• Title/Summary/Keyword: OMPS

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Ovarian Malignancy Probability Score (OMPS) for Appropriate Referral of Adnexal Masses

  • Arab, Maliheh;Honarvar, Zahra;Hosseini-Zijoud, Seyed-Mostafa
    • Asian Pacific Journal of Cancer Prevention
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    • v.15 no.20
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    • pp.8647-8650
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    • 2014
  • Background: Ovarian cancer is the most common cancer cause of gynecologic cancer deaths. In order to increase the likelihood of patient survival through primary operation by gyneco-oncologists, an appropriate algorithm for referral is considered here. Materials and Methods: Suspicious adnexal mass cases including ovarian malignancy probability score-1 (OMPS1) scores between 2.3-3.65 are re-evaluated by OMPS2. Sensitivity and specificity of each score were determined. Results: Sensitivity and specificity with a 3.82 score of OMPS2 in the studied subgroup (OMPS1 scores between 2.3-3.65) were 64% and 76.9% respectively. Conclusions: Management of OMPS1 scores of below 2.3 with sensitivity of 100% and above 3.65 with specificity of 72.9% is clear. In the subgroup of cases with OMPS1 score between 2.3-3.65, OMPS2 is helpful for triage with a cutoff score of 3.82.

Comparison of Two Ovarian Malignancy Prediction Models Based on Age Sonographic Findings and Serum Ca125 Measurement

  • Arab, Maliheh;Yaseri, Mehdi;Ashrafganjoi, Tahereh;Maktabi, Maryam;Noghabaee, Giti;Sheibani, Kourosh
    • Asian Pacific Journal of Cancer Prevention
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    • v.13 no.8
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    • pp.4199-4202
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    • 2012
  • Objective: The aim of our study is to compare an ovarian malignancy prediction model based on age and four sonographic findings (OMPS1) with a new model called OMPS2 which differs just by adding serum CA125 measurement to (OMPS1). Methods: In a cross sectional comparative study OMPS1 was validated in 830 operated ovarian masses within a 3 years period (2006-2009). Logistic regression analysis was used to construct OMPS2 based on OMPS1 adding serum CA125 findings. The area under the curve for two models was compared in 411 patients. Results: OMPS2 was calculated as follows: OMPS1 + 1.444 (if serum CA125= 36-200) or 3.842 (if serum CA125 is more than 200). AUC of OMPS2 was increased to 84.3% (CI 95% 78.1- 89.8) in comparison to OMPS1 with AUC of 78.1% (CI 95% 71.8-84.5). Conclusion: Our second model is more accurate in prediction of ovarian malignancy, compared with our first model.

Protection of Rabbits from Experimental Pseudomonas Endophthalmitis by Human Anti-P. aeruginosa Outer Membrane Proteins IgG

  • Lee, Na-Gyong;Ahn, Bo-Young;Kwon, Oh-Woong
    • Journal of Microbiology and Biotechnology
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    • v.13 no.3
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    • pp.444-450
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    • 2003
  • In order to develop an effective means to treat P. aeruginosa infections, we have purified P. aeruginosa outer membrane proteins (OMPs)-specific human IgG antibody. In this study, we investigated the protective activity of the purified anti-OMPs IgC against P. aeruginosa infection in a rabbit endophthalmitis model. Rabbits were inoculated by an intravitreal injection with P. aeruginosa, and treated with a single dose of 1 mg anti-P. aeruginosa OMPs IgG. All the control rabbits predominantly developed edematous responses and opacity in the eyes, but the rabbits treated with the antibody showed only very limited degree of edema. Aliquots of the vitreous humor were extracted and analyzed for the number of viable bacteria and endotoxin level. The results showed that the anti-OMPs IgC significantly reduced the bacterial count compared with the control group, and that the endotoxin level of the vitreous from the IgG-treated rabbits was more than 70-fold lower 6 h after the administration than the control animals. These data suggested that the anti-P. aeruginosa OMPs IgG is effective in inhibiting the bacterial growth and thereby in reducing endotoxin levels in the vitreous, warranting further development of the anti-P. aeruginosa OMPs IgG as a therapeutic means for treating Pseudomonas endophthalmitis.

Proteomic Analysis and Protective Effects of Outer Membrane Proteins from Salmonella Gallinarum in Chickens (Salmonella Gallinarum 세포외막단백질의 프로테옴 분석 및 닭에서의 방어능 효과)

