• Title/Summary/Keyword: PEP-1

Search Result 183, Processing Time 0.024 seconds

Double-guidewire technique for selective biliary cannulation does not increase the rate of post-endoscopic retrograde cholangiopancreatography pancreatitis in patients with naïve papilla

  • Han Taek Jeong;June Hwa Bae;Ho Gak Kim;Jimin Han
    • Clinical Endoscopy
    • /
    • v.57 no.2
    • /
    • pp.226-236
    • /
    • 2024
  • Background/Aims: This study aimed to compare the safety of the double-guidewire technique (DGT) with that of the conventional single-guidewire technique (SGT) in real-world situations. Methods: A total of 240 patients with naïve papilla who underwent endoscopic retrograde cholangiopancreatography (ERCP) at Daegu Catholic University Medical Center between January 2021 and December 2021 were included. The primary outcome was the rate of post-ERCP pancreatitis (PEP) in the SGT and DGT groups. Results: A total of 163 patients (67.9%) belonged to the SGT group, and 77 (32.1%) belonged to the DGT group. The rates of successful biliary cannulation were 95.7% and 83.1% in the SGT and DGT groups, respectively (p=0.002). In the study group, PEP occurred in 14 patients (5.8%). The PEP rates were not significantly different between the SGT and DGT groups (4.3% vs. 9.1%, p=0.150). In the multivariate analysis, the age of <50 years (odds ratio [OR], 9.305; 95% confidence interval [CI], 1.367-63.358; p=0.023) and hyperlipidemia (OR, 7.384; 95% CI, 1.103-49.424; p=0.039) were significant risk factors for PEP in the DGT group. Conclusions: DGT did not increase the PEP rate in patients with naïve papilla. In addition, the age of <50 years and hyperlipidemia were significant risk factors for PEP in the DGT group.

Transduced PEP-1-Grb7 Fusion Protein Suppressed LPS-induced COX-2 Expression

  • An, Jae-Jin;Kim, So-Young;Lee, Sun-Hwa;Kim, Dae-Won;Ryu, Hea-Jin;Yeo, Seung-Il;Jang, Sang-Ho;Kwon, Hyung-Joo;Kim, Tae-Yoon;Lee, Sang-Chul;Poo, Ha-Ryoung;Cho, Sung-Woo;Lee, Kil-Soo;Park, Jin-Seu;Eum, Won-Sik;Choi, Soo-Young
    • BMB Reports
    • /
    • v.40 no.2
    • /
    • pp.189-195
    • /
    • 2007
  • Although the incidence and severity of atopic dermatitis (AD) is steadily increasing at an alarming rate, its pathogenic mechanisms remain poorly understood yet. Recently, we found that the expression of Grb7 protein was markedly decreased in AD patients using proteomic analysis. In the present study, human Grb7 gene was fused with PEP-1 peptide in a bacterial expression vector to produce a genetic in-frame PEP-1-Grb7 fusion protein. The expressed and purified PEP-1-Grb7 fusion proteins transduced efficiently into skin cells in a time- and dose-dependent manner when added exogenously in culture media. Once inside the cells, the transduced PEP-1-Grb7 protein was stable for 48 h. In addition, transduced PEP-1-Grb7 fusion protein markedly increased cell viability in macrophage RAW 264.7 cells treated with LPS by inhibition of the COX-2 expression level. These results suggest that the PEP-1-Grb7 fusion protein can be used in protein therapy for inflammatory skin disorders, including AD.

Effects of PEP-1-FK506BP on cyst formation in polycystic kidney disease

  • Jo, Hyo Sang;Eum, Won Sik;Park, Eun Young;Ko, Je Young;Kim, Do Yeon;Kim, Dae Won;Shin, Min Jea;Son, Ora;Cho, Su Bin;Park, Jung Hwan;Lee, Chi Hern;Yeo, Eun Ji;Yeo, Hyeon Ji;Choi, Yeon Joo;Youn, Jong Kyu;Cho, Sung-Woo;Park, Jinseu;Park, Jong Hoon;Choi, Soo Young
    • BMB Reports
    • /
    • v.50 no.9
    • /
    • pp.460-465
    • /
    • 2017
  • Polycystic kidney disease (PKD) is one of the most common inherited disorders, involving progressive cyst formation in the kidney that leads to renal failure. FK506 binding protein 12 (FK506BP) is an immunophilin protein that performs multiple functions, including regulation of cell signaling pathways and survival. In this study, we determined the roles of PEP-1-FK506BP on cell proliferation and cyst formation in PKD cells. Purified PEP-1-FK506BP transduced into PKD cells markedly inhibited cell proliferation. Also, PEP-1-FK506BP drastically inhibited the expression levels of p-Akt, p-p70S6K, p-mTOR, and p-ERK in PKD cells. In a 3D-culture system, PEP-1-FK506BP significantly reduced cyst formation. Furthermore, the combined effects of rapamycin and PEP-1-FK506BP on cyst formation were markedly higher than the effects of individual treatments. These results suggest that PEP-1-FK506BP delayed cyst formation and could be a new therapeutic strategy for renal cyst formation in PKD.

