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1.
Scand J Med Sci Sports ; 28(1): 246-251, 2018 Jan.
Article in English | MEDLINE | ID: mdl-28207961

ABSTRACT

Previous history of medial tibial stress syndrome (MTSS) is a risk factor for MTSS relapse, which suggests that there might be some physical factors that are related to MTSS development in runners with a history of MTSS. The relationship between MTSS and muscle stiffness can be assessed in a cross-sectional study that measures muscle stiffness in subjects with a history of MTSS, who do not have pain at the time of measurement, and in those without a history of MTSS. The purpose of this study was to compare the shear elastic modulus, which is an index of muscle stiffness, of all posterior lower leg muscles of subjects with a history of MTSS and those with no history and investigate which muscles could be related to MTSS. Twenty-four male collegiate runners (age, 20.0±1.7 years; height, 172.7±4.8 cm; weight, 57.3±3.7 kg) participated in this study; 14 had a history of MTSS, and 10 did not. The shear elastic moduli of the lateral gastrocnemius, medial gastrocnemius, soleus, peroneus longus, peroneus brevis, flexor hallucis longus, flexor digitorum longus, and tibialis posterior were measured using shear wave elastography. The shear elastic moduli of the flexor digitorum longus and tibialis posterior were significantly higher in subjects with a history of MTSS than in those with no history. However, there was no significant difference in the shear elastic moduli of other muscles. The results of this study suggest that flexor digitorum longus and tibialis posterior stiffness could be related to MTSS.


Subject(s)
Elastic Modulus , Medial Tibial Stress Syndrome/physiopathology , Muscle, Skeletal/physiopathology , Running , Cross-Sectional Studies , Humans , Male , Young Adult
2.
Epidemiol Infect ; 143(12): 2660-5, 2015 Sep.
Article in English | MEDLINE | ID: mdl-25578079

ABSTRACT

Corynebacterium ulcerans (toxigenic C. ulcerans) produces the diphtheria toxin, which causes pharyngeal and cutaneous diphtheria-like disease in people, and this bacterium is commonly detected in dogs and cats that are reared at home. It is considered dangerous when a carrier animal becomes the source of infection in people. To investigate the carrier situation of toxigenic C. ulcerans of cats bred in Japan, bacteria were isolated from 37 cats with a primary complaint of rhinitis in 16 veterinary hospitals in Osaka. Toxigenic C. ulcerans was detected in two of the cats. By drug sensitivity testing, the detected bacterium was sensitive to all investigated drugs, except clindamycin. It appears necessary to create awareness regarding toxigenic C. ulcerans infection in pet owners because this bacterium is believed to be the causative organism for rhinitis in cats.


Subject(s)
Carrier State/veterinary , Cat Diseases/microbiology , Corynebacterium/isolation & purification , Rhinitis/veterinary , Animals , Anti-Bacterial Agents/pharmacology , Bacterial Toxins/genetics , Bacterial Toxins/pharmacology , Carrier State/microbiology , Cats , Cell Survival/drug effects , Corynebacterium/drug effects , Corynebacterium/genetics , Japan , Male , Microbial Sensitivity Tests , Rhinitis/microbiology , Vero Cells
3.
J Mol Biol ; 287(2): 221-37, 1999 Mar 26.
Article in English | MEDLINE | ID: mdl-10080887

ABSTRACT

Heterogeneous nuclear ribonucleoprotein (hnRNP) D0 has two ribonucleoprotein (RNP)-type RNA-binding domains (RBDs), each of which can bind solely to the UUAG sequence specifically. The structure of the N-terminal RBD (RBD1) determined by NMR is presented here. It folds into a compact alphabeta structure comprising a four-stranded antiparallel beta-sheet packed against two alpha-helices, which is characteristic of the RNP-type RBDs. Special structural features of RBD1 include N-capping boxes for both alpha-helices, a beta-bulge in the second beta-strand, and an additional short antiparallel beta-sheet coupled with a beta-turn-like structure in a loop. Two hydrogen bonds which restrict the positions of loops were identified. Backbone resonance assignments for RBD1 complexed with r(UUAGGG) revealed that the overall folding is maintained in the complex. The candidate residues involved in the interactions with RNA were identified by chemical shift perturbation analysis. They are located in the central and peripheral regions of the RNA-binding surface composed of the four-stranded beta-sheet, loops, and the C-terminal region. It is suggested that non-specific interactions with RNA are performed by the residues in the central region of the RNA-binding surface, while specific interactions are performed by those in the peripheral regions. It was also found that RBD1 has the ability to inhibit the formation of the quadruplex structure.


Subject(s)
RNA/chemistry , Ribonucleoproteins/chemistry , Amino Acid Sequence , Binding Sites , HeLa Cells , Heterogeneous-Nuclear Ribonucleoproteins , Humans , Hydrogen Bonding , Magnetic Resonance Spectroscopy , Models, Molecular , Molecular Sequence Data , Protein Folding , Protein Structure, Secondary , RNA-Binding Proteins/chemistry
4.
Nucleic Acids Symp Ser ; (34): 59-60, 1995.
Article in English | MEDLINE | ID: mdl-8841551

ABSTRACT

Thermodynamic parameters for duplex formation were determined from CD melting curves for r(GGACGAGUCC)2 and d(GGACGAGTCC)2, both of which have been demonstrated to form two consecutive 'sheared' A:G base pairs at the center by our previous studies. The parameters were determined also for r(GGACUAGUCC)2 and d(GGACTAGTCC)2, where the A:G mismatches are replaced by Watson-Crick A:U(T) base pairs. Thermodynamic properties for duplex formation are compared between the sheared and the Watson-Crick base pairs, and between RNA and DNA. Difference in the thermodynamic stability is analyzed and discussed in terms of enthalpy and entropy changes.


Subject(s)
DNA/chemistry , RNA/chemistry , Base Composition , Base Sequence , Circular Dichroism , Entropy , Molecular Structure , Nucleic Acid Conformation , Oligodeoxyribonucleotides/chemistry , Oligoribonucleotides/chemistry , Thermodynamics
5.
Nucleic Acids Symp Ser ; (34): 197-8, 1995.
Article in English | MEDLINE | ID: mdl-8841620

ABSTRACT

The CD study of r(GGAGGAA) has indicated that it forms a higher order structure upon either increase of the strand concentration or addition of K+. Gel electrophoresis showed that a high molecular weight species is formed in the presence of K+. The NMR study revealed a nearly 1:1 equilibrium of two kinds of higher order structures at the strand concentration of 2.1 mM and 100 mM Na+. This equilibrium shifted drastically upon addition of K+, and only one structure remained at 40 mM K+. It is suggested that the structure formed by r(GGAGGAA) in the presence of K+ is a new type of RNA quadruplex, where an A-quartet stabilized by mutual hydrogen bonding among the four adenine bases is sandwiched by conventional G-quartets.


Subject(s)
RNA/chemistry , Adenine/chemistry , Base Sequence , Circular Dichroism , Guanine/chemistry , Hydrogen Bonding , Magnetic Resonance Spectroscopy , Molecular Structure , Nucleic Acid Conformation , Oligoribonucleotides/chemical synthesis , Oligoribonucleotides/chemistry , Potassium
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