  • Sun, Jisun;Cho, Youngjae;Jang, Joo-Hyun;Kang, Zheng-Wu;Han, Jang-Hyuk;Hahn, Tae-Wook
    • Food Science of Animal Resources
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    • v.33 no.2
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    • pp.281-286
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    • 2013
  • Salmonella Gallinarum (SG) is known as an important pathogen that causes fowl typhoid in chickens. To investigate SG outer-membrane proteins (OMPs) as a vaccine candidate, we used proteomic mapping and database analysis techniques with extracted OMPs. Also, extracted OMPs were evaluated in several aspects to their safety, immune response in their host and protective effects. Our research has established a proteomic map and database of immunogenic SG-OMPs used as inactive vaccine against salmonellosis in chickens. A total of 22 spots were detected by 2-dimensional gel electrophoresis and immunogenic protein analysis. Eight spots were identified by Matrix-Assisted Laser Desorption/Ionization-Time of Flight-Mass spectrometry (MALDI-TOF-MS) and peptide mass fingerprinting (PMF) and categorized into four different types of proteins. Among these proteins, OmpA is considered to be an immunogenic protein and involved in the hosts' immune system. To estimate the minimum safety dose in chickens, 35 brown layers were immunized with various concentrations of OMPs, respectively. Consequently, all chickens immunized with more than a $50{\mu}g$ dose were protected against challenges. Moreover, intramuscular administration of OMPs to chickens was more effective compared to subcutaneous administration. These results suggest that the adjuvanted SG-OMP vaccine not only induces both the humoral and cellular immune response in the host but also highly protects the hosts' exposed to virulent SG with $50{\mu}g$ OMPs extracted by our method.

The Cross-validation of Satellite OMI and OMPS Total Ozone with Pandora Measurement (지상 Pandora와 위성 OMI와 OMPS 오존관측 자료의 상호검증 방법에 대한 분석 연구)

  • Baek, Kanghyun;Kim, Jae-Hwan;Kim, Jhoon
    • Korean Journal of Remote Sensing
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    • v.36 no.3
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    • pp.461-474
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    • 2020
  • Korea launched Geostationary Environmental Monitoring Satellite (GEMS), a UV/visible spectrometer that measure pollution gases on 18 February 2020. Because satellite retrieval is an ill-posed inverse solving process, the validation with ground-based measurements or other satellite measurements is essential to obtain reliable products. For this purpose, satellite-based OMI and OMPS total column ozone (TCO), and ground-based Pandora TCO in Busan and Seoul were selected for future GEMS validation. First of all, the goal of this study is to validate the ground ozone data using characteristics that satellite data provide coherent ozone measurements on a global basis, although satellite data have a larger error than the ground-based measurements. In the cross validation between Pandora and OMI TCO, we have found abnormal deviation in ozone time series from Pandora #29 observed in Seoul. This shows that it is possible to perform inverse validation of ground data using satellite data. Then OMPS TCO was compared with verified Pandora TCO. Both data shows a correlation coefficient of 0.97, an RMSE of less than 2 DU and the OMPS-Pandora relative mean difference of >4%. The result also shows the OMPS-Pandora relative mean difference with SZA, TCO, cross-track position and season have insignificant dependence on those variables.In addition, we showed that appropriate thresholds depending on the spatial resolution of each satellite sensor are required to eliminate the impact of the cloud on Pandora TCO.

경구투여 백신 후보물질로서의 Helicobacter pylori 외막 단백질의 조사

  • 박형배;최태부
    • Microbiology and Biotechnology Letters
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    • v.25 no.2
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    • pp.129-136
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    • 1997
  • Helicobacter pylori is a spiral-shaped, microaerophilic human gastric pathogen causing chronic-active gastritis in association with duodenal ulcer and gastric cancer. To investigate the possibility of H. pylori outer membrane proteins (OMPS) as the oral vaccine antigens, sarcosine-insoluble outer membrane fraction has been prepared from H. pylori NCTC 11637. The major OMPs having apparent molecular masses of 62 kDa, 54 kDa and 33 kDa were detected by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), which were identified as urease B subunit (UreB), heat shock protein (Hsp54 kDa) and urease A subunit (UreA), respectively. Minor protein bands of 57 kDa, 52 kDa, 40 kDa, 36 kDa and 31 kDa were also observed. The antigenicity of H. pylori OMPs and antigenic cross-reactivity among the strains were determined by immunoblot analysis using anti-H. pylori OMPs antisera or intestinal lavage solutions. The results showed that UreB, Hsp54 kDa, UreA and 40 kDa proteins vigorously stimulated mucosal immune response rather than systemic immunity. From this results, these proteins seemed to be useful as the antigen candidates for the oral vaccine. The immunoblotting results with surface proteins from eight isolated H. pylori strains were similar to that of H. pylori NCTC 11637. The IgA which had been arised from oral administration of H. pylori OMPs, was able to bind H. pylori whole-cells.

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Analysis of Vibrio parahaemolyticus OMPs and Production of Antibodies against OMPs

  • Kim, Soo-Min;Noh, Bong-Soo;Kim, Hae-Yeong;Park, Se-Jin;Ji, Geun-Eog
    • Food Science and Biotechnology
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    • v.14 no.3
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    • pp.410-412
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    • 2005
  • Vibrio parahaemolyticus is a gram-negative bacterium which acts as a causative agent for food poisoning. Studies with respect to specific extracellular proteins of V. parahaemolyticus would be useful for the development of specific detection methods against V. parahaemolyticus. In our present study, outer membrane proteins (OMPs) of V. parahaemolyticus were obtained from insoluble traction of 1% sarkosyl treated-cell wall materials. SDS-PAGE analysis showed the presence of several conserved outer membrane proteins among five strains of V. parahaemolyticus, and three bands were identified as V. parahaemolyticus OMPs through MALDI-TOF analysis. Polyclonal antibodies enriched with anti-OmpU were obtained from immunized rabbits. The antibodies against these proteins may be useful for the development of detection methods for V. parahaemolyticus.

