OBJECTIVES: We examined the agreement between the Autism Diagnostic Observation Schedule (ADOS) and the Childhood Autism Rating Scale (CARS) in the diagnosis of autism spectrum disorder. METHODS: The ADOS and CARS scores of 78 children were retrospectively collected from a chart review. A correlation analysis was performed to examine the concurrent validity between the two measures. Using the receiver operating characteristic (ROC) curve, we determined the optimal cut-off score of the CARS for identifying autism spectrum disorder. RESULTS: The CARS score was significantly correlated with the ADOS score (r=0.808, p < 0.001). Taking ADOS as the ideal standard, the optimal cut-off scores of CARS for identifying autism and autism spectrum were 30 and 24.5, respectively. CONCLUSION: We determined the optimal cut-off scores of CARS for screening and diagnosing autism spectrum disorder.
Appointments and Schedules* ; Autism Spectrum Disorder* ; Autistic Disorder* ; Child ; Diagnosis* ; Humans ; Mass Screening ; Retrospective Studies ; ROC Curve

PURPOSE: We designed this study to demonstrate the pathophysiology of hemophilic arthropathy (HA) by creating an animal model for determining the effect of repeated intraarticular bleeding in the synovium and articular cartilage. MATERIALS AND METHODS: 20 normal male New Zealand white rabbits were used for this study. We injected 1 ml of autologous blood from the ear vein of the rabbits into the right knee joint three timeds a week for 18 weeks, and we injected 1 ml of normal saline into the left knee joint three times a week for 18 weeks as a control group. We examined the pathologic changes by microscopy and plain X-ray, and we determined the mRNA expression of proinflammatory cytokines in the synovium of the HA by performing real time RT-PCR at the 11th week and 18th week after starting blood-injection. We also examined the GAG and the PGE2 production in cultured chondrocytes that were extracted from the HA knees. RESULTS: At the 11th week, after blood injection there were no remarkable gross changes in the HA knees and the control knee joints. At the 18th weeks, the experimental knee joints (HA knees) showed grossly swelling and degenerative changes by X-ray. The infiltration of inflammatory cells and the synovial proliferation in the HA knee joints were compared with that in the control knee joints by microscopic examination. The expressions of the mRNA of TNF-alpha, IL-1, MMP-1 and MMP-3 in the HA synovium were increased, as determined by real time RT- PCR, as compared with that in the control knee. In the cultured chondrocytes, the GAG production was decreased and the PGE2 was increased, but the MMP-1 and MMP-3 were not changed, as determined by ELISA. CONCLUSION: Our results showed that the GAG production of chondrocytes of the HA knees was decreased and there was increased PGE2, so that the cartilage degeneration by intra-articular bleeding was caused by the decreased metabolism of chondrocytes rather than by increased catabolism of the chondrocytes. We suggest that HA was associated with synovitis and cartilage degeneration, but decreased cartilage metabolism was the major mechanism of HA.
Animals ; Cartilage ; Chondrocytes ; Cytokines ; Dinoprostone ; Ear ; Hemorrhage ; Humans ; Interleukin-1 ; Knee ; Knee Joint ; Male ; Microscopy ; Models, Animal ; Polymerase Chain Reaction ; Rabbits ; RNA, Messenger ; Synovial Membrane ; Synovitis ; Tumor Necrosis Factor-alpha ; Veins

