Pharmacy and Pharmaceutical Sciences Commons^™

Measured Energy Expenditure Of Tube-Fed Patients With Severe Neurodevelopment Disabilities, Roland N. Dickerson, Rex O. Brown, Jane M. Gervasio, Emily B. Hak, Lawrence J. Hak, John E. Williams

Scholarship and Professional Work – COPHS

Objective: To determine measured resting energy expenditure (REE) of nonambulatory tube-fed patients with severe neurological neurodevelopmental disabilities.

Methods: Twenty patients were prospectively studied. Only steady state indirect calorimetry measurements were taken. All measurements were conducted using a canopy system. Nutritional needs were met entirely by enteral feedings via a permanent ostomy.

Results: REE was widely distributed from 16 kcals/kg/day to 39 kcals/kg/day. The mean REE (888 ±176 kcals/day) of the patients was significantly (p < 0.01) lower than predicted as estimated by the Harris-Benedict equations (1081 ± 155 kcals/day) and World Health Organization equations (1194 ± 167 kcals/day). Fat-free mass (FFM) was the best parameter for predicting REE. Two predictive equations were developed that are not significantly biased and more precise (≤ 15% error) than conventional predictive formulas.

Conclusion: Conventional formulas for estimating energy expenditure are inaccurate and generally overestimate measured energy expenditure of nonambulatory patients with severe developmental …

Cooperative Binding Of Heat Shock Factor To The Yeast Hsp82 Promoter In Vivo And In Vitro, Alexander M. Erkine, Serena F. Magrogan, Edward A. Sekinger, David S. Gross

Scholarship and Professional Work – COPHS

revious work has shown that heat shock factor (HSF) plays a central role in remodeling the chromatin structure of the yeastHSP82 promoter via constitutive interactions with its high-affinity binding site, heat shock element 1 (HSE1). The HSF-HSE1 interaction is also critical for stimulating both basal (noninduced) and induced transcription. By contrast, the function of the adjacent, inducibly occupied HSE2 and -3 is unknown. In this study, we examined the consequences of mutations in HSE1, HSE2, and HSE3 on HSF binding and transactivation. We provide evidence that in vivo, HSF binds to these three sites cooperatively. This cooperativity is seen …