ABSTRACT
BACKGROUND: As nurses seek to advance their education through online courses, considering best practices in feedback is especially important. Rich and rapid feedback has long been considered a best teaching practice, but how to provide this feedback in an online course environment is not always clear. This study was conducted to identify how experienced faculty provide feedback to online students. METHODS: This descriptive exploratory study surveyed faculty about their approach to feedback with broad exploratory questions and a validation survey. The sample included faculty in four different states who benchmark online educational best practices. RESULTS: Content analysis was used to evaluate data, with 15 themes emerging. These themes were organized into three categories: using best available tools; having a system; and creating a feedback-rich environment. CONCLUSION: The findings support and extend the guidelines for best practices in online education, including a focus on multisource feedback opportunities during course design.
Subject(s)
Computer-Assisted Instruction/methods , Education, Nursing, Continuing/methods , Faculty, Nursing , Feedback, Psychological , Models, Educational , Benchmarking , Computer-Assisted Instruction/standards , Education, Nursing, Continuing/standards , HumansABSTRACT
The Ca(v)1.2 L-type Ca2+ channel is the dominant voltage-activated Ca2+ channel in heart and smooth muscle. The functional significance of this channel was studied in intestinal smooth muscle from mice carrying a smooth muscle-specific, conditional inactivation of the Ca(v)1.2 gene (Ca(v)1.2SMACKO mice). Inactivation was complete within 4 wk after tamoxifen treatment and confirmed by RT-PCR, Western blot and functional analysis. Ca(v)1.2SMACKO mice show reduced feces excretion, absence of rhythmic contractions in small and large intestinal muscle and signs of paralytic ileus. Extracellular field stimulation evoked smaller contractions in jejunum muscles from Ca(v)1.2SMACKO than from CTR mice, whereas carbachol-induced contractions of similar magnitude in both muscles. The Ca2+ needed for contraction in jejunum was provided mainly by Ca(v)1.2 channels and by store-operated channels in muscles from CTR and Ca(v)1.2SMACKO mice, respectively. In conclusion, the Ca(v)1.2 channel is essential for electromechanical coupling and important for pharmaco-mechanical coupling in intestinal smooth muscle and cannot be substituted functionally by other Ca2+ entry pathways.
Subject(s)
Calcium Channels, L-Type/physiology , Gastrointestinal Motility , Animals , Calcium Channels, L-Type/genetics , Carbachol/pharmacology , Cholinergic Agonists/pharmacology , Intestines/anatomy & histology , Intestines/drug effects , Intestines/physiology , Mice , Mice, Knockout , Muscle Contraction/drug effects , Muscle, Smooth/physiologyABSTRACT
The error in quantitative gel electrophoresis/Western blotting was investigated considering the purity testing of erythropoietin. The overall error was over 35% relative standard deviation. However, an analysis of variance elucidated that the interoperator variability was the dominant error source, which already explained almost 80% of the total variance. Careful compilation and investigation of the possible error sources strongly indicates that the immunoreaction after blotting and the subsequent color reaction are the major error sources in this case.
Subject(s)
Electrophoresis, Polyacrylamide Gel/methods , Analysis of Variance , Blotting, Western/methods , Blotting, Western/standards , Electrophoresis, Polyacrylamide Gel/standards , Erythropoietin/analysis , Erythropoietin/isolation & purification , Reproducibility of ResultsABSTRACT
Mice deficient in the smooth muscle Cav1.2 calcium channel (SMACKO, smooth muscle alpha1c-subunit calcium channel knockout) have a severely reduced micturition and an increased bladder mass. L-type calcium current, protein, and spontaneous contractile activity were absent in the bladder of SMACKO mice. K+ and carbachol (CCh)-induced contractions were reduced to 10-fold in detrusor muscles from SMACKO mice. The dihydropyridine isradipine inhibited K+- and CCh-induced contractions of muscles from CTR but had no effect in muscles from SMACKO mice. CCh-induced contraction was blocked by removing extracellular Ca2+ but was unaffected by the PLC inhibitor U73122 or depletion of intracellular Ca2+ stores by thapsigargin. In muscles from CTR and SMACKO mice, CCh-induced contraction was partially inhibited by the Rho-kinase inhibitor Y27632. These results show that the Cav1.2 Ca2+ channel is essential for normal bladder function. The Rho-kinase and Ca2+-release pathways cannot compensate the lack of the L-type Ca2+ channel.
Subject(s)
Calcium Channels, L-Type/physiology , Muscle, Smooth/drug effects , Urinary Bladder/physiology , Amides/pharmacology , Animals , Calcium/metabolism , Calcium Channels, L-Type/deficiency , Calcium Channels, L-Type/genetics , Carbachol/pharmacology , Enzyme Inhibitors/pharmacology , Estrenes/pharmacology , Intracellular Signaling Peptides and Proteins , Ion Channel Gating , Ion Transport/drug effects , Isradipine/pharmacology , Mice , Mice, Knockout , Muscle Contraction/drug effects , Muscle, Smooth/physiopathology , Patch-Clamp Techniques , Protein Serine-Threonine Kinases/antagonists & inhibitors , Protein Serine-Threonine Kinases/physiology , Pyridines/pharmacology , Pyrrolidinones/pharmacology , Receptors, Muscarinic/drug effects , Receptors, Muscarinic/physiology , Reverse Transcriptase Polymerase Chain Reaction , Thapsigargin/pharmacology , Urination Disorders/genetics , Urination Disorders/physiopathology , rho-Associated KinasesABSTRACT
The cGMP kinase signaling complex identified previously in tracheal smooth muscle membranes contains a number of cGMP kinase substrates termed G0 through G4. G0, G1, and G2 were identified as IP(3) receptor I (IP(3)RI), IRAG, and cGMP kinase I. Sequencing of purified G3 and G4 showed that these proteins were proteolytic cleavage products of IRAG. However, the purified cGMP kinase signaling complex contained following additional proteins: alpha-actin, calponin H1, and phospholamban (PLB) as verified by MALDI-TOF as well as MS/MS sequencing and immune detection. The complex of these six proteins was immune precipitated by antibodies to each protein. The proteins were phosphorylated by the endogenous cGMP kinase I with the exception of alpha-actin and calponin H1. The complex did not contain the Ca(2+)-ATPase SERCA II. PLB, IP(3)RI, and cGMP kinase Ibeta were co-immune precipitated after expression in COS-7 cells. These results suggest that PLB may have additional functions to regulate the activity of SERCA II.