Human brain pyridoxal-5'-phosphate phosphatase (PLPP): protein transduction of PEP-1-PLPP into PC12 cells

  • Lee, Yeom-Pyo;Kim, Dae-Won;Lee, Min-Jung;Jeong, Min-Seop;Kim, So-Young;Lee, Sun-Hwa;Jang, Sang-Ho;Park, Jin-Seu;Kang, Tae-Cheon;Won, Moo-Ho;Cho, Sung-Woo;Kwon, Oh-Shin;Eum, Won-Sik;Choi, Soo-Young
    • BMB Reports
    • /
    • v.41 no.5
    • /
    • pp.408-413
    • /
    • 2008
  • Pyridoxal-5'-phosphate phosphatase (PLPP) catalyzes the dephosphorylation of pyridoxal-5'-phosphate (PLP). A human brain PLPP gene was fused with a PEP-1 peptide and produced a genetic in-frame PEP-1-PLPP fusion protein. The purified PEP-1-PLPP fusion protein was efficiently transduced into PC12 cells in a time- and dose-dependent manner when added exogenously to culture media. Once inside the cells, the transduced PEP-1-PLPP fusion protein was stable for 36 h. The concentration of PLP was markedly decreased by the addition of exogenous PEP-1-PLPP to media pretreated with the vitamin $B_6$ precursors; pyridoxine, pyridoxal kinase and pyridoxine-5'-phosphate oxidase into cells. The results suggest that the transduction of the PEP-1-PLPP fusion protein can be one mode of PLP level regulation, and to replenish this enzyme in the various neurological disorders related to vitamin $B_6$.

Genomic Analysis of Satellite RNA of Cucumber mosaic virus-Paf Related with Mild Symptoms (Cucumber mosaic virus Paf 계통의 약독 병징과 관련된 satellite RNA의 유전자 해석)

  • Sung, Mi-Young;Jung, Min-Young;Lee, Sang-Yong;Ryu, Ki-Hyun;Choi, Jang-Kyung
    • Research in Plant Disease
    • /
    • v.10 no.4
    • /
    • pp.241-247
    • /
    • 2004
  • Recently, we reported a satellite RNA (Paf-satRNA) which is encapsidated in a pepper isolate of Cucumber mosaic virus (CMV-Paf) regulated symptom attenuation of the helper virus. To characterize mild symptom domain of Paf-satRNA, a series of chimeric cDNAs of satRNAs were created by using full-length cDNA clones of Paf-satRNA and a Pep-satRNA, chlorosis-inducing satRNA in pepper plants, and analyzed for determinants of symptom attenuation. When compared the nucleotide sequences, the 3' and 5' terminal sequences of the two wild-type (wt) satRNAs contained relatively conserved sequences which are the typical to CMV satRNA. Ten bases insertions were found in PepY-satRNA, and two variable regions, 81st to 113th and 183rd to 265th from the 5'-end, were located in the middle parts of the satRNAs. To delineate the attenuated symptom-related domain for the Paf-satRNA, in vitro transcripts RNAs transcribed from the wt cDNAs and constructed chimeric cDNAs were combined with genomic RNAs, RNA1, RNA2 and RNA3, of CMV-Fny and inoculated onto Nicotiana benthamiana plants. These transcripts were fully infectious onto the N. benthamiana and infectivity was confirmed by the RT-PCR. Chimeric Paf(H/N)-satRNA and PepY(N/A)-satRNA as well as Paf-satRNA induced very mild mosaic or symptomless infection on N. benthamiana. By contrast, typical mosaic symptom and stunting of infected plants were induced when PepY-satRNA, PepY(H/N)-satRNA and Paf(N/A)-satRNA were infected to N. benthamiana. Paf-satRNA coinfected with CMV-Fny RNAs induced very mild to sympomless on pepper plants whereas PepY-satRNA-infected pepper expressed typical chlorosis mosaic symptom. Two kinds of chimeric mutants, Paf(H/N)-satRNA and PepY(N/A)-satRNA, induced mild mosaic or symptomless infection onto pepper plants, while PepY(H/N)-satRNA and Paf(N/A)-satRNA showed typical chlorosis and mosaic symptom with stunting. This results suggest that mild symptom-related domain for the Paf-satRNA was located on HpaI-NarI region.

