Influence of knee flexion and femoral cross-pin insertion angle on posterolateral structures of the knee and lateral fixation lengths during ACL reconstruction.

PURPOSE: Some studies have investigated knee flexion angle on the sagittal plane and insertion angle of the cross-pin on the coronal plane to evaluate proper femoral fixation. They evaluated the possibilities of injury to the posterolateral (PL) and neurovascular structures using several methods. The purposes of this study were to evaluate (1) the influence of knee flexion and femoral cross-pin insertion angles on knee PL structures and (2) the lateral fixation length of the cross-pin. METHODS: Ten fresh cadaveric knees with no previous surgeries around the knee were used. Transtibial femoral tunnels (1:30 or 10:30 o'clock position) were made at three different knee flexion angles (70°, 90°, and 110°). Two cross-pin guidewires (superior and inferior pins) were drilled at three different insertion angles [downward 30°, 0° (parallel to floor line), and upward 30°] for each knee flexion position. The distances from the insertion point of the two cross-pins to the lateral collateral ligament (LCL) and popliteus tendon (PT), and the distance from the lateral wall of the femoral tunnel to the lateral cortex of the femoral condyle were measured. RESULTS: No significant differences were observed in the superior and inferior pin depths (p = 0.56 and 0.39). The distances from the superior pin to the LCL and from the inferior pin to the LCL were significantly shorter in all knee flexions with 0° and an upward 30° insertion angle than with 70° and 90° knee flexion with a downward 30° insertion angle, respectively (superior pin: p = 0.02 and 0.03; inferior pin: p = 0.03 and 0.03). No significant difference was observed in the distance between the superior pin and inferior pins and the PT (p = 0.25). CONCLUSIONS: The cross-pin was inserted close to the LCL and PT, and a downward 30° angle was the safest insertion angle. Lateral fixation length was sufficient for the cross-pin fixation in the 10:30- or 1:30-positioned femoral tunnel.

Topical application of liposomal cobalamin hydrogel for atopic dermatitis therapy.

Topical vitamin B12 was shown to be effective for atopic dermatitis. However, vitamin B12 itself is light sensitive and has low skin permeability, thus reducing its therapeutic effectiveness. In the present study, we prepared a liposomal hydrogel of adenosylcobalamin (AdCbl), a vitamin B12 derivative, and investigated possible beneficial effects of AdCbl on atopic dermatitis using an NC/Nga murine atopic dermatitis model. AdCbl was loaded into liposomes prepared by a thin film hydration method using a pH gradient method that employed citric acid buffer solution. This resulted in AdCbl-loaded liposomes that were 106.4 +/- 2.2 nm in size. The loading efficiency was 40% (of the initial AdCbl amount). Lipo-AdCbl had enhanced skin permeability, being about 17-fold compared with AdCbl-gel. Topical administration of Lipo-AdCbl-gel to 2,4-dinitrochlorobenzene (DNCB)-induced atopic dermatitis-like skin lesions in NC/Nga mice ameliorated lesion intensity scores, dorsal skin thickness, and total serum IgE in a concentration-dependent manner. Other preparations, including AdCbl solution, AdCbl cream, liposomes alone, and a mixture of AdCbl solution and liposomes had little effect. Taken together, our findings indicate that Lipo-AdCbl-gel has protective effects against atopic dermatitis symptoms, and suggest that it may be of benefit in the treatment of human inflammatory skin diseases.

Molecular and functional characterization of CaLEA6, the gene for a hydrophobic LEA protein from Capsicum annuum.

We used differential screening to isolate a full-length dehydration-responsive cDNA clone encoding a hydrophobic late embryogenesis abundant (LEA)-like protein from PEG-treated hot pepper leaves. Named CaLEA6 (for Capsicum annuum LEA), this gene belongs to the atypical hydrophobic LEA Group 6. The full-length CaLEA6 is 709 bp long with an open reading frame encoding 164 amino acids. It is predicted to produce a highly hydrophobic, but cytoplasmic, protein. The putative M(r) of CaLEA6 protein is 18 kDa, with a theoretical pI of 4.63. Based on our Southern blot analysis, CaLEA6 appears to exist as a small gene family. CaLEA6 was not expressed prior to any treatment, but its transcript was rapidly and greatly increased following trials with PEG, ABA, and NaCl. Chilling also induced its rapid induction, but to a much lesser extent. Accumulation of CaLEA6 protein occurred soon after NaCl applications, but considerably delayed after treatment with PEG. Tobacco plants that overexpressed CaLEA6 showed enhanced tolerance to dehydration and NaCl but not to chilling, as defined by their leaf fresh weights, Chl contents, and the general health status of the leaves. Therefore, we suggest that CaLEA6 protein plays a potentially protective role when water deficit is induced by dehydration and high salinity, but not low temperature.