ABSTRACT
BACKGROUND AND PURPOSE: The effect of a sociability-based fitness approach on parkinsonian disability in patients with Parkinson's disease (PD) was assessed. METHODS: Eighty patients diagnosed with PD were randomly assigned to either the group-based rehabilitation (GBR) group (n = 40) or the individual-based rehabilitation (IBR) group (n = 40). The primary outcome was the difference between the two groups in the mean change from baseline to post-training in the total score on the Unified Parkinson's Disease Rating Scale (UPDRS). The secondary outcomes included the change in mental status and the difference in the mean change from baseline to month 3 and month 6 in the total score on the UPDRS. RESULTS: The mean (±SD) UPDRS scores were 72.0 ± 21.0 in the GBR group and 72.1 ± 18.6 in the IBR group. The UPDRS scores from baseline to post-training were 22.8 ± 13.5 in the GBR group and 10.9 ± 8.8 in the IBR group (difference 11.8 points; 95% confidence interval [CI] 5.0-18.6; p = 0.001). The difference between the groups from baseline to month 3 (difference 10.06 points; 95% CI 3.3-16.8) and the difference between the groups from baseline to month 6 (difference 11.7 points; 95% CI 4.9-18.5) were also significant (p = 0.004 and p = 0.001, respectively). The scores of cognitive function and depression had not changed significantly. CONCLUSIONS: Patients receiving GBR demonstrated significant improvements in parkinsonian symptoms, suggesting that the sociability-based fitness can be applied to clinical treatment by sustaining the motivation in PD.
Subject(s)
Parkinson Disease , Double-Blind Method , Exercise , HumansABSTRACT
Protein glutaminase, which converts a protein glutamine residue to a glutamate residue, is expected to be useful as a new food-processing enzyme. The crystal structures of the mature and pro forms of the enzyme were refined at 1.15 and 1.73 Å resolution, respectively. The overall structure of the mature enzyme has a weak homology to the core domain of human transglutaminase-2. The catalytic triad (Cys-His-Asp) common to transglutaminases and cysteine proteases is located in the bottom of the active site pocket. The structure of the recombinant pro form shows that a short loop between S2 and S3 in the proregion covers and interacts with the active site of the mature region, mimicking the protein substrate of the enzyme. Ala-47 is located just above the pocket of the active site. Two mutant structures (A47Q-1 and A47Q-2) refined at 1.5 Å resolution were found to correspond to the enzyme-substrate complex and an S-acyl intermediate. Based on these structures, the catalytic mechanism of protein glutaminase is proposed.
Subject(s)
Chryseobacterium/enzymology , Glutaminase/chemistry , Amino Acid Sequence , Catalysis , Catalytic Domain , Crystallization , Crystallography, X-Ray/methods , Cysteine Proteases/chemistry , Glutamine/chemistry , Molecular Sequence Data , Mutagenesis, Site-Directed , Mutation , Proline/chemistry , Protein Binding , Protein Conformation , Transglutaminases/chemistryABSTRACT
Following recent advance in medical technology, the increase of immunocompromised patients results in an increase of opportunistic infections such as nocardiosis. However, little is known about relationships between clinical features of nocardial infections and each Nocardia species, especially newly identified ones. Therefore, we identified clinical isolates of Nocardia species by genetic methods and analyzed clinical features of nocardiosis. Nine clinical isolates were obtained in Kyushu University Hospital from 2005 to 2008. Six different Nocardia species were identified by 16Sr RNA: Nocardiafarcinia (n=2), Nocardia brasiliensis (n=2), Nocardia cyriacigeorgica (n=2), Nocardia transvalensis (n=1), Nocardia araoensis (n=1) and Nocardia testacea (n=1). The underlying diseases of 9 patients were pulmonary diseases(n=5), malignant diseases(n=3), collagen diseases(n=1) or primary immunodeficiency diseases (n=l). According to antimicrobial susceptibility testing, none of them was resistant to minocycline or linezolid. Among seven isolates from respiratory specimens, one was resistant to imipenem, sulfamethoxazole/trimethoprim and amikacin, two were to ciprofloxacin. Three species identified recently (N cyriacigeorgica, N. araoensis and N. testacea) were involved in this study and most of them were considered as infectious pathogens to human. These data suggested the identification of Nocardia to the species level and susceptibility testing were important for diagnosis as infectious diseases and treatments.