Inhibitory Activity of Plant Extracts against Prolyl Endopeptidase (식물자원의 Prolyl Endopeptidase 저해활성 탐색)

  • Kim, Geum-Soog;Lee, Seung-Eun;Lee, Hee-Ju;Kim, Yi-Min;Jeon, So-Young;Park, Chun-Geon;Seong, Nak-Sul;Song, Kyung-Sik
    • Korean Journal of Medicinal Crop Science
    • /
    • v.12 no.1
    • /
    • pp.1-9
    • /
    • 2004
  • Prolyl endopeptidase (PEP) is proline-specific serine protease, cleaving peptide bonds on the biologically active neuropeptides such as substance P, vassopressin, and thyrotropin-releasing hormone and is, therefore, suggested to play important roles in learning and memory process. In this work, the inhibitory effect of plant extracts on PEP was investigated. Out of 200 plant extracts, Prunus mume, Pyrola. japonica, Hypericum ascyron, Astilbe chinensis var. typica, and Elaeagnus umbellata inhibited more than 90% of PEP activity at the concentration of 5 ppm.

PEP-1-HO-1 prevents MPTP-induced degeneration of dopaminergic neurons in a Parkinson's disease mouse model

  • Youn, Jong Kyu;Kim, Dae Won;Kim, Seung Tae;Park, Sung Yeon;Yeo, Eun Ji;Choi, Yeon Joo;Lee, Hae-Ran;Kim, Duk-Soo;Cho, Sung-Woo;Han, Kyu Hyung;Park, Jinseu;Eum, Won Sik;Hwang, Hyun Sook;Choi, Soo Young
    • BMB Reports
    • /
    • v.47 no.10
    • /
    • pp.569-574
    • /
    • 2014
  • Heme oxygenase-1 (HO-1) degrades heme to carbon dioxide, biliverdin, and $Fe^{2+}$, which play important roles in various biochemical processes. In this study, we examined the protective function of HO-1 against oxidative stress in SH-SY5Y cells and in a Parkinson's disease mouse model. Western blot and fluorescence microscopy analysis demonstrated that PEP-1-HO-1, fused with a PEP-1 peptide can cross the cellular membranes of human neuroblastoma SH-SY5Y cells. In addition, the transduced PEP-1-HO-1 inhibited generation of reactive oxygen species (ROS) and cell death caused by 1-methyl-4-phenylpyridinium ion ($MPP^+$). In contrast, HO-1, which has no ability to transduce into SH-SY5Y cells, failed to reduce $MPP^+$-induced cellular toxicity and ROS production. Furthermore, intraperitoneal injected PEP-1-HO-1 crossed the blood-brain barrier in mouse brains. In a PD mouse model, PEP-1-HO-1 significantly protected against 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP)-induced toxicity and dopaminergic neuronal death. Therefore, PEP-1-HO-1 could be a useful agent in treating oxidative stress induced ailments including PD.

Solution Structure of LXXLL-related Cofactor Peptide of Orphan Nuclear Receptor FTZ-F1

  • Yun, Ji-Hye;Lee, Chul-Jin;Jung, Jin-Won;Lee, Weon-Tae
    • Bulletin of the Korean Chemical Society
    • /
    • v.33 no.2
    • /
    • pp.583-588
    • /
    • 2012
  • Functional interaction between Drosophila orphan receptor FTZ-F1 (NR5A3) and a segmentation gene product fushi tarazu (FTZ) is crucial for regulating genes related to define the identities of alternate segmental regions in the Drosophila embryo. FTZ binding to the ligand-binding domain (LBD) of FTZ-F1 is of essence in activating its transcription process. We determined solution structures of the cofactor peptide ($FTZ^{PEP}$) derived from FTZ by NMR spectroscopy. The cofactor peptide showed a nascent helical conformation in aqueous solution, however, the helicity was increased in the presence of TFE. Furthermore, $FTZ^{PEP}$ formed ${\alpha}$-helical conformation upon FTZ-F1 binding, which provides a receptor bound structure of $FTZ^{PEP}$. The solution structure of $FTZ^{PEP}$ in the presence of FTZ-F1 displays a long stretch of the ${\alpha}$-helix with a bend in the middle of helix.

