Search

Thoracolumbar fractures are usually treated by open posterior pedicle screw fixation. However, this procedure involves massive paraspinal muscle stripping, inflicting surgical trauma, and prolonged X-ray exposure. In this study, we observed 127 patients with single-segment injury thoracolumbar fractures. Thirty-six patients were treated by the modified Wiltse's paraspinal approach with minimally invasive channel system, while 91 patients were treated via traditional posterior approach. Operation time, intraoperative blood loss, intraoperative fluoroscopy frequency, screw placement accuracy, visual analogue scale score, and Cobb's angle of two groups were compared. The X-ray exposure times were notably reduced (4.2±1.6) in the new approach group (P<0.05). The pedicle screw placement accuracy and Cobb's angle after surgery were similar in the two groups. We conclude that modified Wiltse's paraspinal approach with spinal minimally invasive channel system surgery can significantly reduce the X-ray exposure times and is an alternative therapy for the thoracolumbar fracture. [ABSTRACT FROM AUTHOR]

BACKGROUND Hemoglobin is a precursor of antibacterial peptides. Our aim was to identify an antibacterial peptide in human endometrium. We tested the antimicrobial activities of hemoglobin and a derived peptide in vitro and in vivo in rats. METHODS Samples (n = 3) were scraped from the surface of endometrium. Acid-soluble proteins underwent electrophoresis followed by gel overlay assay and reversed-phase high-performance liquid chromatography. Antibacterial activities were determined by agar radial diffusion assay. Purified peptides were further characterized by electrophoresis, mass spectrometry, N-terminal amino acid (AA) sequencing and protein structure analysis. A rat model was used to test the inhibitory activity of human hemoglobin on vaginal infection with Escherichia coli, using one experimental group (intravaginal hemoglobin, n = 9) and three control groups (n = 14). Vaginal histology was studied. RESULTS The purified peptide exhibited potent antibacterial activities against E. coli ML-35P. The N-terminal AA sequence was F L S F P T T K T Y, identical to AA 32–41 of the human hemoglobin α chain, and it had the same mass (m/z = 6776.8) as the α chain 32–93 AA fragment, with at least three α-helices. Histology indicated that the hemoglobin group changed significantly compared with the matrix control group (no treatment after infection): the surface layer of stratified squamous epithelium was smoother, inflammatory cell infiltration was relieved in the lamina propria and congestion pattern was decreased. CONCLUSIONS These results suggest that erythrocytes from endometrium are another source of the antimicrobial molecules. Hemoglobin and its derived peptides may play a role in the host defense against pathogens in human vagina. [ABSTRACT FROM AUTHOR]