Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 4 de 4
Filter
Add more filters











Database
Language
Publication year range
1.
NeuroRehabilitation ; 29(1): 23-7, 2011.
Article in English | MEDLINE | ID: mdl-21876292

ABSTRACT

PURPOSE: This case study was conducted to highlight the clinical and radiological features of a patient with progressive neuromuscular scoliosis before and after robo-horseback riding therapy (HBRT). DESIGN: A clinical, laboratory, and radiological analysis of a single case. SUBJECT: An 11-year-old child, dignosed right thoracolumbar neuromuscular scoliosis secondary to cerebral palsy. METHOD: The child received a 5-week course of robo-HBRT, comprising of 60-minute periods a day, five times a week. Postural alignment was determined by Cobb's method. A real-time magnetic resonance imaging (MRI) was performed to determine the robo-HBRT-induced changes in cross-sectional area (CSA) of bilateral thoracic (T2) and lumbar (L2) paraspinalis. Clinical tests including the standard Gross Motor Function Measure (GMFM) and manual muscle testing (MMT) with the Lafayette Manual Muscle Tester were used to compare the intervention-related changes in motor performance and power. The surface EMG was also used to examine therapy-induced changes in muscle activity amplitude for bilateral T2 and L2 paraspinalis and rectus abdominis muscles. RESULTS: Clinical motor and strength scores increased after the intervention. Radiographic Cobb's angle, MRI, and electromyographic amplitude data demonstrated notably enhanced spinal alignment and muscle fiber CSA and symmetry, respectively. CONCLUSIONS: This is the first study to provide evidence of the therapeutic efficacy of a novel form of robo-HBRT on motor function and associated structural and motor control improvements, thus suggesting a method of augmenting therapy in neuromuscular scoliosis.


Subject(s)
Equine-Assisted Therapy/methods , Muscle, Skeletal/physiopathology , Robotics/methods , Scoliosis/rehabilitation , Child , Electromyography , Humans , Magnetic Resonance Imaging , Male , Muscle Strength/physiology , Muscle, Skeletal/diagnostic imaging , Scoliosis/pathology , Severity of Illness Index , Spinal Cord/diagnostic imaging , Spinal Cord/pathology , Spinal Cord/physiopathology , Tomography, X-Ray Computed/methods , Treatment Outcome
2.
PLoS One ; 6(2): e17203, 2011 Feb 15.
Article in English | MEDLINE | ID: mdl-21347244

ABSTRACT

BACKGROUND: Apolipoprotein E receptor 2 (ApoEr2) is a postsynaptic protein involved in long-term potentiation (LTP), learning, and memory through unknown mechanisms. We examined the biological effects of ApoEr2 on synapse and dendritic spine formation-processes critical for learning and memory. METHODOLOGY/PRINCIPAL FINDINGS: In a heterologous co-culture synapse assay, overexpression of ApoEr2 in COS7 cells significantly increased colocalization with synaptophysin in primary hippocampal neurons, suggesting that ApoEr2 promotes interaction with presynaptic structures. In primary neuronal cultures, overexpression of ApoEr2 increased dendritic spine density. Consistent with our in vitro findings, ApoEr2 knockout mice had decreased dendritic spine density in cortical layers II/III at 1 month of age. We also tested whether the interaction between ApoEr2 and its cytoplasmic adaptor proteins, specifically X11α and PSD-95, affected synapse and dendritic spine formation. X11α decreased cell surface levels of ApoEr2 along with synapse and dendritic spine density. In contrast, PSD-95 increased cell surface levels of ApoEr2 as well as synapse and dendritic spine density. CONCLUSIONS/SIGNIFICANCE: These results suggest that ApoEr2 plays important roles in structure and function of CNS synapses and dendritic spines, and that these roles are modulated by cytoplasmic adaptor proteins X11α and PSD-95.


