Session presented on Friday， July 25， 2014： Purpose： Perioperative Nurse Managers are an integral part of the administration of quality health care， performing an array of clinical， financial， and leadership roles. The focus of this research is to improve the human and social conditions of the Perioperative Nurse Managers. Perioperative Nurse Managers lack the available resources to effectively cope with role demands on a daily basis. Lack of resources has led to decreased work engagement， job dissatisfaction， frustration， and ultimately attrition. The Job Demands-Resource Model provides a conceptual framework to increase work engagement， motivation， and organizational outcomes. Methods： qualitative case study design was employed to investigate， from the perspective of Perioperative Nurse Managers， how to manage job demands and identify viable resources to increase motivation and prevent burnout. The sample consisted of ten Perioperative Nurse Managers who were interviewed utilizing a pre-established Nurse Manager Engagement Questionnaire (NMEQ) to better understand the experiences of this group of individuals. Data was transcribed and coded， using elements of the conceptual framework and research questions， to determine common themes to help implement new work and social strategies. Results： Eight out of ten of the participants indicated a lack of formal leadership training， which was never provided in either their educational curricula or was limited within the institution. Other themes emerged including a lack of role clarity， being overtasked on a daily basis， and the desire for motivation through positive verbal feedback. Conclusion： In order to prevent burnout of Perioperative Nurse Managers， roles need to clearly be delineated and appropriately delegated to decrease overtasking. Positive feedback from providers， patients， and staff members must be encouraged and embraced by upper administration to assist in motivating the Perioperative Nurse Managers. Formal and informal leadership training is an imperative aspect of professional development that must be fostered to increase motivation and work engagement， and prevent burnout.
Analysis of cardiac muscarinic receptors recognized selectively by nonquaternary but not by quaternary ligands.
Abstract Three muscarinic receptor antagonists， [3H]quinuclidinyl benzilate ([3H]QNB)， N-[3H]methylscopolamine ([3H]NMS and N-[methyl-3H]QNB ([3H]NMeQNB)， each bind to an apparently homogeneous population of receptors on intact chick heart cells. [3H]QNB binds to approximately 9500 sites/cells， whereas [3H]NMS and [3H]NMeQNB bind to approximately 5000 sites/cell. Atropine and scopolamine compete with all three radioligands with a single， high affinity. Their quaternary analogs N-methylatropine and NMS and the quaternary agonist carbachol also show a single affinity for [3H]NMS and [3H]NMeQNB binding sites， but have biphasic competition curves for [3H]QNB sites with low "apparent" affinity for a subpopulation of sites. When 10 nM or greater propylbenzilylcholine mustard is used to alkylate receptors virtually all [3H]NMS binding is abolished， whereas [3H]QNB still labels a significant fraction of the binding sites seen in control cells. The sites with low apparent affinity for quaternary ligands are shown to have characteristics of muscarinic receptors， but do not appear necessary for muscarinic receptor-mediated phosphoinositide hydrolysis. We suggest that a subpopulation of nonfunctional muscarinic receptors are sequestered within the membrane or otherwise inaccessible to hydrophilic or charged ligands.
Influence of ligand choice on the apparent binding profile of gallamine to cardiac muscarinic receptors. Identification of three main types of gallamine-muscarinic receptor interactions.
The binding profile of the positively charged muscarinic antagonist， gallamine， was studied in rat heart homogenates. A proportion of the binding sites labeled by the tertiary muscarinic ligands [( 3H]quinuclidinyl benzilate (QNB) and [3H]atropine) were inaccessible to their quaternary analogs [( 3H]N-methyl-QNB (NMeQNB) and [3H]-N-methylscopolamine (NMS)] or gallamine. Whereas gallamine displaced the binding of [3H]NMeQNB with high affinity， biphasic competition curves were observed using [3H]NMS only at higher ligand concentrations. The rank order of potency of gallamine in allosterically decelerating ligand dissociation kinetics was： [3H]NMS greater than [3H]atropine greater than [3H]NMeQNB greater than [3H]QNB. Our calculations demonstrate that the displayed heterogeneity of gallamine binding sites detected using [3H]NMS， but not the tertiary ligands， might be accounted for by the allosteric modification of the binding of this ligand by gallamine. Based on these findings， the exhibited binding profile of gallamine to muscarinic receptors is influenced strongly by ligand choice， and also by the ligand concentration used in the binding experiment. Furthermore， it is concluded that gallamine binds to three major sites on the muscarinic receptor， thereby revealing an apparent heterogeneity of its binding sites， even in a tissue which presumably possesses one major muscarinic receptor subtype such as the heart. According to several lines of evidence， gallamine binds competitively and with high affinity to NMS-accessible sites on the receptor. Under certain experimental conditions， it also appears to identify another low-affinity site， either due to its binding to NMS-inaccessible sites or through its differential ability to alter the binding of ligands to the main binding domain on the receptor in an allosteric fashion.
