Implementing the Medicare drug benefit in a diverse inner-city community.

PURPOSE: An integrated effort to maintain continued access to pharmacy services and prescribed medications for patients in an inner-city community before and during the implementation of the Medicare prescription drug benefit is described. SUMMARY: An academic medical center and college of pharmacy in a culturally diverse, inner-city Chicago community created a strategy to provide uninterrupted pharmacy services to all of their Medicare Part D eligible patients, particularly those dual eligible for Medicaid and Medicare, during the transition from Medicaid to Medicare Part D, effective January 1, 2006. The percentage of dual-eligible patients in the Medicare Part D eligible population at the institution was more than twice the national average. A task force was created to prepare for the onset of Medicare Part D. The task force had goals in three areas: education, outreach, and operations; it was also responsible for the development of a contingency plan for any problems that could happen after January 1. A Medicare drug benefit consult service was formed to ensure that Medicare eligible patients understood the Medicare drug benefit and received customized assistance. Although problems were encountered, the investment in the preparation and implementation of the Medicare drug benefit, especially the consult service, resulted in a positive return on the institution's investment. Suggestions for other institutions facing the challenge of the implementation of the Medicare drug benefit are provided. CONCLUSION: Implementing a federal-level program among a diverse subset of patients is challenging and requires concerted efforts from health care providers and support from the institution. The Medicare drug benefit task force at the institution assumed responsibility for all pharmacy activities related to Medicare Part D and achieved its goals in education, outreach, and operations. This resulted in continued access to pharmacy services and prescribed medications for patients.

The SANT2 domain of the murine tumor cell DnaJ-like protein 1 human homologue interacts with alpha1-antichymotrypsin and kinetically interferes with its serpin inhibitory activity.

The murine tumor cell DnaJ-like protein 1 or MTJ1/ERdj1 is a membrane J-domain protein enriched in microsomal and nuclear fractions. We previously showed that its lumenal J-domain stimulates the ATPase activity of the molecular chaperone BiP/GRP78 (Chevalier, M., Rhee, H., Elguindi, E. C., and Blond, S. Y. (2000) J. Biol. Chem. 275, 19620-19627). MTJ1/ERdj1 also contains a large carboxyl-terminal cytosolic extension composed of two tryptophan-mediated repeats or SANT domains for which the function(s) is unknown. Here we describe the cloning of the human homologue HTJ1 and its interaction with alpha(1)-antichymotrypsin (ACT), a member of the serine proteinase inhibitor (serpin) family. The interaction was initially identified in a two-hybrid screening and further confirmed in vitro by dot blots, native electrophoresis, and fluorescence studies. The second SANT domain of HTJ1 (SANT2) was found to be sufficient for binding to ACT, both in yeast and in vitro. Single tryptophan-alanine substitutions at two strictly conserved residues significantly (Trp-497) or totally (Trp-520) abolished the interaction with ACT. SANT2 binds to human ACT with an intrinsic affinity equal to 0.5 nm. Preincubation of ACT with nearly stoichiometric concentrations of SANT2 wild-type but not SANT2: W520A results in an apparent loss of ACT inhibitory activity toward chymotrypsin. Kinetic analysis indicates that the formation of the covalent inhibitory complex ACT-chymotrypsin is significantly delayed in the presence of SANT2 with no change on the catalytic efficiency of the enzyme. This work demonstrates for the first time that the SANT2 domain of MTJ1/HTJ1/ERdj1 mediates stable and high affinity protein-protein interactions.