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Blended learning, a combination of online and face-to-face classroom experiences, is of particular interest in health sciences education. Mayo School of Health Sciences, one of the five schools within the Mayo Clinic College of Medicine, assessed the use of blended learning across three allied health education programs: clinical neurophysiology, histology, and phlebotomy. The process involved analysis of the individual programs and the establishment of a philosophy to underpin the use of blended learning within the school. To evaluate the results of the redesigned blended phlebotomy program that was implemented in September 2012, we collected data on resource use, program accessibility, student performance, and student satisfaction. The results showed that the blended learning environment enhanced the overall course framework, by providing greater accessibility (geographically and temporally), and improved efficiency in the use of faculty, classroom and laboratory space; while maintaining strong student performance. Although student satisfaction decreased initially, program adjustments resulted in subsequent student cohorts reporting high satisfaction. We showed the utility of blended learning being adopted in health sciences programs traditionally delivered face-to-face and the value of technology used effectively in teaching and learning. ABBREVIATIONS:MSHS - Mayo School of Health Sciences, NAACLS - National Accrediting Agency for Clinical Laboratory Sciences

We have investigated the effects of PTH-induced desensitization on second messenger interactions in the rat osteosarcoma cell line ROS 17/2.8. Adenylate cyclase activation was assessed by accumulation of immunoassayable cAMP, and cytosolic calcium ion ([Ca2+]i) concentrations were measured in adherent perifused cells loaded with the Ca2(+)-sensitive bioluminescent protein aequorin. Preexposure to rat PTH-(1-34) [rPTH-(1-34); 10(-8) M for 48 h, then 10(-7) M for 24 h] dramatically reduced (by 85%) the cAMP response to fresh challenge [2 min; 10(-9)-10(-7) M rPTH-(1-34)], but the peak PTH-induced rise of [Ca2+]i was not diminished significantly (0-20%). Nevertheless, we did observe other changes in the PTH-induced [Ca2+]i response. Exposure of treated cells to (Bu)2cAMP nearly abolished the [Ca2+]i response to PTH (greater than 80% reduction), but had much less effect on the PTH-stimulated [Ca2+]i increment of the naive cells (less than 35% reduction). Treated cells also had a blunted [Ca2+]i response to PTH in the presence of low extracellular calcium (greater than 60% reduction), but in the naive cells, low extracellular Ca2+ did not significantly diminish the peak PTH-induced [Ca2+]i rise, although low extracellular Ca2+ dramatically reduced the area under this [Ca2+]i transient (greater than 50%). Low extracellular Ca2+ had no influence on the peak [Ca2+]i responses of treated cells to bradykinin or prostaglandin F2 alpha. Although the peak PTH-stimulated [Ca2+]i rise of treated cells in normal Ca2+ medium was not significantly attenuated, the time to half-maximum [Ca2+]i concentration was significantly increased (greater than 100%), and the area under the [Ca2+]i transient was diminished. These alterations in the [Ca2+]i response of treated cells were not observed upon challenge with bradykinin or prostaglandin F2 alpha. Thus, 1) the cAMP and [Ca2+]i responses of ROS 17/2.8 cells to rPTH-(1-34) are not obligatorily coupled; 2) the response of naive cells to PTH includes both the release of Ca2+ from intracellular stores and the entry of extracellular Ca2+; and 3) pretreatment of these cells with rPTH-(1-34) augments the dependence on Ca2+ entry during hormone rechallenge. We propose that the preserved PTH-stimulated [Ca2+]i rise in treated cells results partly from loss of cAMP-mediated inhibition of extracellular Ca2+ entry.

Plasma concentrations and 3H and 14C specific activities (specific radioactivities) of leucine and alpha-ketoisocaproate (KIC) and leucine specific radioactivity in hydrolyzed tissue and plasma proteins were determined using an automated isocratic high-performance liquid chromatographic (HPLC) system. Within-day variability of leucine and KIC specific radioactivity in plasma was congruent to 1%, whereas that observed for leucine derived from protein hydrolysis was congruent to 5%. Day-to-day variability of leucine and KIC specific radioactivity in plasma was congruent to 5% and in protein-derived leucine congruent to 6%. In addition, an indirect method is described to measure low specific activities of [3H]- and [14C]leucine derived from the hydrolysis of in vivo labeled proteins with low turnover rates (skeletal muscle and diaphragm). In proteins with higher turnover rates (fibrin, kidney, liver, jejunum and heart muscle), this indirect method gave similar results to the direct HPLC method. Using these methods, fractional protein synthetic rates in a variety of tissues can be accurately determined using radioisotopes of KIC and/or leucine.