ABSTRACT
BACKGROUND: At Texas Children's Hospital in Houston, numerous celiac tests are ordered from a wide range of nonspecialty healthcare providers. OBJECTIVE: To retrospectively examine the ordering of celiac tests before and after a test ordering initiative at our institution, to determine whether the initiative impacted appropriate usage of those tests and affected costs. METHODS: We carefully scrutinized all orders for comprehensive celiac testing from July 2016 through September 2017, implemented an in-house celiac-disease screening cascade, and reflexed it to the comprehensive celiac testing panel if an abnormal screening result was obtained. RESULTS: A total of 60 celiac test orders were issued during the 14-month study period. The ordering physician was a gastroenterologist in 6 cases and a nongastroenterologist in 54 cases. Of the 60 orders, only 4 were approved for sending out for comprehensive celiac testing; in 52 of the 60 cases, the order was altered to celiac screening. In the remaining 4 cases, the tests were canceled as a result of incorrect orders. Only 1 of the 52 celiac screenings yielded a positive result and thus was reflexed to the comprehensive panel. CONCLUSIONS: We were able to induce appropriate celiac test usage by implementing a celiac-reflexive cascade. Also, our strategy proved to be extremely cost effective.
Subject(s)
Algorithms , Celiac Disease/diagnosis , Clinical Laboratory Services/statistics & numerical data , Facilities and Services Utilization/statistics & numerical data , Child , Child, Preschool , Clinical Laboratory Services/economics , Clinical Laboratory Services/standards , Costs and Cost Analysis , Facilities and Services Utilization/economics , Facilities and Services Utilization/standards , Female , Humans , Male , Point-of-Care Systems , Quality ImprovementABSTRACT
Ankyrin repeat (AR) proteins are composed of tandem repeats of a basic structural motif of ca. 33 amino acid residues that form a ß-turn followed by two antiparallel α-helices. Multiple repeats stack together in a modular fashion to form a scaffold that is ideally suited for the presentation of multiple functional groups and/or recognition elements. Here we describe a biosynthetic strategy that takes advantage of the modular nature of these proteins to generate multivalent ligands that are both chemically homogeneous and structurally well-defined. Glycosylated AR proteins cluster the tetrameric lectin concanavalin A (Con A) at a rate that is comparable to the rate of Con A aggregation mediated by globular protein conjugates and variable density linear polymers. Thus, AR proteins define a new class of multivalent ligand scaffolds that have significant potential application in the study and control of a variety of multivalent interactions.
