII with the estrogen receptor alpha ligand-binding domain predicts that the ligand will have greater antagonist activity on the full-length receptor.

The ligand binding profiles of estrogen receptors alpha and beta are species dependent.

Estrogens and selective estrogen receptor modulators are used for the treatment and prevention of conditions resulting from menopause. Since estrogens exert their activity by binding to nuclear receptors, there is intense interest in developing new ligands for the two known estrogen receptor subtypes, ER-alpha and ER-beta. Characterization assays used to profile new estrogen receptor ligands often utilize receptors from different species, with the assumption that they behave identically. To test this belief, we have profiled a number of estrogens, other steroids, phytoestrogens and selective estrogen receptor modulators in a solid phase radioligand binding assay using recombinant protein for human, rat, and mouse ER-alpha and ER-beta. Certain compounds show species dependent binding preferences for ER-alpha or ER-beta, leading to differences in receptor subtype selectivity. The amino acids identified by crystallography as lining the ligand binding cavity are the same among the three species, suggesting that as yet unidentified amino acids contribute to the structure of the binding site. We conclude from this analysis that the ability of a compound to selectively bind to a particular ER subtype can be species dependent.