Campylobacter jejuni isolates from diarrhea patients and chickens in 2008 in Iksan, Korea were tested for biochemical characteristics, and for possession of genes hipO, mutated gyrA, and cdtB. Among the chickens tested 52% carried C. jejuni. All 28 patient isolates and 48 chickens isolates had typical biochemical characteristics, except for nalidixic acid resistance. All isolates from patients and chickens were resistant to ciprofloxacin, and had mutated gyrA gene indicating good correlation of the two tests. Analysis of pulsed-field gel electrophoresis (PFGE) pattern of SmaI-restricted DNA of 53 isolates showed 14 clusters. Twenty-eight patient isolates and two chicken isolates (57%) showed an identical pattern (cluster 9). Chicken isolates C37 and C48 (cluster 2), C31 and C33 (cluster 3), C29, C34, C35, and C36 (cluster 4), and C43, C44 (cluster 6) had identical patterns. All patient isolates, compared to 87% and 80% of chicken isolates, were susceptible to amikacin and chloramphenicol, respectively. Antibiotics with the lowest MIC90 were imipenem, gentamicin, and erythromycin, whereas, those with the highest were ampicillin and tetracycline. In conclusion, C. jejuni carriage rate of chickens in Iksan, Korea, was high, all 28 isolates from patients and two from chickens were an identical clone, whereas isolates from patients and remaining chickens were different clones with only 62% similarity, all isolates had hipO and cdtB genes, and all isolates were resistant to ciprofloxacin.
Amikacin ; Ampicillin ; Anti-Bacterial Agents ; Bacterial Toxins ; Campylobacter ; Campylobacter jejuni ; Chickens ; Chloramphenicol ; Ciprofloxacin ; Clone Cells ; Diarrhea ; DNA ; Electrophoresis, Gel, Pulsed-Field ; Erythromycin ; Genotype ; Gentamicins ; Humans ; Imipenem ; Korea ; Nalidixic Acid ; Tetracycline

Type 1 myotonic dystrophy (DM1) is an autosomal-dominant inherited disorder with a multisystem involvement, caused by an abnormal expansion of the CTG sequence of the dystrophic myotonia protein kinase (DMPK) gene. DM1 is a variable multisystem disorder with muscular and nonmuscular abnormalities. Increasingly, endocrine abnormalities, such as gonadal, pancreatic, and adrenal dysfunction are being reported. But, Electrolytes imbalance is a very rare condition in patients with DM1 yet. Herein we present a 42-yr-old Korean male of DM1 with abnormally elevated serum sodium and potassium. The patient had minimum volume of maximally concentrated urine without water loss. It was only cured by normal saline hydration. The cause of hypernatremia was considered by primary hypodipsia. Hyperkalemic conditions such as renal failure, pseudohyperkalemia, cortisol deficiency and hyperkalemic periodic paralysis were excluded. Further endocrine evaluation suggested selective hyperreninemic hypoaldosteronism as a cause of hyperkalemia.
Adult ; Humans ; Hyperkalemia/complications/*diagnosis ; Hypernatremia/complications/*diagnosis ; Hypoaldosteronism/complications/diagnosis ; Kidney Concentrating Ability ; Male ; Myotonic Dystrophy/complications/*diagnosis/*genetics ; Potassium/blood ; Protein-Serine-Threonine Kinases/*genetics ; Sodium/blood

Clathrin-coated vesicles (CCVs) are involved in protein and lipid trafficking between intracellular compartments in eukaryotic cells. CCVs are composed of clathrin and assembly proteins. The clathrin assembly protein lymphoid myeloid leukemia (CALM) gene, encodes a homologoue of the neuronal clathrin assembly protein AP180. In this study, we characterized the properties of the CALM expressed in E. coli. The molecular weight of bacterially expressed GST-CALM fusion protein was approximately 105 kD on SDS-PAGE. The CALM protein could promote clathrin triskelia into clathrin cages and could bind the preformed clathrin cage. However, 33 kD N-terminal domain of CALM could not bind pre-assembled clathrin cages, but assemble clathrin triskelia into clathrin cages. The CALM protein was bound to SH3 domain through N-terminal domain1, in vitro. The CALM protein is proteolyzed by caspase 3, caspase 8 and calpain through C-terminal domain.
Animal ; Antibodies, Monoclonal ; Calpain/chemistry ; Caspases/chemistry ; Clathrin-Coated Vesicles/metabolism* ; Electrophoresis, Polyacrylamide Gel ; Escherichia coli/metabolism ; Escherichia coli/genetics ; Female ; Glutathione Transferase/genetics* ; Mice ; Mice, Inbred BALB C ; Nerve Tissue Proteins/metabolism ; Nerve Tissue Proteins/metabolism ; Nerve Tissue Proteins/chemistry* ; Phosphoproteins/metabolism ; Phosphoproteins/genetics ; Phosphoproteins/chemistry* ; Protein Binding ; Rabbits ; Recombinant Fusion Proteins/metabolism ; Recombinant Fusion Proteins/genetics ; Recombinant Fusion Proteins/chemistry* ; src Homology Domains