Subject(s)
Dendritic Spines/metabolism , LDL-Receptor Related Proteins/metabolism , Synapses/metabolism , Adaptor Proteins, Signal Transducing/metabolism , Animals , COS Cells , Chlorocebus aethiops , Coculture Techniques , Cytoplasm/metabolism , Disks Large Homolog 4 Protein , Extracellular Space/metabolism , Guanylate Kinases/metabolism , Hippocampus/cytology , Humans , LDL-Receptor Related Proteins/chemistry , LDL-Receptor Related Proteins/deficiency , Membrane Proteins/metabolism , Mice , Nerve Tissue Proteins/metabolism , Protein Structure, Tertiary , Receptors, AMPA/metabolism
3.
Rapid Commun Mass Spectrom ; 21(8): 1468-74, 2007.
Article in English | MEDLINE | ID: mdl-17385792

ABSTRACT

Some experimental factors affecting the resolution in glycerol infrared matrix-assisted laser desorption/ionization (IR-MALDI) time-of-flight (TOF) mass spectrometry were investigated. Loading the sample inside a cavity covered with a grid was found to improve the resolving power as reported previously, although not to the extent attainable in UV-MALDI using the same instrument. The resolving power improved as the laser spot area at the sample position got larger, becoming almost comparable with that in UV-MALDI when the spot area was a little larger than the cavity size. Reduced concentration of the ablated materials in the acceleration region with the use of the grid and large irradiation area may be responsible for the enhanced resolution. In addition, the threshold laser fluences measured in this work were lower than those reported in the literature and tended to decrease more rapidly as the irradiation area increased than predicted previously. The implication of similar threshold fluences for matrix and analyte ions is discussed in relation to the analyte ion formation mechanism.


Subject(s)
Glycerol/chemistry , Infrared Rays , Lasers , Spectrometry, Mass, Electrospray Ionization/methods , Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization/instrumentation , Tandem Mass Spectrometry
4.
Rapid Commun Mass Spectrom ; 21(3): 359-68, 2007.
Article in English | MEDLINE | ID: mdl-17206742

ABSTRACT

A tandem time-of-flight mass spectrometer was built for photodissociation (PD) of singly protonated peptides and small proteins generated by matrix-assisted laser desorption/ionization. PD was performed in a second source after deceleration of precursor ions. The delayed extraction/post-acceleration scheme was used for the product ions. For the PD at 193 nm of small singly protonated peptides, the present instrument showed much better sensitivity and resolution for product ions than the previous one (Moon JH, Yoon SH, Kim MS, Bull. Korean Chem. Soc. 2005; 26: 763) even though the overall spectral patterns obtained with the two instruments were similar. The present instrument was inferior in precursor ion selection and background noise level. PD was achieved for precursor ions as large as the singly protonated ubiquitin (m/z 8560.63), indicating that the photoexcitation is capable of supplying a sufficient amount of internal energy to dissociate large singly protonated proteins. As the precursor ion m/z increased, however, product ion signals deteriorated rather rapidly. As in the PD of small peptide ions with m/z around 1000, the types of the product ions generated from singly protonated peptides with m/z in the range 2000-4000 were mostly determined by the positions of arginine residues. Namely, a(n) and d(n) ions dominated when an arginine residue(s) was near the N-terminus while v(n), w(n), x(n) and y(n) dominated when the same residue(s) was near the C-terminus. In addition, d(n), v(n) and w(n) ions were generated according to the correlation rules previously observed in the collisionally activated dissociation. Isoleucine and leucine isomers could be easily distinguished based on the w(n) and d(n) ions.


Subject(s)
Lasers , Peptide Mapping/instrumentation , Peptides/chemistry , Photochemistry/instrumentation , Proteins/chemistry , Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization/instrumentation , Acceleration , Amino Acid Sequence , Equipment Design , Equipment Failure Analysis , Ions , Molecular Sequence Data , Peptide Mapping/methods , Peptides/analysis , Photochemistry/methods , Proteins/analysis , Protons , Reproducibility of Results , Sensitivity and Specificity , Sequence Analysis, Protein/instrumentation , Sequence Analysis, Protein/methods , Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization/methods
SELECTION OF CITATIONS
SEARCH DETAIL