Heat stroke, a medical emergency, occurs when the body's thermal regulation is upset and unable to dissipate adequate amounts of heat with a rise in body temperature. It is characterized by hyperyrexia, with a core temperature of 40degrees C or more, hot dry skin, and central nervous system disturbance and usually results in rhabdomyolysis and multiorgan failure. Our case, a 43-year-old healthy male, was caused by a marathon, half course, on a sunny day in late summer. He suddenly fell down on the road and was delivered to a nearby hospital, where a seizure developed. He was transfered to our hospital and then displayed Central Nervous System disturbance, hot dry skin, acute liver failure, rhabdomyolysis, anuric acute renal failure, and disseminated intravasculular coagulopathy. He was treated with general supportive care and hemofiltration. Despite the aggressive management, he died of shock on the fifth day after admission.
Acute Kidney Injury ; Adult ; Body Temperature ; Central Nervous System ; Emergencies ; Heat Stroke* ; Hemofiltration ; Hot Temperature* ; Humans ; Liver Failure, Acute ; Male ; Rhabdomyolysis ; Seizures ; Shock ; Skin

Spontaneous spinal epidural hemorrhage(SSEH) represent 0.3%~0.9% of spinal epidural-space-occupying lesions. The therapeutic outcome seems to be determined by the accuracy of the diagnosis and by the time interval between the onset of symptom and surgical decompression. Thus, SSEH is a rare spinal emergency and a diagnostic challenge. We experienced two such cases. In one case, the symptoms were confused with those for a ureter stone, aortic aneurysm, spinal cord infarction. That patient completely recovered spontaneously within 2 hours. In the other case, which was initially diagnosed incorrectly as a cerebral infarction, surgical decompression was performed. That patient recovered completely within 1 month.
Aortic Aneurysm ; Cerebral Infarction ; Decompression, Surgical ; Diagnosis ; Emergencies ; Hematoma, Epidural, Spinal* ; Humans ; Infarction ; Spinal Cord ; Ureter

As part of an initial inquiry into the function of the outer membrane proteins (OMPs) of Helicobacter pylori Korean strain 51, we have conducted an extensive proteome analysis via quadrupole time of flight (Q-TOF) mass spectrometry (MS). Fifty one OMPs of H. pylori were purified using sarcosine and resolved via two-dimensional electrophoresis with immobilized pH gradient strips. The most abundant proteins were observed in the alkaline pI regions (6.0~11.0) at molecular masses between 10~100 KDa. Here, 15 spots were identified, representing 9 types of genes (KHP0852, KHP0853, KHP1353, KHP1017, KHP0172, KHP0076, KHP0617, KHP1069, KHP0614) from the sarcosin-insoluble fraction of H. pylori 51. These may be employed in the characterization of the OMPs of H. pylori 51, which will help to identify new potential target proteins for vaccine development and drug therapy.
Electrophoresis ; Helicobacter ; Helicobacter pylori ; Mass Spectrometry ; Membrane Proteins ; Membranes ; Proteins ; Proteome ; Proton-Motive Force ; Sarcosine ; Sprains and Strains

The mouse model is alleged to be a useful tool for understanding of pathophysiological roles of Helicobacter pylori in the development of gastric disorders. However, it has been observed that H. pylori strains significantly differed in their fitness in mice and even mouse strains differed in their susceptibilities to a H. pylori strain. Bacterial components of H. pylori which could affect on its fitness in mice have to be elucidated for the establishment of the mouse model for H. pylori infections. In the comparison of colonization ability between two H. pylori Korean isolates, 51 (isolated from a patient with duodenal ulcer) and 52 (isolated from a patient with gastric cancer), 52 could colonize better than 51 on the gastric mucosa of mouse. Proteome components of H. pylori 52, as a good colonizer and H. pylori 51, as a poor one were quantitatively compared each other. Five bacterial proteins including catalase, urease subunit alpha/beta, enolase and ferritin, were up-regulated in 52. In addition, the respective proteome components of the two strains were also compared with their mouse-passaged homologous strains. Seven and five proteins, which included catalase, flagellin A/B in common, were up-regulated in mouse-adapted 51 and 52, respectively. Among the fourteen identified proteins, urease subunit alpha/beta, flagellin A/B, catalase, ferritin, superoxide dismutase and neutrophil-activation protein have been previously known to be necessary to gastric colonization of H. pylori in animal models. The other up-regulated proteins including enolase, elongation factor Tu and fructose-bisphosphate aldolase have been reported to be associated with acid tolerance of H. pylori. These data provide confirmatory evidence for the importance of those proteins in the development of H. pylori-associated gastric disorders.
Animals ; Bacterial Proteins ; Catalase ; Colon ; Ferritins ; Flagellin ; Fructose-Bisphosphate Aldolase ; Gastric Mucosa ; Helicobacter ; Helicobacter pylori ; Humans ; Mice ; Models, Animal ; Peptide Elongation Factor Tu ; Phosphopyruvate Hydratase ; Proteins ; Proteome ; Sprains and Strains ; Superoxide Dismutase ; Urease

