Active precepting in the residency clinic: a pilot study of a new model.

OBJECTIVE: This study's objective was to develop and implement a model of "active precepting" as a teaching and patient care quality improvement project at a community-based family medicine residency program. METHODS: The Prepare, Orchestrate, Educate, Review (POwER) model was developed with input from faculty, students, residents, and staff. Five measures of conformance to the model were monitored with daily feedback cards from November 2001 to February 2002. Faculty, residents, and clinic staff were surveyed and interviewed after the intervention for perceptions about active precepting. Two follow-up patient flow studies were completed for concomitant quality improvement efforts, and those findings were reviewed along with intervention findings. RESULTS: Preceptors reported reviewing resident schedules prior to clinic sessions more often after the model was put in place, and clinic staff reported that residents and faculty were more willing to help solve problems. Concurrent flow studies showed that patient time in clinic decreased from 110 minutes before the intervention to < 70 minutes after, while resident time with patients, including precepting time, decreased from 44 minutes to < 30 minutes. CONCLUSIONS: Our results point to the potential of the POwER model of active precepting to contribute to improved patient care, teaching, stakeholder satisfaction, and better flow in the family medicine teaching clinic.

Engineering the proteolytic specificity of activated protein C improves its pharmacological properties.

Human activated protein C (APC) is an antithrombotic, antiinflammatory serine protease that plays a central role in vascular homeostasis, and activated recombinant protein C, drotrecogin alfa (activated), has been shown to reduce mortality in patients with severe sepsis. Similar to other serine proteases, functional APC levels are regulated by the serine protease inhibitor family of proteins including alpha(1)-antitrypsin and protein C inhibitor. Using APC-substrate modeling, we designed and produced a number of derivatives with the goal of altering the proteolytic specificity of APC such that the variants exhibited resistance to inactivation by protein C inhibitor and alpha(1)-antitrypsin yet maintained their primary anticoagulant activity. Substitutions at Leu-194 were of particular interest, because they exhibited 4- to 6-fold reductions in the rate of inactivation in human plasma and substantially increased pharmacokinetic profiles compared with wild-type APC. This was achieved with minimal impairment of the anticoagulant/antithrombotic activity of APC. These data demonstrate the ability to selectively modulate substrate specificity and subsequently affect in vivo performance and suggest therapeutic opportunities for the use of protein C derivatives in disease states with elevated serine protease inhibitor levels.