正 高安氏病(Takayau's disease)是一种主动脉弓及大动脉的慢性进行性炎症性疾病，比较少见.笔者遇1例，特报道如下.患者女性，31岁，已婚，农民，因右眼视物不清10天，71989年6月14日入院.无红痛及外伤史.3年前曾发现上胶血压测不出，并有昏厥史，个人史及家族史无特殊.
Hypothyroidism inhibits the formation of inositol phosphate in response to carbachol in the striatum of adult rat.
ABSTRACT The effects of hypothyroidism on the muscarinic cholinergic receptor-coupled inositol phospholipid hydrolysis in the adult rat brain were examined. Tissue slices of striatum， hippocampus， and cortex from either euthyroid or hypothyroid rats were labeled with [3H]myoinositol and incubated with carbachol， a muscarinic cholinergic agonist. In other experiments， crude plasma membranes of each brain region obtained from either euthyroid or hypothyroid rats were incubated with [3H]N-methylquinuclidinyl benzilate ([3H]NMeQNB)， a muscarinic cholinergic antagonist， in the presence or absence of atropine. Carbachol produced a significant increase in [3H]inositol phosphate ([3H]IP) formation in each brain region in a dose dependent manner. Hypothyroidism caused a marked decrease in carbachol-stimulated [3H]IP formation in the striatum， whereas it did not affect the formation of [3H]IP in the cortex or hippocampus. In contrast， the affinity constant and the maximal binding of [3H]NMeQNB to plasma membranes in these regions were not changed by hypothyroidism. The present results suggest that thyroid hormones might participate in regulating the muscarinic cholinergic neurotransmission in the striatum of adult rat.
1. Muscarinic receptors on endothelial cells of bovine thoracic aorta were characterized by binding assays in which (-)-[3H]-N-methyl quinuclidinyl benzilate ([3H]-NMeQNB) was used as radioligand. 2. Binding of [3H]-NMeQNB to crude membranes of freshly isolated endothelial cells was atropine-displaceable and of high affinity (KD = 0.48 nM) to a single class of sites (maximum binding capacity： 14 +/- 3 fmol mg-1 protein). Stereospecificity of the binding sites was demonstrated in experiments in which [3H]-NMeQNB binding was inhibited by dexetimide in the nanomolar range (KI = 0.63 nM) and by levetimide， its stereoisomer in the micromolar range (KI = 3.2 microM) (selectivity factor： approximately 5000). 3. Drug competition curves indicated a single class of binding sites for antagonists and the following apparent affinities (KI， nM)： methyl atropine： 1.1： 4-diphenylacetoxy N-methyl piperidine methyl bromide (4-DAMP)： 3.4; pirenzepine： 16; 11-[2-diethylamino-methyl)-1-piperidinyl- acetyl]-5，11-dihydro-6H-pyrido(2，3-b)1，4-benzodiazepine-6-one (AF-DX 116); 2.500. Competition of acetylcholine with [3H]-NMeQNB was best described by two affinity sites (or states) (KH = 0.82 microM， KL = 1.6 microM). In the presence of guanylimido diphosphate [Gpp(NH)p] (100 microM)， acetylcholine affinity (IC50) was slightly， but significantly reduced (factor approximately 4). 4. Binding of [3H]-NMeQNB to freshly harvested intact cells was also atropine-displaceable， stereospecific (selectivity factor： approximately 3500) and of high affinity (KD = 0.35 nM). The maximum binding capacity (9 +/- 2 fmol mg-1 total cell protein) was comparable to that of membranes and corresponded to approximately 900 binding sites per endothelial cell. Binding to enzymatically harvested and cultured endothelial cells， or membranes derived therefrom， showed no atropine-displaceable binding. 5. The results suggest that (1) bovine aortic endothelial cells contain muscarinic binding sites with all necessary criteria of functional muscarinic receptors; (2) the receptor most closely corresponds to the M1 subtype and is of comparatively very low density， and (3) cultured endothelial cells lose their receptors during isolation or culture procedures.