As the usage of biologics for rheumatic diseases increases, such as rheumatoid arthritis and ankylosing spondylitis, various cutaneous adverse events are also being increasingly reported. We experienced a case of development of vitiligo during a TNF-alpha antagonist therapy in a 22-year-old woman with rheumatoid arthritis. The patient was presented with vitiligo lesions on the dorsum of both hands after 1 month of treatment with etanercept. Vitiligo improved with topical tacrolimus ointment and excimer laser treatment without the discontinuation of etanercept. No clearly defined mechanism for vitiligo induced by TNF-alpha antagonist exits. However, considering that vitiligo is an autoimmune disorder, the development of this skin lesion in association with the TNF-alpha antagonist could be explained by a paradoxical induction of the autoimmune process.
Arthritis, Rheumatoid ; Biological Agents ; Female ; Hand ; Humans ; Immunoglobulin G ; Lasers, Excimer ; Receptors, Tumor Necrosis Factor ; Rheumatic Diseases ; Skin ; Spondylitis, Ankylosing ; Tacrolimus ; Tumor Necrosis Factor-alpha ; Vitiligo ; Young Adult ; Etanercept

An overlap syndrome is a combination of major features of more than one connective tissue diseases which is presented in the same patient. An overlap syndrome of rheumatoid arthritis (RA) and polymyositis (PM) which involved the upper pharyngeal muscle has not been reported in Korea. Herein, we report a rare case of a patient with a long-history RA presenting proximal muscle weakness and swallowing difficulty, who was successfully treated with a high-dose of corticosteroid, azathioprine and tacrolimus.
Arthritis, Rheumatoid ; Azathioprine ; Connective Tissue Diseases ; Deglutition ; Humans ; Korea ; Muscle Weakness ; Pharyngeal Muscles ; Polymyositis ; Tacrolimus

BACKGROUND: Glomerular diseases of diverse origins are characterized by heavy proteinuria and tubulointerstitial changes in pathology. Numerous studies have recently demonstrated that interstitial fibrosis and tubular atrophy are better predictors of renal disease progression compared with glomerular pathology. One of the important mechanisms of these tubulointerstitial injury is tubulointerstitial damage due to increased protein trafficking across the proximal tubular epithelial cells. We tested the hypothesis that tubular cells exposed to high concentration of protein express TGF-beta, which can be related to tubulointerstitial fibrosis, and Fas antigen, which can be associated with tubular cell apoptosis. METHODS: Cultured human proximal tubular cells were incubated with varying concentrations of BSA (1, 10 mg/mL) and nephrotic range proteinuria, due to diabetic nephropathy (1, 10 mg/mL), with or without inactivation of complement. After 24 hr-incubation period, the expressions of TGF-beta and Fas mRNA were examined by RT-PCR. RESULTS: The amount of expression of TGF-beta was increased in BSA 10 mg/mL group (0.78+/-0.12, p=0.016) and in diabetic proteinuria 10 mg/mL group (0.7+/-0.08, p=0.012) compared to control group which was incubated in medium alone (0.48+/-0.02), and the amount of expression of Fas was increased in BSA 10 mg/mL group (0.97+/-0.09, p=0.021) and showed increased tendency in diabetic proteinuria 10 mg/mL group (0.94+/-0.14, p=0.067) also. Furthermore, the anti TGF-beta antibody ameliorated the increased albumin-induced expression of Fas. CONCLUSION: Collectively, our results showed that protein overload increased the expression of TGF-beta & Fas, which can play an important role in tubulointerstitial atrophy by inducing apoptosis of renal tubular cells.
Antigens, CD95 ; Apoptosis ; Atrophy ; Complement System Proteins ; Diabetic Nephropathies ; Disease Progression ; Epithelial Cells ; Fibrosis ; Humans* ; Pathology ; Protein Transport ; Proteinuria* ; RNA, Messenger ; Transforming Growth Factor beta*

