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1.
J Pediatr Orthop B ; 23(1): 55-8, 2014 Jan.
Article in English | MEDLINE | ID: mdl-24157570

ABSTRACT

We report a case of primary pyomyositis in the obturator internus muscle. Pyomyositis involving muscles around the hip needs to be differentiated from septic arthritis because these infections show similar symptoms. Management with antibiotics can avoid the need for surgical intervention. Uncontrolled pyomyosistis can cause sequelae such as septic shock, osteomyelitis of adjacent bone, and septic arthritis. Awareness of this condition will facilitate correct diagnosis and early treatment.


Subject(s)
Arthritis, Infectious/diagnosis , Diagnostic Imaging/methods , Hip Joint , Psoas Muscles/physiopathology , Pyomyositis/diagnosis , Staphylococcal Infections/diagnosis , Anti-Bacterial Agents/therapeutic use , Arthralgia/diagnostic imaging , Arthralgia/drug therapy , Arthralgia/physiopathology , Arthritis, Infectious/drug therapy , Child , Disease Progression , Emergency Service, Hospital , Follow-Up Studies , Humans , Infusions, Intravenous , Magnetic Resonance Imaging/methods , Male , Psoas Muscles/microbiology , Pyomyositis/drug therapy , Risk Assessment , Severity of Illness Index , Staphylococcal Infections/drug therapy , Tomography, X-Ray Computed/methods , Treatment Outcome , Ultrasonography, Doppler/methods
3.
Clin Rheumatol ; 26(8): 1284-92, 2007 Aug.
Article in English | MEDLINE | ID: mdl-17205215

ABSTRACT

The objective of this study is to examine the differential expression of mast cell tryptase and its receptor, protease-activated receptor-2 (PAR-2), in the synovium and synovial fluid of patients with rheumatoid arthritis (RA) and osteoarthritis (OA). Biochemical and immunohistochemical analyses were performed to determine whether the trypsin-like protease in the synovium is identical to mast cell tryptase. The effects of mast cell tryptase on the proliferation of synovial fibroblast-like cells (SFCs) and the release of IL-8 thereof were evaluated by the [3H]-thymidine incorporation and ELISA, respectively. The trypsin-like protease in the synovium of RA patients was identical to human mast cell tryptase, which was composed of two subunits: 33 and 34 kDa. The 33- and 34-kDa proteins are different glycosylated forms of the 31-kDa protein, which was unglycosylated. Mast cell tryptase activity in RA synovial fluid was significantly higher than that in OA synovial fluid, while their activities and expression in the synovium were similar. Expression of PAR-2 mRNA in the synovium was higher in RA than in OA. Mast cell tryptase containing the unglycosylated 31-kDa subunit was the predominant form in synovial fluid. RA patients had higher amounts of this subunit in their synovial fluid than OA patients. Mast cell tryptase and PAR-2 activating peptide stimulated the proliferation of SFCs and release of IL-8 from these cells. Mast cell tryptase secretion into RA synovial fluid is higher than OA synovial fluid. Mast cell tryptase in synovial fluid stimulates the proliferation of SFCs and the release of pro-inflammatory cytokines via PAR-2, which may contribute to exacerbation of synovitis in RA.


Subject(s)
Arthritis, Rheumatoid/metabolism , Osteoarthritis/metabolism , Receptor, PAR-2/metabolism , Synovial Membrane , Synovitis/metabolism , Tryptases/metabolism , Adult , Aged , Aged, 80 and over , Female , Humans , Knee Joint/pathology , Male , Middle Aged , RNA, Messenger , Synovial Fluid/cytology , Synovial Fluid/metabolism , Synovial Membrane/cytology , Synovial Membrane/metabolism , Synovial Membrane/pathology , Tryptases/chemistry
4.
Mod Rheumatol ; 15(6): 450-3, 2005.
Article in English | MEDLINE | ID: mdl-17029112

ABSTRACT

We report the case of a 42-year-old Japanese woman with unusual diaphyseal dysplasia of bilateral femora. Radiographs showed thickening and sclerosis of the cortex with resultant enlargement of the diaphysis, unclear demarcation of the surface of the cortex, and no periosteal reaction. These changes were found on the left femur at the first presentation, and those on the right femur developed within several years. Although this patient partly presented characteristics of Ribbing disease and Camurati-Engelmann disease, the focal involvement of bilateral femora suggested an unknown pathogenesis.

