Molecular chaperones are well known for their role in facilitating the folding of nascent and newly synthesized proteins, but have other roles, including the assembly, translocation and renaturation of intracellular proteins. Axons are convenient tissues for the study of some of these other roles because they lack the capacity for significant protein synthesis. We examine the axonal transport of the cytosolic chaperonin containing T- complex polypeptide 1 (CCT) by labeling lumbar motor neurons with [35S]methionine and examining sciatic nerve proteins by 2-D gel electrophoresis and immunoblotting. All CCT subunits identifiable with specific antibodies, namely CCTalpha, CCTbeta, CCTgamma and CCTepsilon/CCTtheta; (the latter two subunits colocalized in analyses of rat nerve samples), appeared to be labeled in "slow component b" of axonal transport along with the molecular chaperone Hsc73 and actin, a major folding substrate for CCT. Our results are consistent with molecular chaperones having a post-translational role in maintaining the native form of actin during its slow transport to the axon terminal and ensuring its correct assembly into microfilaments.
As COVID-19 hospital admissions rose in 2020, there was a requirement to prepare wards and staff to care for COVID-19 patients, especially given the rapidly emerging and frequently evolving guidance, and high levels of re-deployment (GMC, 2020). In one London Trust, this need for educational material geared towards ward staff resulted in a multi-disciplinary simulation education team being commissioned to produce an e-learning resource. We measured the effectiveness of the resource for ward staff as well as any improvement in learners’ COVID-19 knowledge.The aim of the study was to quantify the effectiveness of an e-learning package in improving learners’ COVID-19 knowledge.In November 2020, an e-learning package was created, comprising a video series documenting the journey of a patient with COVID-19 covering admission to discharge (filmed from the patient perspective). This was integrated with content highlighting key aspects of COVID-19 care, ending with a mandatory assessment with an 80% pass mark. The e-learning was disseminated to hospital staff (doctors, nurses and allied healthcare professionals) with data collection via SurveyMonkey® from November 2020 for 3 months. Pre- and post-surveys were included to investigate the average improvement of learners and the impact of the resource on learner self-efficacy through self-rating on six learning outcomes. Free-text options in the post-survey allowed qualitative feedback, aiding continual resource development.In total, 108 learners, about half of whom were doctors, completed both surveys, with a significant difference (p < 0.01) between the pre- and post-learning results and an overall improvement in learners’ knowledge after completion of the e-learning (Average pre- and post-learning scores of learners’ self-reported knowledge and percentage improvement*Treatment escalation plans.E-learning can rapidly disseminate learning, at a time when most feel the pandemic has had a mixed or negative impact on learning opportunities (Dean E, 2020; GMC, 2020). The e-learning is continually updated with new evidence, with plans to expand access across London. An iterative process was undertaken with updates in response to learner feedback due to the speed at which the resource needed to be developed, for example, turning resources into PDFs for home access. The e-learning remains live given rising COVID-19 cases. Further work is required to investigate the effectiveness of this resource across London and how beneficial it has been for clinical work.
National Confidential Enquiry into Patient Outcome and Death (NCEPOD) states that emergency patients must have prompt access to theatres, critical care facilities and appropriately-trained staff at all times. Due to the increased number of trauma cases treated by our orthopaedic teams a dedicated Day Surgery Trauma List (DSTL) was introduced. This article is a retrospective study of operations, cost implications and patient satisfaction of this list. We reviewed 49 patients operated on by the first author in six months from October 2008 to March 2009. The type of operation, place of operative decision and the time taken from the decision to actual operation was recorded. The cost was analysed with the help of the finance department. Patient satisfaction was calculated from a questionnaire. Decision to operate was taken in accident and emergency in 60% cases and 40% in fracture clinic. The average time from the decision to operation was two days. Cost-benefit to the NHS was £300 per case. 28 patients answered the questionnaire with overall patient satisfaction of 8.57 out of 10. The day surgery trauma list may be used to perform various orthopaedic trauma procedures with significant cost containment (£14 400 in six months). Benefits to patients were specified operative time, reduced waiting times and good clinical care.
T h e chaperonin containing TCP-1 (CCT) is composed from eight -60 k D a ATPase subunits encoded by separate, conserved genes. Unlike its bacterial GroEL relative, CCT forms hetero-oligomeric rings, with 8-fold symmetry. Moreover, CCT assists folding of archetypically eukaryotic polypeptides, especially actins a n d tubulins. Presently CCT is seen as a n essential chaperone for the maturation of actin monomer and tubulin dimer, acting after prefoldin (GimC) to receive nascent chains from ribosomes a n d before they achieve a native (polymerisable) state. In the case of tubulin dimer formation a n d assembly, post-CCT cofactors are required. Our research challenges ideas of CCT being limited to a role as a fixed 16-mer involved only in peri-(or immediately post-) translational folding. CCT subunits selectively interact with polymerised microtubules, influence actin assembly a n d bind F-actin in vitro. CCT subunits are also found a t sites of actin assembly in cells away from ribosomes and remain associated with actin over days during its slow axonal transport in vivo, a strictly post-translational process. The structural differences between bovine lens alpha-A and alphaLens alpha-A and alpha-B crystallin have been reported to act differently in their protection against non-thermal destabilisation of proteins. The nature of this difference, however, is not completely understood. Therefore we used a combination of thermally and solvent-induced structural changes to investigate the difference in the secondary, the tertiary and the quaternary structure of alpha-A and alpha-B crystallin. We demonstrated the relation between the changes in the tertiary and the quaternary structure for both polypeptides. Far-ultraviolet circular dichroism revealed that the secondary structure of alpha-B crystallin is more stable than alpha-A crystallin and the temperature-induced secondary structure changes of both polypeptides are partially reversible. Tryptophan fluorescence revealed two distinct transitions for both alpha-A and alpha-B crystallin. Compared to alpha-B crystallin, both transitions of alpha-A crystallin ocurred at high temperature. The changes in the hydrophobicity are accompanied by changes in the quaternary structure and are biphasic, as shown by bis-1-anilino-8-napthalenesulfonate fluorescence and sedimentation velocity. These phenomena explain the difference in the chaperone capacity of alpha-A and alpha-B crystallin carried out at different temperatures. The quaternary structure of alpha crystallin is more stable than alpha-A and alpha-B crystallin. The latter has a strong tendency to dissociate under thermal or solvent destabilisation. This phenomenon is related to the difference in subunit organisation of alpha-A and alpha-B crystallin where both hydrophobic and ionic interactions are involved. We find that an important subunit rearrangement of alpha-A crystallin takes place once the molecule is destabilised. This subunit rearrangement is a requisite phenomenon for maintaining alpha crystallin in its globular for...
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