BACKGROUND: Glomerular diseases of diverse origins are characterized by heavy proteinuria and tubulointerstitial changes in pathology. Numerous studies have recently demonstrated that interstitial fibrosis and tubular atrophy are better predictors of renal disease progression compared with glomerular pathology. One of the important mechanisms of these tubulointerstitial injury is tubulointerstitial damage due to increased protein trafficking across the proximal tubular epithelial cells. We tested the hypothesis that tubular cells exposed to high concentration of protein express TGF-beta, which can be related to tubulointerstitial fibrosis, and Fas antigen, which can be associated with tubular cell apoptosis. METHODS: Cultured human proximal tubular cells were incubated with varying concentrations of BSA (1, 10 mg/mL) and nephrotic range proteinuria, due to diabetic nephropathy (1, 10 mg/mL), with or without inactivation of complement. After 24 hr-incubation period, the expressions of TGF-beta and Fas mRNA were examined by RT-PCR. RESULTS: The amount of expression of TGF-beta was increased in BSA 10 mg/mL group (0.78+/-0.12, p=0.016) and in diabetic proteinuria 10 mg/mL group (0.7+/-0.08, p=0.012) compared to control group which was incubated in medium alone (0.48+/-0.02), and the amount of expression of Fas was increased in BSA 10 mg/mL group (0.97+/-0.09, p=0.021) and showed increased tendency in diabetic proteinuria 10 mg/mL group (0.94+/-0.14, p=0.067) also. Furthermore, the anti TGF-beta antibody ameliorated the increased albumin-induced expression of Fas. CONCLUSION: Collectively, our results showed that protein overload increased the expression of TGF-beta & Fas, which can play an important role in tubulointerstitial atrophy by inducing apoptosis of renal tubular cells.
Antigens, CD95 ; Apoptosis ; Atrophy ; Complement System Proteins ; Diabetic Nephropathies ; Disease Progression ; Epithelial Cells ; Fibrosis ; Humans* ; Pathology ; Protein Transport ; Proteinuria* ; RNA, Messenger ; Transforming Growth Factor beta*

BACKGROUND: Blood-dialyzer membrane interaction in hemodialysis has the potential to activate blood coagulation and fibrinolysis, and it might elicit production of inflammatory cytokine such as TNF-alpha by monocytes activation. The aim of the present study was to; i) assess changes in coagulation status, fibrinolytic activity and plasma level of TNF-alpha during hemodialysis; ii) determine whether the extent of activation is dependent on the dialyzer material used. METHODS: Twenty-five end-stage renal failure patients who had undergone maintenance hemodialysis were included in the study. Patients were randomly divided into two groups; one using hemophan dialyzer membrane (n=13) and the other using polysulfone dialyzer membrane (n=12). On sixth dialysis session, blood samples were obtained before and at the end of hemodialysis. Thrombin-antithrombin complex (TAT) and D-dimer, each reflecting in vivo thrombin generation and fibrin degradation product respectively, were measured for coagulatory and fibrinolytic activity. Tissue plasminogen activator (tPA), plasminogen activator inhibitor-1(PAI-1), and fibrinogen were measured. Activated partial thromboplastin time (aPTT) was measured for efficancy of anticoagulant. Plasma level of TNF-alpha was also measured. RESULTS: During hemodialysis, plasma level of TNF-alpha did not change. Between hemophan dialysis and polysulfone dialysis group, the change in plasma level of TNF-alpha (delta TNF-alpha ) was not different. Significant changes were observed in aPTT, fibrinogen, TAT, D-dimer, tPA during hemodialysis (p<0.05) except in PAI-1 (p=0.71). Between two groups, changes in aPTT, fibrinogen, D-dimer, PAI-1 and tPA (delta aPTT, delta fibrinogen, delta D-dimer, delta PAI-1, delta tPA) were not different (p>0.05). However, the change in TAT (delta TAT) was significantly lower in polysulfone dialysis group (p=0.049). CONCLUSION: Hemodialysis enhances coagulatory activity despite the use of anticoagulant and also enhances fibrinolytic activity, which is likely the result of tPA release. In activation of coagulatory system, biocompatibility of polysulfone membrane is superior to that of hemophan membrane. Plasma level of TNF-alpha did not change during hemodialysis, further study should be considered.
Blood Coagulation* ; Dialysis ; Fibrin ; Fibrinogen ; Fibrinolysis ; Humans ; Kidney Failure, Chronic ; Membranes* ; Monocytes ; Partial Thromboplastin Time ; Plasma ; Plasminogen Activator Inhibitor 1 ; Plasminogen Activators ; Renal Dialysis ; Thrombin ; Tissue Plasminogen Activator ; Tumor Necrosis Factor-alpha*