Miscoding in the Nationwide Inpatient Sample Database Raises Questions About Validity for Arthroplasty Research.

BACKGROUND: The use of administrative databases in arthroplasty research has increased over the past decade. The Nationwide Inpatient Sample (NIS) is one of the first and most frequently used. Despite many published articles using this dataset, there exists no standardization resource accounting for the potential of biased results. The purpose of our study was to assess the amount of discordant data between clinically relevant variables and propose a standard for using this database in primary total hip arthroplasty (THA) and total knee arthroplasty (TKA). METHODS: An initial set of patients undergoing total joint arthroplasty were identified from the NIS between 2016 and 2019 using the International Classification of Diseases, 10th Revision, Procedure Coding System. All records with THA and TKA in any of the procedure variables (PR1-PR20) were included. A total of 63 relevant and consistent variables were selected for individual comparison including diagnosis-related group (1), elective (1), procedure codes (20), day of main procedure (1), and diagnosis codes (40). Descriptive statistics were used. A total of 3,562,819 patients were included in the initial set. RESULTS: Using diagnosis-related groups, 5.3% were revision surgeries, 4.7% were not elective, 2.3% did not have THA or TKA as their primary procedure for hospitalization, and 2.9% of THA and 9.7% of TKA were bilateral. A total of 6.2% of the surgeries were done day(s) before or after admission, and 10.8% of THA and 6.3% of TKA were missing an orthopedic diagnosis for admission. Many had multiple orthopedic diagnoses for admission, 3.2% of THA and 0.7% of TKA. Overall miscoding was 23.3%. CONCLUSIONS: Using the NIS without standardized data processing to study elective, unilateral, primary THA and TKA introduces major bias. A logical and stepwise approach to curate the data before analysis is proposed to improve research quality when using this database in hip and knee arthroplasty studies.

Biomechanical properties of porcine meniscus as determined via AFM: Effect of region, compartment and anisotropy.

The meniscus is a fibrocartilaginous tissue that plays an essential role in load transmission, lubrication, and stabilization of the knee. Loss of meniscus function, through degeneration or trauma, can lead to osteoarthritis in the underlying articular cartilage. To perform its crucial function, the meniscus extracellular matrix has a particular organization, including collagen fiber bundles running circumferentially, allowing the tissue to withstand tensile hoop stresses developed during axial loading. Given its critical role in preserving the health of the knee, better understanding structure-function relations of the biomechanical properties of the meniscus is critical. The main objective of this study was to measure the compressive modulus of porcine meniscus using Atomic Force Microscopy (AFM); the effects of three key factors were investigated: direction (axial, circumferential), compartment (medial, lateral) and region (inner, outer). Porcine menisci were prepared in 8 groups (= 2 directions x 2 compartments x 2 regions) with n = 9 per group. A custom AFM was used to obtain force-indentation curves, which were then curve-fit with the Hertz model to determine the tissue's compressive modulus. The compressive modulus ranged from 0.75 to 4.00 MPa across the 8 groups, with an averaged value of 2.04±0.86MPa. Only direction had a significant effect on meniscus compressive modulus (circumferential > axial, p = 0.024), in agreement with earlier studies demonstrating that mechanical properties in the tissue are anisotropic. This behavior is likely the result of the particular collagen fiber arrangement in the tissue and plays a key role in load transmission capability. This study provides important information on the micromechanical properties of the meniscus, which is crucial for understanding tissue pathophysiology, as well as for developing novel treatments for tissue repair.

Development of an Effective Electronic Medical Record for Student-Run Free Health Fairs Using Research Electronic Data Capture (REDCap) Software.

BACKGROUND: The University of Miami Mitchell Wolfson Sr. Department of Community Service (DOCS) is a student-run organization providing free health care to the medically underserved in South Florida. For a large organization providing care to thousands of people per year, an effective electronic medical record (EMR) is necessary to keep track of patient records. METHODS: A REDCap project was configured in a way that allows it to mimic a basic EMR. This was done by assigning patients medical record numbers, creating repeating events allowing patient results to be seen over time, and incorporating extensive logic to facilitate clinical decision-making. RESULTS: DOCS was able to create a basic EMR using REDCap and has seen success with this approach. DISCUSSION: REDCap is capable of functioning as a robust, basic EMR which can be suitable for any purpose. It is HIPAA-compliant, comprehensive and low-cost, making it suitable for serving underserved populations.

Phosphorylation of Mnk1 by caspase-activated Pak2/gamma-PAK inhibits phosphorylation and interaction of eIF4G with Mnk.

The mitogen-activated protein kinase-interacting kinase 1 (Mnk1) is phosphorylated by caspase-cleaved protein kinase Pak2/gamma-PAK but not by Cdc42-activated Pak2. Phosphorylation of Mnk1 is rapid, reaching 1 mol/mol within 15 min of incubation with Pak2. A kinetic analysis of the phosphorylation of Mnk1 by Pak2 yields a K(m) of 0.6 microm and a V(max) of 14.9 pmol of (32)P/min/microg of Pak2. Two-dimensional tryptic phosphopeptide mapping of Mnk1 phosphorylated by Pak2 yields two distinct phosphopeptides. Analysis of the phosphopeptides by automated microsequencing and manual Edman degradation identified the sites in Mnk1 as Thr(22) and Ser(27). Mnk1, activated by phosphorylation with Erk2, phosphorylates the eukaryotic initiation factor (eIF) 4E and the eIF4G components of eIF4F. Phosphorylation of Mnk1 by Pak2 does not activate Mnk1, as measured with either eIF4E or eIF4F as substrate. Phosphorylation of Erk2-activated Mnk1 by Pak2 has no effect on phosphorylation of eIF4E but reduces phosphorylation of eIF4G by Mnk1 by up to 50%. Phosphorylation of Mnk1 by Pak2 inhibits binding of eIF4G peptides containing the Mnk1 binding site by up to 80%. When 293T cells are subjected to apoptotic induction by hydrogen peroxide, Mnk1 is phosphorylated at both Thr(22) and Ser(27). These results indicate a role for Pak2 in the down-regulation of translation initiation in apoptosis by phosphorylation of Mnk1.