Meniscal Injury Does Not Significantly Affect the Dimensions of the Intact Meniscus in the Opposite Compartment of the Knee

Background: Meniscal allograft transplant requires precise matching of the size of the allograft with the dimensions of the recipient knee. Estimation of contralateral meniscal size on magnetic resonance imaging (MRI) has been considered the ideal method to measure menisci before transplant. We questioned whether a contralateral intact meniscus with meniscal injury in the opposite compartment could be used as a reference to determine allograft size. Our question was derived from knowledge of meniscal injury influencing structures of the opposite compartment of the knee, including the meniscus. Purpose: To compare meniscal dimensions between intact meniscus with meniscal injury in the opposite compartment and normal meniscus with a normal opposite compartment. Study Design: Cross-sectional study; Level of evidence, 3. Methods: This observational, cross-sectional study was performed between 2016 and 2017. The control group consisted of 200 knees with normal medial and lateral menisci. The medial intact group consisted of 150 cases of medial intact meniscus with injured lateral meniscus, and the lateral intact group consisted of 150 cases of lateral intact meniscus with injured medial meniscus. All patients were male. Mean age, height, and weight did not differ among groups. We investigated meniscal dimensions on MRI, including anteroposterior and mediolateral lengths, distance between the anterior and posterior horns (AHPH distance), and widths and heights of the anterior and posterior horns and midbody. Results: Most medial meniscal dimensions were similar between the control and medial intact groups, but the AHPH distance was smaller in the medial intact group ( P < .001). Likewise, most lateral meniscal dimensions were similar between the control and lateral intact groups, but the AHPH distance was smaller in the lateral intact group ( P < .001). Conclusion: Most dimensions of the intact meniscus with meniscal injury in the opposite compartment were similar to those of the normal meniscus with normal opposite compartment. Measuring the dimensions of the contralateral intact meniscus with meniscal injury in the opposite compartment on MRI can be an appropriate method to determine meniscal allograft size.

Indication for Unicompartmental Knee Replacement versus Osteotomy around the Knee

Unicompartmental medial or lateral osteoarthritis of the knee is found in up to 50% of all osteoarthritic patients and may be addressed surgically either by knee osteotomies or unicompartmental replacements. The limits for indicating one procedure or the other are somehow not defined. This article discusses the diagnostic algorithm and the most important decision factors. A long-leg radiograph and formal deformity analysis is mandatory. If constitutional or posttraumatic metaphyseal deformity in the frontal plane is detected and the opposite compartment is intact, an osteotomy should be considered. The result is not depending on age and grade of osteoarthritis. Unicompartmental knee arthroplasty is indicated in substantial osteoarthritis of one compartment (bone-on-bone) with intact ligaments and a functionally intact contralateral compartment. The anatomy of the femur and tibia should be normal with no gross osseous deformity. Age, obesity, or asymptomatic patellofemoral degeneration are not considered exclusion criteria for those surgical procedures.

Identification of Tyr residues that enhance folate substrate binding and constrain oscillation of the proton-coupled folate transporter (PCFT-SLC46A1)

The proton-coupled folate transporter (PCFT) mediates intestinal folate absorption and transport of folates across the choroid plexus. This study focuses on the role of Tyr residues in PCFT function. The substituted Cys-accessibility method identified four Tyr residues (Y291, Y362, Y315, and Y414) that are accessible to the extracellular compartment; three of these (Y291, Y362, and Y315) are located within or near the folate binding pocket. When the Tyr residues were replaced with Cys or Ala, these mutants showed similar (up to 6-fold) increases in influx Vmax and Kt/ Ki for [3H]methotrexate and [3H]pemetrexed. When the Tyr residues were replaced with Phe, these changes were moderated or absent. When Y315A PCFT was used as representative of the mutants and [3H]pemetrexed as the transport substrate, this substitution did not increase the efflux rate constant. Furthermore, neither influx nor efflux mediated by Y315A PCFT was transstimulated by the presence of substrate in the opposite compartment; however, substantial bidirectional transstimulation of transport was mediated by wild-type PCFT. This resulted in a threefold greater efflux rate constant for cells that express wild-type PCFT than for cells that express Y315 PCFT under exchange conditions. These data suggest that these Tyr residues, possibly through their rigid side chains, secure the carrier in a high-affinity state for its folate substrates. However, this may be achieved at the expense of constraining the carrier's mobility, thereby decreasing the rate at which the protein oscillates between its conformational states. The Vmax generated by these Tyr mutants may be so rapid that further augmentation during transstimulation may not be possible.

The purified and reconstituted ornithine/citrulline carrier from rat liver mitochondria catalyses a second transport mode: ornithine+/H+ exchange

The mechanism of unidirectional transport of ornithine (i.e. in the absence of a counter-metabolite) has been investigated in proteoliposomes reconstituted with the ornithine carrier purified from rat liver mitochondria. The efflux of [3H]ornithine from proteoliposomes was stimulated by the addition of H+ (but not of other cations) to the incubation medium . On keeping the pH in the compartment containing ornithine constant at 8.0, the flux of ornithine into or out of the proteoliposomes increased on decreasing the pH in the opposite compartment from 8.0 to 6.0. Ornithine influx was also stimulated when a higher H+ concentration was generated inside the vesicles relative to the outside by the K+/H+ exchanger nigericin in the presence of an outwardly directed K+ gradient. A valinomycin-induced electrogenic flux of K+ did not affect ornithine transport in the absence of a counter-metabolite. Furthermore, changes in fluorescence of the pH indicator pyranine, included inside the proteoliposomes, showed that the flux of ornithine is accompanied by translocation of H+ in the opposite direction. It is concluded that the mitochondrial ornithine carrier catalyses an electroneutral exchange of ornithine+ for H+, in addition to the well-known 1:1 exchange of metabolites. Lysine+, but not citrulline, can also be exchanged for H+ by the ornithine carrier. The ornithine+/H+ transport mode of the exchanger is an essential step in the catabolism of excess arginine.