Gamma-glutamyltranspeptidase (GGT) was purified to electrophoretic homogeneity from the cell extract of H. pylori. The purified enzyme consisted of heavy and light subunits with molecular weights of 38 kDa and 21 kDa, respectively. N-terminal amino acid sequence of heavy and light subunits revealed that H. pylori GGT was processed into 3 parts for a signal peptide of 27 amino acid residues, a heavy subunit of 352 residues, and a light subunit of 188 residues during translation. The reaction rate for hydrolysis of gamma-GpNA was 84.4 micromol/min per milligram of protein, and that for the gamma-glutamyl transfer from gamma-GpNA to gly-gly was 23.8 micromol/min per milligram of protein. The apparent Km values of H. pylori GGT for gamma-glutamyl compounds were on the order of 10-3 to 10-4 M and those for acceptor peptides and amino acids were on the order of 10-1 to 10-2 M. The GGT protein kept approximately 80% of the initial enzymatic activity on incubation at 60degrees C for 15 min. The optimum temperature and pH for reactions of both hydrolysis and transpeptidation were 40degrees C and 9.0, respectively. The transpeptidation and hydrolysis reactions catalyzed by H. pylori GGT were strongly inhibited by L-Gln and moderately inhibited by L-Ala, L-Ser, beta-chloro-L-Ala, and L-Glu. These results demonstrated that the biochemical properties of H. pylori GGT are different from those of other bacterial GGTs. Further, H. pylori GGT might degrade glutathione in the gastric mucous layer of humans if the enzyme could be secreted in the bacterial niches.
Amino Acid Sequence ; Amino Acids ; Glutathione ; Helicobacter ; Helicobacter pylori ; Humans ; Hydrogen-Ion Concentration ; Hydrolysis ; Light ; Molecular Weight ; Peptides ; Protein Sorting Signals

OBJECTIVES: This study was designed to investigate the distribution of Helicobacter pylori(HP), the relationship between HP colonization and gastritis scores graded according to the Sydney system, epithelial damage, and lymphoid follicles, and to assess the effect of eradication of HP infection on the different histological parameters. METHODS: Gastritis scores, epithelial damage, and lymphoid follicles were assessed in gastric antral, body, and fundic biopsy specimens before and 4 weeks after antiHP triple therapy in 32 patients with HP-related gastritis. RESULTS: The mean initial scores of all histological parameters were higher in the antrum compared with the body and fundus. A significant, positive correlation was noted between HP score and the score for inflammation, for activity, and for mucus depletion. After eradication of HP infection, significant improvement in activity, chronic inflammation, and mucus depletion was detected in responders with a successful HP eradication ; the activity return to normal in follow-up, and chronic inflammation and mucus depletion was decreased significally in severity in responders(p<0.05). No significant reduction in severity of gastritis and mucus depletion was detected in the non-responders with persistent HP infection following anti-HP triple therapy. CONCLUSIONS: The eradication of HP results in a rapid, significant histopathological improvement in the gastritis scores and epithelial damage in gastric mucosa.
Biopsy ; Colon ; Follow-Up Studies ; Gastric Mucosa ; Gastritis* ; Helicobacter ; Helicobacter pylori ; Humans ; Inflammation ; Mucus

Capsule endoscopy is being increasingly used for investigating GI bleeding of an obscure origin and also the bleeding that's due to Crohn's disease. Capsule endoscopy is a safe procedure with few complications. Complications of capsule endoscopy are capsule retention, incomplete small bowel examination, swallowing disorders and technical complications. However, capsule retention still remains a major concern. Crohn's disease may rarely show its first manifestation as GI bleeding. We present here a case of obscure GI bleeding in which the diagnosis of isolated Crohn's enteritis was made by using wireless CE. The retained capsule at the jejunal stricture of Crohn's disease was successfully retrieved by performing double balloon enteroscopy.
Capsule Endoscopy ; Constriction, Pathologic ; Crohn Disease* ; Deglutition Disorders ; Diagnosis ; Double-Balloon Enteroscopy* ; Gastrointestinal Hemorrhage ; Hemorrhage ; Methods

