ABSTRACT
BACKGROUND:Adolescent idiopathic scoliosis is a common disease that can affect physical appearance of adolescents in the clinic at present. However, there are lacks of studies on coronal plane imbalance after fixation using Logistic regression equation at present. OBJECTIVE:To investigate the reasons for coronal plane imbalance after fixation in patients with Lenke type II adolescent idiopathic scoliosis. METHODS:141 cases of Lenke type II adolescent idiopathic scoliosis admitted by Department of Spinal Surgery of the First Affiliated Hospital of Xinjiang Medical University in China from January 2001 to November 2012 were chosen as subjects. Multivariate single factor and multiple-factor Logistic regression were performed. Risk factors for the coronal plane imbalance after fixation in adolescent idiopathic scoliosis patients were screened, and predictive models were established. RESULTS AND CONCLUSION:Coronal plane imbalance occurred in 30 of the 141 patients, accounting for 21.28%. For Lenke type II adolescent idiopathic scoliosis patients, preoperative apical vertebral Nash-More rotation level 3-4, Risser grade 4-5, major curve correction rate/flexibility>1, lower thoracic Cobb angle>70° were vulnerable to postoperative coronal plane imbalance. Multivariate logistic regression showed that vertebral rotation, Risser grade, major curve correction rate/flexibility, lower thoracic Cobb angle were independent risk factors for postoperative coronal plane imbalance in Lenke type II adolescent idiopathic scoliosis patients. The predictive model was Y=1/[1+exp(-1.182X 1+1.228X 2+1.671X 3-0.71X 4+0.407)].
ABSTRACT
The 70 kDa heat shock proteins (Hsp70s) are highly conserved in evolution, leading to striking similarities in structure and composition between eukaryotic Hsp70s and their homologs in prokaryotes. The eukaryotic Hsp70 like the DnaK (Escherichia coli equivalent Hsp70) protein, consist of three functionally distinct domains: an N-terminal 44-kDa ATPase portion, an 18-kDa peptide-binding domain and a C-terminal 10-kDa fragment. Previously, the amino acid sequence of eukaryotic (the brine shrimp Artemia franciscana) Hsp70 and DnaK proteins were shown to share a high degree of homology, particularly in the peptide-binding domain (59.6%, the putative innate immunity-activating portion) compared to the N-terminal ATPase (48.8%) and the C-terminal lid domains (19.4%). Next to this remarkable conservation, these proteins have been shown to generate protective immunity in Artemia against pathogenic Vibrio campbellii. This study, aimed to unravel the Vibrio-protective domain of Hsp70s in vivo, demonstrated that gnotobiotically cultured Artemia fed with recombinant C-terminal fragment (containing the conserved peptide binding domain) of Artemia Hsp70 or DnaK protein were well protected against subsequent Vibrio challenge. In addition, the prophenoloxidase (proPO) system, at both mRNA and protein activity levels, was also markedly induced by these truncated proteins, suggesting epitope(s) responsible for priming the proPO system and presumably other immune-related genes, consequently boosting Artemia survival upon challenge with V. campbellii, might be located within this conserved region of the peptide binding domain.
