1.4 Cases of Duodenal Diverticular Bleeding Treated by Endoscopic Therapy.
Se Lim CHOI ; Hae Dong PARK ; Man Jo KIM ; Jung Seop EUM ; Young Seok LEE ; Dong Ju SONG ; Soo Hyun KIM ; Sung Min KIM ; Seong Ho CHOI ; Hee Seung PARK
Korean Journal of Gastrointestinal Endoscopy 2002;25(3):147-152
Duodenal diverticulum appears in 6% of upper gastrointestinal examinations and up to 23% of endoscopic retrograde cholangiopancreaticographies and up to 22% at autopsy. Most of these patients are asymptomatic, but a small fraction develop complications including choledocholithiasis, cholangitis, pancreatitis, diverticulitis, perforation, fistular formation and bleeding. Among these complications, only a few documented cases of bleeding have been reported in the literature, and the experience of endoscopist to the sequence of diagnosis, endoscopic treatment, and subsequent relief of the symptoms remains limited. Aggressive but careful endoscopic examination can help diagnosis of the cases. Also, endoscopic treatment of duodenal diverticular bleeding is very effective and proved to be an effective alternative to surgery. We report 4 patients with duodenal diverticular bleeding in whom both diagnosis and definitive treatment were successful by endoscopy alone.
Autopsy
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Cholangitis
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Choledocholithiasis
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Diagnosis
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Diverticulitis
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Diverticulum
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Endoscopy
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Hemorrhage*
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Humans
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Pancreatitis
2.Inhibition of LPS-induced cyclooxygenase 2 and nitric oxide production by transduced PEP-1-PTEN fusion protein in Raw 264.7 macrophage cells.
Sun Hwa LEE ; Yeom Pyo LEE ; So Young KIM ; Min Seop JEONG ; Min Jung LEE ; Hye Won KANG ; Hoon Jae JEONG ; Dae Won KIM ; Eun Joung SOHN ; Sang Ho JANG ; Yeon Hyang KIM ; Hyung Joo KWON ; Sung Woo CHO ; Jinseu PARK ; Won Sik EUM ; Soo Young CHOI
Experimental & Molecular Medicine 2008;40(6):629-638
Phosphatase and tensin homologue deleted on chromosome 10 (PTEN) is a tumor suppressor. Although it is well known to have various physiological roles in cancer, its inhibitory effect on inflammation remains poorly understood. In the present study, a human PTEN gene was fused with PEP-1 peptide in a bacterial expression vector to produce a genetic in-frame PEP-1-PTEN fusion protein. The expressed and purified PEP-1-PTEN fusion protein were transduced efficiently into macrophage Raw 264.7 cells in a time- and dose- dependent manner when added exogenously in culture media. Once inside the cells, the transduced PEP-1-PTEN protein was stable for 24 h. Transduced PEP-1-PTEN fusion protein inhibited the LPS-induced cyclooxygenase 2 (COX-2) and iNOS expression levels in a dose-dependent manner. Furthermore, transduced PEP-1-PTEN fusion protein inhibited the activation of NF-kappa B induced by LPS. These results suggest that the PEP-1-PTEN fusion protein can be used in protein therapy for inflammatory disorders.
Animals
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Cell Line
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Cyclooxygenase 2/*metabolism
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Cysteamine/*analogs & derivatives
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Enzyme Activation
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Humans
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Lipopolysaccharides/*pharmacology
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Macrophages/*metabolism
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Mice
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NF-kappa B/metabolism
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Nitric Oxide/*biosynthesis
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Nitric Oxide Synthase Type II/metabolism
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PTEN Phosphohydrolase/*genetics
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Peptides/*genetics
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Recombinant Fusion Proteins/*biosynthesis/genetics
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Signal Transduction