Proteomic Analysis of Outer Membrane Proteins in Salmonella enterica Enteritidis

  • Cho, Youngjae;Park, Soyeon;Barate, Abhijit Kashinath;Truong, Quang Lam;Han, Jang Hyuck;Jung, Cheong-Hwan;Yoon, Jang Won;Cho, Seongbeom;Hahn, Tae-Wook
    • Journal of Microbiology and Biotechnology
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    • v.25 no.2
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    • pp.288-295
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    • 2015
  • Salmonella enterica serovar Enteritidis is the predominant agent causing salmonellosis in chickens and other domestic animals. In an attempt to identify antigenic S. Enteritidis outer membrane proteins (OMPs) that may be useful for subunit vaccine development, we established a proteomic map and database of antigenic S. Enteritidis OMPs. In total, 351 and 301 spots respectively from S. Enteritidis strain 270 and strain 350 were detected by two-dimensional gel electrophoresis. Fifty-one antigen-reactive spots were detected by antisera on two-dimensional immunoblots and identified as 12 specific proteins by matrix-assisted laser desorption ionization time-of-flight mass spectrometry. OmpA and DNA starvation/stationary phase protection protein (Dps) were the most abundant proteins among the identified OMPs, comprising 22 and 12 protein species, respectively. Interestingly, we found that the Dps of S. Enteritidis is also antigenic. OmpW was also verified to have high antigenicity. These results show that OmpA, Dps, and possibly OmpW are antigenic proteins. This study provides new insights into our understanding of the immunogenic characteristics of S. Enteritidis OMPs.

Analysis of Outer Membrane Proteins of Yersinia enterocolitica Isolated from Mountainspring Water and Pig

  • Shin, Sung-Jae;Park, Joo-Youn;Park, In-Soo;Shin, Na-Ri;Lee, Deog-Yong;Cho, Young-Wook;Park, Yong-Ha;Yoo, Han-Sang
    • Journal of Microbiology and Biotechnology
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    • v.12 no.4
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    • pp.674-678
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    • 2002
  • Yersinia enterocolitica causes various diseases in humans, including enteritis. The onset of such diseases is closely related with the expression of important virulence factors, particularly outer membrane proteins (OMPs). The expression of OMPs depends on several factors, including temperature, and origin, biotype and serotype of the bacteria. Recently, concerns over food safety have increased along with the demand for the development of sensitive, rapid, and pathogen-specific detection methods. To develop a suitable detection method for Y. enterocolitica isolated from Korean moutainspring water and pig feces, the OMP expression patterns were analyzed phenotypically and immunologically using 12 representative strains from 51 Y. enterocolitica Korean isolates. A 38-kDa OMP was commonly observed in all strains. However, additional OMPs were also observed in different biotypes and serotypes as well as bacterial origins, by incubating Y. enterocolitica at a low temperature. The specificity of the 38-kDa OMP was confirmed by a Western blot analysis with antisera against Y. enterocolitica and Brucella abortus. The results, therefore, indicate that the 38-kDa OMP could be used as a marker for detecting Y. enterocolitica in the environment or for seromonitoring.

Analysis of outer mombrane proteins of Brucella abortus using two dimensional polyacrylamide gel electrophoresis (2차원 전기영동법을 이용한 Brucella abortus 세포외막 특이단백질의 분석)

  • Kim, Byung-su;Kim, Sun-hee;Kim, Jong-suk;Baek, Byeong-kirl
    • Korean Journal of Veterinary Research
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    • v.38 no.2
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    • pp.328-335
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    • 1998
  • Outer membrane proteins(OMPs) of Brucella abortus 1119-3 strain were extracted by Triton X-100 treatment, and fractionated by DEAE-cellulose column chromatography and Sephacryl S-300 column chromatography. The antigenic proteins in these fractions were identified by Western blot analysis. In Western blot analysis, a single band(38kDa) was observed in the DEAE fractions from 36th fraction to 38th fraction against sera of cattle infected with B abortus. And other fractions have several bands. However, the Sephacryl S-300 fractions exhibited a total of 3 peaks of proteins with a broad range from about 30 to 116kDa. In order to characterize further, the extracted OMPs and the DEAE fractions were analyzed by two dimensional polyacrylamide gel electrophoresis(2-DE) and Western blot using serum from naturally infected cattle with Brucella spp. The 2-DE immunoblots of DEAE fraction showed immunoreactive spots more than twenty two. The major protein spots have ranging from about 32 to 47kDa. The pI values of the spots were detected from pH 4.7 to 5.4. Among the major protein spots, the 38kDa protein which is a specific antigen, located at the point of approximately a pI 4.8.

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