5.
Mil Med ; 168(6): 442-6, 2003 Jun.
Article in English | MEDLINE | ID: mdl-12834132

ABSTRACT

This prospective study was designed to evaluate whether static stretching can prevent training-related injuries in Japan Ground Self-Defense Force military recruits. A total of 901 recruits between 1996 and 1998 were divided into two groups. Of which, 518 recruits were assigned to the stretching group and practiced static stretching before and after each physical training session. The control subjects (383 recruits in the nonstretching group) did not stretch statically prior to exercise. The static stretching consisted of 18 exercises. We collected injury data from medical records and assessed the incidence and the location of injury. The total injury rate was almost the same between two groups; however, the incidences of muscle/tendon injury and low back pain were significantly lower in the stretching group (p < 0.05). Static stretching decreased the incidence of muscle-related injuries but did not prevent bone or joint injuries.


Subject(s)
Athletic Injuries/prevention & control , Exercise Therapy , Military Personnel , Adolescent , Adult , Athletic Injuries/epidemiology , Chi-Square Distribution , Humans , Incidence , Male , Prospective Studies , Treatment Outcome
6.
J Biol Chem ; 278(30): 27406-12, 2003 Jul 25.
Article in English | MEDLINE | ID: mdl-12754259

ABSTRACT

To find a novel human ion channel gene we have executed an extensive search by using a human genome draft sequencing data base. Here we report a novel two-pore domain K+ channel, TRESK (TWIK-related spinal cord K+ channel). TRESK is coded by 385 amino acids and shows low homology (19%) with previously characterized two-pore domain K+ channels. However, the most similar channel is TREK-2 (two-pore domain K+ channel), and TRESK also has two pore-forming domains and four transmembrane domains that are evolutionarily conserved in the two-pore domain K+ channel family. Moreover, we confirmed that TRESK is expressed in the spinal cord. Electrophysiological analysis demonstrated that TRESK induced outward rectification and functioned as a background K+ channel. Pharmacological analysis showed TRESK to be inhibited by previously reported K+ channel inhibitors Ba2+, propafenone, glyburide, lidocaine, quinine, quinidine, and triethanolamine. Functional analysis demonstrated TRESK to be inhibited by unsaturated free fatty acids such as arachidonic acid and docosahexaenoic acid. TRESK is also sensitive to extreme changes in extracellular and intracellular pH. These results indicate that TRESK is a novel two-pore domain K+ channel that may set the resting membrane potential of cells in the spinal cord.


Subject(s)
Potassium Channels/biosynthesis , Potassium Channels/physiology , Amino Acid Sequence , Analgesics, Non-Narcotic/pharmacology , Animals , Anti-Arrhythmia Agents/pharmacology , Arachidonic Acid/pharmacology , Barium/pharmacology , Cell Line , Cloning, Molecular , Docosahexaenoic Acids/pharmacology , Electrophysiology , Ethanolamines/pharmacology , Fatty Acids/metabolism , Fatty Acids, Nonesterified/metabolism , Glyburide/pharmacology , Humans , Hydrogen-Ion Concentration , Lidocaine/pharmacology , Mice , Models, Biological , Molecular Sequence Data , Patch-Clamp Techniques , Phylogeny , Potassium Channels/chemistry , Propafenone/pharmacology , Protein Structure, Tertiary , Quinidine/pharmacology , Quinine/pharmacology , Reverse Transcriptase Polymerase Chain Reaction , Spinal Cord/metabolism , Tissue Distribution , Transfection
7.
FEBS Lett ; 512(1-3): 230-4, 2002 Feb 13.
Article in English | MEDLINE | ID: mdl-11852086

ABSTRACT

We report identification and characterization of Kv6.3, a novel member of the voltage-gated K(+) channel. Reverse transcriptase-polymerase chain reaction analysis indicated that Kv6.3 was highly expressed in the brain. Electrophysiological studies indicated that homomultimeric Kv6.3 did not yield a functional voltage-gated ion channel. When Kv6.3 and Kv2.1 were co-expressed, the heteromultimeric channels displayed the decreased rate of deactivation compared to the homomultimeric Kv2.1 channels. Immunoprecipitation studies indicated that Kv6.3 bound with Kv2.1 in co-transfected cells. These results indicate that Kv6.3 is a novel member of the voltage-gated K(+) channel which functions as a modulatory subunit.


Subject(s)
Potassium Channels, Voltage-Gated , Potassium Channels/metabolism , Amino Acid Sequence , Cloning, Molecular , Delayed Rectifier Potassium Channels , Electric Conductivity , Humans , Ion Channel Gating , Molecular Sequence Data , Potassium Channels/classification , Potassium Channels/genetics , Protein Subunits , Sequence Homology, Amino Acid , Shab Potassium Channels , Tissue Distribution
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