ABSTRACT
BACKGROUND: It is important to quantitatively assess tremor for accurate diagnosis and evaluation of the response to interventions in patients with essential tremor (ET). OBJECTIVE: The purpose of this study was to investigate the relationship between quantitative measures of postural tremor and clinical rating scale in patients with ET. METHODS: 18 ET patients performed a postural tremor task that required them to hold their arms outstretched parallel to the floor while wearing a gyro sensor based measurement system. The time domain variables were derived from the sensor signals. Additionally, the frequency domain variables were derived from the power spectrum of the angular velocity signal. Spearman correlation analysis was employed in the relationship between the variables and clinical score. RESULTS: The RMS angular velocity of roll and yaw directions at the hand joint were strongly correlated with the clinical rating scale (r= 0.7, p< 0.01). Similarly, the peak power of roll and yaw directions at the hand joint were moderately correlated with the clinical rating scale (r= 0.61 and r= 0.67, p< 0.01). In contrast, no significant correlation coefficients were observed in the peak frequency (p> 0.05). CONCLUSION: These results indicate that hand tremor of roll and yaw directions are more associated with assessment of severity of ET compared to other joints. This study suggests that quantitative measurements of postural tremor should be considered as tremor directionality as well as attachment location.
Subject(s)
Essential Tremor/diagnosis , Essential Tremor/physiopathology , Tremor/physiopathology , Upper Extremity/physiopathology , Wearable Electronic Devices , Aged , Female , Humans , Male , Middle Aged , Reproducibility of ResultsABSTRACT
Hemolysin of Vibrio fluvialis (VFH) was purified from culture supernatants by ammonium sulfate precipitation and successive column chromatographies on DEAE-cellulose and Mono-Q. N-terminal amino acid sequences of the purified VFH were determined. The purified protein exhibited hemolytic activity on many mammalian erythrocytes with rabbit erythrocytes being the most sensitive to VFH. Activity of the native VFH was inhibited by the addition of Zn2+, Ni2+, Cd2+ and Cu2+ ions at low concentrations. Pores formed on rabbit erythrocytes were approximately 2.8-3.7 nm in diameter, as demonstrated by osmotic protection assay. Nucleotide sequence analysis of the vfh gene revealed an open reading frame (ORF) consisting of 2200 bp which encodes a protein of 740 amino acids with a molecular weight of 82 kDa. Molecular weight of the purified VFH was estimated to be 79 kDa by SDS-PAGE and N-terminal amino acid sequence revealed that the 82 kDa prehemolysin is synthesized in the cytoplasm and is then secreted into the extracellular environment as the 79 kDa mature hemolysin after cleavage of 25 N-terminal amino acids. Deletion of 70 amino acids from the C-terminus exhibited a smaller hemolytic activity, while deletion of 148 C-terminal amino acids prevented hemolytic activity.
Subject(s)
Hemolysin Proteins/metabolism , Vibrio/metabolism , Amino Acid Sequence , Animals , Bacterial Proteins , Cations, Divalent , Chickens , Cloning, Molecular , Erythrocytes/metabolism , Genes, Bacterial , Hemolysin Proteins/genetics , Hemolysin Proteins/isolation & purification , Hemolysis , Mice , Molecular Sequence Data , Mutagenesis , Osmosis , Rabbits , Sequence Homology, Amino Acid , Temperature , Vibrio/geneticsABSTRACT
Vibrio mimicus is a typical strain of Vibrio cholerae and produces a phospholipase (PhlA) which shares a highly conserved amino acid sequence with the lecithinase (Lec) of V. cholerae. The recombinant protein (rPhlA) produced from the phlA gene of V. mimicus was expressed in Escherichia coli as His-tag fused protein. The rPhlA was purified by gel filtration and Ni-metal affinity chromatographies. When the action mode was investigated by TLC and GC-MS, the purified rPhlA protein showed a phospholipase A activity, which cleaved the fatty acids at the sn-1 and sn-2 positions of phosphatidylcholine. However, it did not show lysophospholipase, sphingomyelinase, and phospholipase C activities. The rPhlA showed maximum activity at temperature of about 40 degrees C and pH around 8-9. Some divalent cations could affect the activity of PhlA. The addition of Co(2+) increased the activity, whereas Mg(2+) and Zn(2+) did not enhance the enzyme activity. The rPhlA could lyse the erythrocytes obtained from the fish such as rainbow trout and tilapia. A significant cytotoxic activity on a fish cell line, CHSE-214, was observed after 24h exposure to 40 microg rPhlA protein.
