Accurate temperature assessment is essential in neonatal patients and allows for prompt recognition of illness. Temperature can be measured by rectum, which is subject to injury, axillary, which is time-consuming, and temporal artery, which is safe and fast. The purpose of this evidence-based practice quality improvement project was to create an educational toolkit for nurses teaching temporal artery thermometers for routine temperature measurement on neonates, to establish the content validity of the toolkit, and to make recommendations for implementation of the toolkit. The format applied was the Kellogg Logic Model that proceeded from the assumption, to planned work, and results. The theoretical framework was Roger's Diffusion of Innovations, which identifies champions as the initial change agents, helps engage the staff, and facilitates the change. The project consisted of a two-phase process. Phase 1 was the development of the toolkit contents by integrating the evidence and applying the framework in the context of working nurses. Phase 2 was the validation of the toolkit by expert nurses and educators with Item-CVI ranging from 0.80 to 1.00 and the scale-CVI at 0.98. The Toolkit for Implementation of Temporal Artery Thermometers for Neonates with three short video presentations was validated. The toolkit is shared on multiple webpages and is available to the public. Adopting the temporal artery thermometer for routine temperature measurement could be a new standard for temperature monitoring that is accurate and fast. Improved family satisfaction would result from a quicker temperature process and a less invasive method resulting in a more comfortable experience for their infant.

Amyloid is a form of abnormal protein aggregation within the living body. Massive deposits can lead to organ failure. There is also increasing evidence that smaller pre-amyloid aggregates exert direct toxic effects to cells. To date 25 different proteins are known to occur as amyloid deposition in human tissues, although not all of these conditions are known to be associated with clinical diseases. This thesis deals with the very common form of amyloid localized to the arterial media. The fibril protein called ‘medin’ was identified in 1999. Medin is a 50 amino acid residue internal fragment of the precursor protein lactadherin. Lactadherin, first found in human milk, is expressed in various tissues such as breast epithelium (including carcinomas), macrophages and aorta. The function of the protein is not known but it has several functional domains. There is an EFG like domain, including an RGD-sequence, in the N-terminal part of the molecule. The C-terminal part consists of C1 and C2 coagulation factor V and VIII like domains. Medin is from within the C2 domain. This region is suggested to be involved in phosphatidyl serine binding, important in phagocytosis of apoptotic cells. Medin amyloid was originally described from studies of the aorta. It is shown here that deposits are more widely spread and can be found in many large arteries, particularly within the upper part of the body. The prevalence of medin amyloid increases with age and deposits are found, to a certain degree, in virtually everyone above the age of 60 years. The amyloid is not only found extracellularly but intracellular deposits may also occur. Amyloid is usually associated with elastic lamina or lamellae which often show signs of fragmentation. Given the localization of amyloid to elastic structures of the arterial media, three different vascular diseases were studied: temporal (giant cell) arteritis, thoracic aortic aneurysm and thoracic aortic dissection. Medin amyloid was found in temporal arteries with and without inflammation. In inflamed arteries, amyloid was mainly located along the broken internal elastic lamina. Medin was also demonstrated within giant cells. It is suggested that medin may be an antigen triggering autoimmune giant cell arteritis. In the study of thoracic aortic aneurysms and dissections, we found significant less medin amyloid in diseased aortic tissues compared with a control material. On the other hand, immunoreactive medin, probably in the state of oligomeric aggregates, was regularly found in association with aneurysms and dissections but not in the control material. It is suggested that medin oligomers exert toxic effects on smooth muscle cells which may lead to weakening of the arterial wall with aneurysm or dissection as a consequence.