Background: Orthopedic surgeons depend on the intraoperative use of fluoroscopy to facilitate procedures across all subspecialties. The versatility of the C-arm fluoroscope allows acquisition of nearly any radiographic view. This versatility, however, creates the opportunity for difficulty in communication between surgeon and radiation technologist. Poor communication leads to delays, frustration and increased exposure to ionizing radiation. There is currently no standard terminology employed by surgeons and technologists with regards to direction of the fluoroscope. Methods:The investigation consisted of a web-based survey in 2 parts. Part 1 was administered to the membership of the Canadian Orthopedic Association, part 2 to the membership of the Canadian Association of Medical Radiation Technologists. The survey consisted of open-ended or multiple-choice questions examining experience with the C-arm fluoroscope and the terminology preferred by both orthopedic surgeons and radiation technologists. Results:The survey revealed tremendous inconsistency in language used by orthopedic surgeons and radiation technologists. It also revealed that many radiation technologists were inexperienced in operating the fluoroscope. Conclusion:Adoption of a common language has been demonstrated to increase efficiency in performing defined tasks with the fluoroscope. We offer a potential system to facilitate communication based on current terminology used among Canadian orthopedic surgeons and radiation technologists.
Orthopaedic surgeons should recognize the value of preoperative skin signing for all procedures and the additional value of the "time out" protocol. We recommend that surgeons strive for 100% compliance with both strategies.
The active center histidines of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system proteins; histidine-containing protein, enzyme I, and enzyme IIA Glc were substituted with a series of amino acids (serine, threonine, tyrosine, cysteine, aspartate, and glutamate) with the potential to undergo phosphorylation. Histidine is a unique amino acid with the potential for phosphorylation at two distinct positions 1 , either the N ␦1 or the N ⑀2 atom of the imidazole ring. There are many examples of proteins, both prokaryotic and eukaryotic, in which a histidine is phosphorylated at one of these positions. It has been estimated that phosphohistidine may account for up to 6% of total protein phosphorylations in eukaryotic cells (1). Protein phosphorylations involving phosphohistidines are much more prominent than other phosphoamino acids in organisms such as Escherichia coli and Salmonella typhimurium (2) that utilize sugars via the phosphoenolpyruvate:sugar phosphotransferase system (PTS). 2 Estimates of the concentrations of the PTS proteins and enzymes (3) suggest that internal concentrations of phosphohistidines might exceed 0.2 mM under certain physiological conditions.The PTS functions in sugar phosphorylation and translocation (see reviews in Refs. 4 -6). The PTS system is also involved in a variety of other related cellular functions, such as the regulation of uptake of non-PTS sugars (see review in Ref. 7), chemotaxis (see review in Ref. 8) and catabolite repression (see reviews in Refs. 5 and 6). The PTS is a linear arrangement of both soluble and membrane-bound phosphocarrier proteins and enzymes, which function through a series of phosphotransfer reactions with the phosphate group originating from phosphoenolpyruvate (PEP) and ultimately leading to phosphorylation of the sugar moiety.The first two reactions of the PTS involve enzyme I and histidine-containing protein (HPr), which are soluble, non-sugar-specific, energy coupling components. Two subsequent phosphotransfer reactions involve a membrane-bound, sugar-specific enzyme II. Enzyme II has three or four common functional domains, ABCD (9). The enzyme IIC domain is a membranetransversing domain involved in translocation, and is in some examples complexed with a similar enzyme IID domain. Except for the enzyme IIC and enzyme IID domains, all other protein and enzyme components of the PTS form phosphorylated residues at their active sites in the course of the phosphoryl transfer reactions. The enzyme IIB domain is the site of sugar phosphorylation. Most enzyme II proteins do not have an enzyme IID domain, and in these the phosphoamino acid formed in the enzyme IIB domain is a phosphocysteine (10). In enzyme II, in which an enzyme IID domain is found, the enzyme IIB domain forms a [N ␦1 -P]histidine. The enzyme IIA domain is phosphorylated to form a [N ⑀2 -P]histidine, at residue 90 (11), HPr has a [N ␦1 -P]histidine, at residue 15 (12, 13), and enzyme I a [N ⑀2 -P]histidine, at residue 189 (14). The reactions of the PTS, involving phosp...
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.
hi@scite.ai
10624 S. Eastern Ave., Ste. A-614
Henderson, NV 89052, USA
Copyright © 2024 scite LLC. All rights reserved.
Made with 💙 for researchers
Part of the Research Solutions Family.