The Purification and Characterization of Bacillus subtilis Tripeptidase (PepT)

  • Park, Yong-Seek;Cha, Myung-Hoon;Yong, Whan-Mi;Kim, Hyo-Joon;Chung, Il-Yup;Lee, Young-Seek
    • BMB Reports
    • /
    • v.32 no.3
    • /
    • pp.239-246
    • /
    • 1999
  • A tripeptidase (PepT) was purified to homogeneity from Bacillus subtilis through four sequential chromatographies including DEAE-Sepharose ion exchange, hydroxylapatite, mono-Q FPLC ion exchange, and Superose-12 FPLC gel filtration. The apparent molecular mass of the enzyme was 49,200 Da and 51,400 Da as determined by sodium dodecylsulfatepolyacrylamide gel electrophoresis (SDS-PAGE) and gel filtration chromatography, respectively, and the enzyme exists in a monomeric form. The physicochemical properties of the enzyme were as follows: optimum pH at 7.5, optimum temperature at $60^{\circ}C$, and pI at 4.9. The $K_m$ and $V_{max}$ values of the enzyme were 4.3 mM and 2.5 mmol/min/mg, respectively, with MetAla-Ser as substrate. The B. subtilis PepT requires $Co^{2+}$ ion(s) for activation, while it is inactivated by EOTA and 1,10-phenanthroline, suggesting that it is a metalloprotein. The enzyme was not inhibited by any of serine protease, aspartic protease, or leucine aminopeptidase inhibitors. The enzyme showed comparable activities towards four different substrates including Met-Ala-Ser, Leu-Gly-Gly, Leu-Ser-Phe, and Leu-Leu-Tyr. The amino terminal sequence of PepT determined by Edman degradation was found to be MKEEIIERFTTYVXV and turned out to be identical to that of PepT deduced from a cloned B. subtilis pepT.

  • PDF

Inhibitory Effect on Infection of Plant Viruses by Filtrate Powder from Culture Broth of Acinetobacter sp. and Its Mode of Action (Acinetobacter sp. 배양여과액 분말제제의 식물바이러스에 대한 감염억제 효과 및 작용)

  • Kim Mi-Soon;Jung Min-Young;Kim Yun-Sung;Jang Cheol;Hwang In-Cheon;Ryu Ki-Hyun;Choi Jang-Kyung
    • Research in Plant Disease
    • /
    • v.12 no.2
    • /
    • pp.91-98
    • /
    • 2006
  • A filtrate powder, designated as KNF2022, produced from culture broth of Acinetobacter sp. KTB3 was tested for their inhibitory effects on Pepper mild mottle virus (PMMoV) infection to Nicotiana glutinosa or N. tabacum cv. Xanthi nc. When 1/100 dilution with distilled water was treated to the plants and PMMoV was inoculated, the inhibition was estimated to be 94.3 and 95.6%, respectively. The same concentrations of KNF2022 inhibited infections of Pepper mottle virus (PepMoV) and Cucumber mosaic virus (CMV) on Chenopodium amaranticolor by 97.1 and 92.5%, respectively. Duration of inhibitory activity of the filtrate powder from Acinetobacter sp. culture broth against PMMoV infection on N. glutinosa was maintained for 2 days at 80% inhibition level, however, the inhibitory effect was diminished from 4 days after treatment to 50% levels. To evaluate inhibitory effects on systemic host plants of the antiviral agent, symptom developments of PMMoV, PepMoV and CMV on KNF2022-treated pepper plants were investigated. Delayed symptom developments until 10 days after inoculation (DAI) were observed for all the three viruses when the viruses were inoculated individually, and these delayed symptom development effects were maintained until 30 DAI in case of PepMoV. Moreover, PepMoV was not detected by RT-PCR and ELISA until 30 DAI. These delayed symptom development effects were diminished in all combinations of three virus co-inoculations due to synergism of three viruses on symptom developments. Inhibitory effect of KNF2022 was verified under electron microscopic examinations using purified virus preparations. Particles of PMMoV and PepMoV were observed on specimens from 5 min after KNF2022 treatment, and the particle sizes were reached in the range of 200-250 nm and 400-600 nm, respectively. Furthermore, the viral particles were destructed and particle sizes were reached in the range of 100-150 nm and 300-500 nm, respectively, on 60 min after treatments. Reduction of local lesion numbers on N. tabacum cv. Xanthi nc and C. amaranticolor were accompanied with reduction of virus particle sizes. In the case of CMV destructed particle numbers were also increased according to incubation period after KNF2022 treatment and local lesions on C. amaranticolor were reduced.