Helicobacter pylori, a causative agent of gastroduodenal diseases, is a Gram-negative microaerophilic bacterium. Although H. pylori locates in the microaerophilic mucous layer, the bacteria would come into contact harmful reactive oxygen species generated by host immune system. It has been reported that H. pylori harbors various defense mechanisms which can protect bacterial cells from oxygen exposure. The change of the gene expression profile of sodB-negative isogenic mutant of H. pylori 26695 was analyzed by high resolution 2-DE followed by matrix assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS) and tandem MS and microarray analysis. Eighteen genes and 41 genes were upregulated and downregulated respectively, either transcriptionally or translationally. Expression levels of three genes including trxB, yxjE and ribE that were changed both on a mRNA level and on a protein level were confirmed by RT-PCR analysis. However, change of expression levels of other major antioxidants such as KatA, AhpC and NapA were not detected, which means Sod is regulated by different way from that of KatA and AhpC. Mutant study of other antioxidant proteins may give us better understanding for the regulation of stress response in H. pylori.
Antioxidants ; Bacteria ; Defense Mechanisms ; Gene Expression* ; Helicobacter pylori ; Helicobacter* ; Immune System ; Mass Spectrometry ; Microarray Analysis ; Oxygen ; Reactive Oxygen Species ; Ribes ; RNA, Messenger ; Superoxide Dismutase* ; Superoxides* ; Transcriptome

Helicobacter pylori are a capnophilic bacterium, which colonize gastric mucosa and are resistant to acidic and oxidative damage. Thiol-active proteins subserve redox functions in tolerating oxidative stress and environmental toxicants, such as hydrogen peroxide and hypochlorous acid. We analyzed disulfide-containing proteins of H. pylori strain 26695. Active disulfide-containing proteins were separated by thiol-affinity chromatography, displayed with two-dimensional electrophoresis (2-DE), and identified by MALDI-TOF-MS. Thirty-five putative disulfide proteins, including AhpC (HP1563), GroEL (HP0011), and FrdB (HP0191), were identified in this study. In addition, 4 disulfide proteins of HypB, FusA, TufB, and AhpC showed enhanced intensities in the periplasmic space when compared with the pellet, suggesting that these proteins might play roles in the first redox system against environmental oxidative stresses. Disulfide-containing proteins identified in this study will provide the standard landscape for constructing the proteome components responsible for redox regulation of H. pylori.
Chromatography ; Colon ; Electrophoresis ; Gastric Mucosa ; Helicobacter ; Helicobacter pylori ; Hydrogen Peroxide ; Hypochlorous Acid ; Oxidation-Reduction ; Oxidative Stress ; Periplasm ; Proteins ; Proteome ; Sprains and Strains

Low molecular proteins (LMPs) which are smaller than 20 kDa are difficult to visible on a standard two-dimensional SDS-polyacrylamide gel electrophoresis (2-D SDS-PAGE) map. LMPs must be enriched appropriately to be analyzed. We isolated LMPs of Helicobacter pylori 26695 from 1-D polyacrylamide gel and digested by pepsin. Pepsin-digested LMPs were separated by HPLC and each fraction was analyzed by hybrid tandem mass spectrometer. Seventy nine peptides, representing 27 genes, including copper ion binding protein (CopP, 7 kDa), thioredoxin (TrxA, 11.9 kDa) and ribosomal protein L23 (Rpl23, 10.5 kDa) were identified. Some proteins larger than 40 kDa including Omp2, Omp21, Omp27, Omp30, Omp32, catalase and HP1083 were also identified. This work may give researchers a useful way to analyse the expressed LMPs which could not be identified on the conventional 2-D SDS-PAGE.
Acrylic Resins ; Carrier Proteins ; Catalase ; Chimera ; Chromatography, High Pressure Liquid ; Chromatography, Liquid ; Copper ; Electrophoresis ; Electrophoresis, Polyacrylamide Gel ; Helicobacter pylori ; Molecular Weight ; Pepsin A ; Peptides ; Proteins ; Proteome ; Ribosomal Proteins ; Thioredoxins