Femoral Component Axial Rotation in the Gap-Balancing Approach to Total Knee Arthroplasty: Measurement by Computed Tomography.

BACKGROUND: Rotational malalignment of total knee arthroplasty (TKA) is a potential cause for revision surgery; therefore, it is important to have valid criteria for evaluation of normal component rotational alignment. Because computed tomography (CT) is considered the most accurate method to assess the rotational alignment of prosthetic components, the objectives in this study were define the femoral component (FC) rotation by measuring the posterior condylar angle (PCA) and the condylar twist angle (CTA) in a patient population that underwent gap-balancing TKA; determine the reliability of the FC rotation by using these measurements; evaluate the inter-relationship between the PCA and CTA; and finally evaluate the frequency and agreement in identification of the medial epicondyle sulcus (MES). METHODS AND RESULTS: In this retrospective study, 2 radiologists examined 50 CT scans. Mean PCA values of -2.26° and -2.56° (internal rotation) and CTA values of -5.54° and -6.28° (internal rotation) were attained by 2 observers with a higher interobserver concordance for the PCA. Both measurements were considered to be reliable. There was moderate interobserver agreement for MES identification, with the MES present in 64% and 78% of patients, as identified by 2 observers. CONCLUSION: Mean FC rotation values as evaluated by PCA were -2.26° and -2.56° and as evaluated by CTA were -5.54° and -6.28°. PCA and CTA measurement by CT is reliable; however, the use of PCA is preferable because of the higher observer concordance. PCA can be inferred by subtracting 3° or 4° from the CTA. MES was identified in 64% and 78% of patients, with only moderate interobserver agreement.

Cloning, heterologous expression in Escherichia coli and characterization of a protein disulfide isomerase from Fasciola hepatica.

A Fasciola hepatica cDNA clone of 1752 bp was isolated from an adult worm cDNA expression library by immunological screening using a rabbit serum against the excretory-secretory antigens. The nucleotide sequence of the cDNA revealed the presence of an open reading frame of 489 codons which encoded a 55 kDa polypeptide, showing a high degree of homology to protein disulfide isomerases. This putative antioxidant protein cDNA was expressed in Escherichia coli as a GST fusion protein. The cleaved recombinant protein was shown to be biologically active in vitro by mediating the oxidative refolding of reduced RNase. Immunoblotting studies using a specific antiserum raised against the recombinant protein showed the presence of a polypeptide of similar molecular mass in the excretory-secretory extract of the adult parasite. The extracellular location of this protein was also supported by the specific immune responses found against this protein in F. hepatica experimentally infected rabbits.