Journal of Immunoassay and Immunochemistry最新文献

{"title":"1-[4-Fluoro-2-(2-nitrovinyl)phenyl]pyrrolidine Suppresses Toll-Like Receptor 4 Dimerization Induced by Lipopolysaccharide","authors":"Sang-Ii Ahn, Ji-Soo Kim, Chae-Yeon Hong, Gyo-Jeong Gu, Hyeon-Myeong Shin, H. Jeong, Kwang Oh Koh, J. Mang, Dae Young Kim, H. Youn","doi":"10.1080/15321819.2015.1135162","DOIUrl":"https://doi.org/10.1080/15321819.2015.1135162","url":null,"abstract":"Toll-like receptor 4 (TLR4) recognizes LPS and triggers the activation of the myeloid differential factor 88 (MyD88)- and toll-interleukin-1 receptor domain-containing adapter, inducing interferon-β (TRIF)-dependent major downstream signaling pathways. Previously, we presented biochemical evidence that 1-[4-Fluoro-2-(2-nitrovinyl)phenyl]pyrrolidine (FPP), which was synthesized in our laboratory, inhibits NF-κB activation induced by LPS. Here, we investigated whether FPP modulates the TLR4 downstream signaling pathways and what anti-inflammatory target in TLR4 signaling is regulated by FPP. FPP inhibited LPS-induced NF-κB activation by targeting TLR4 dimerization. These results suggest that FPP can modulate the TLR4 signaling pathway at the receptor level to decrease inflammatory gene expression.","PeriodicalId":15987,"journal":{"name":"Journal of Immunoassay and Immunochemistry","volume":"22 1","pages":"307 - 315"},"PeriodicalIF":0.0,"publicationDate":"2016-01-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"88417579","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Levels of Schistosoma mansoni Circulating Antigen in Chronic Hepatitis C Patients with Different Stages of Liver Fibrosis","authors":"A. Attallah, M. El-Far, M. Omran, K. Farid, Ahmed A Attallah, Dalal Abd-Elaziz, M. Elbendary, I. El‐Dosoky, H. Ismail","doi":"10.1080/15321819.2015.1135163","DOIUrl":"https://doi.org/10.1080/15321819.2015.1135163","url":null,"abstract":"The goal of this study was to determine the levels of S. mansoni antigen in different liver fibrosis stages with chronic hepatitis C (CHC) Egyptian patients. A total of 174 CHC patients showing HCV-NS4 antigen and HCV- RNA in their sera were included. S. mansoni antigen was detected in serum using Western blot and ELISA. The levels of interferon-γ (IFN- γ) were determined using ELISA. The 50 kDa S. mansoni antigen discriminated patients infected with S. mansoni from healthy individuals with 0.93 area under curve (AUC), 92% sensitivity, and 97% specificity. The level of S. mansoni antigen (μg/ml) was significantly (P < 0.0001) increased with the progression of liver fibrosis stages (26.9 ± 17.5 in F1, 42.1 ± 25.2 in F2, 49.8 ± 30.3 in F3 and 62.2 ± 26.3 μg/mL in F4 liver cirrhosis), 26.9 ± 17.59 in significant fibrosis (F2–F4); 51.2 ± 27.9 in advanced fibrosis (F3–F4). A significant correlation (r = 0.506; P < 0.0001) was shown between the levels of the S. mansoni antigen and the HCV-NS4 antigen. In conclusion, the presence of S. mansoni antigen in different liver fibrosis stages of CHC patients confirming that concomitant schistosome infection aggravates liver disease.","PeriodicalId":15987,"journal":{"name":"Journal of Immunoassay and Immunochemistry","volume":"7 1","pages":"316 - 330"},"PeriodicalIF":0.0,"publicationDate":"2016-01-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"87750731","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Proteomic Approaches for Biomarker Panels in Cancer","authors":"C. Tanase, R. Albulescu, M. Neagu","doi":"10.1080/15321819.2015.1116009","DOIUrl":"https://doi.org/10.1080/15321819.2015.1116009","url":null,"abstract":"Proteomic technologies remain the main backbone of biomarkers discovery in cancer. The continuous development of proteomic technologies also enlarges the bioinformatics domain, thus founding the main pillars of cancer therapy. The main source for diagnostic/prognostic/therapy monitoring biomarker panels are molecules that have a dual role, being both indicators of disease development and therapy targets. Proteomic technologies, such as mass-spectrometry approaches and protein array technologies, represent the main technologies that can depict these biomarkers. Herein, we will illustrate some of the most recent strategies for biomarker discovery in cancer, including the development of immune-markers and the use of cancer stem cells as target therapy. The challenges of proteomic biomarker discovery need new forms of cross-disciplinary conglomerates that will result in increased and tailored access to treatments for patients; diagnostic companies would benefit from the enhanced co-development of companion diagnostics and pharmaceutical companies. In the technology optimization in biomarkers, immune assays are the leaders of discovery machinery.","PeriodicalId":15987,"journal":{"name":"Journal of Immunoassay and Immunochemistry","volume":"68 1","pages":"1 - 15"},"PeriodicalIF":0.0,"publicationDate":"2016-01-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"88201695","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Ed Board EOV","authors":"","doi":"10.1080/15321819.2014.895643","DOIUrl":"https://doi.org/10.1080/15321819.2014.895643","url":null,"abstract":"","PeriodicalId":15987,"journal":{"name":"Journal of Immunoassay and Immunochemistry","volume":"40 1","pages":"ebi - ebi"},"PeriodicalIF":0.0,"publicationDate":"2014-10-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"81538093","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Editorial Board EOV","authors":"","doi":"10.1080/15321819.2013.802887","DOIUrl":"https://doi.org/10.1080/15321819.2013.802887","url":null,"abstract":"","PeriodicalId":15987,"journal":{"name":"Journal of Immunoassay and Immunochemistry","volume":"24 1","pages":"ebi - ebi"},"PeriodicalIF":0.0,"publicationDate":"2013-10-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"75493467","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Editorial Board EOV","authors":"","doi":"10.1080/15321819.2012.721977","DOIUrl":"https://doi.org/10.1080/15321819.2012.721977","url":null,"abstract":"","PeriodicalId":15987,"journal":{"name":"Journal of Immunoassay and Immunochemistry","volume":"40 1","pages":"ebi - ebi"},"PeriodicalIF":0.0,"publicationDate":"2012-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"76224100","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"EDA Fibronectin Isoform of Amniotic Fluid in Relation to Normal Pregnancy Stages and to Pregnancies Complicated by Fetal Postmaturity Syndrome","authors":"L. Hirnle, I. Kątnik-Prastowska","doi":"10.1080/15321810802122103","DOIUrl":"https://doi.org/10.1080/15321810802122103","url":null,"abstract":"Abstract The relative expression of the EDA region in fibronectin (FN) was determined by ELISA, using specific monoclonal antibody anti-EDA-FN, in the amniotic fluid samples derived from: 2nd trimester, early 3rd trimester, term, and post-term pregnancy, delivery at 37–40 weeks and at 41–42 weeks, as well as pregnancies complicated by fetal postmaturity. The expression of EDA-FN isoform was almost on the same level from the 2nd trimester to the 3rd trimester including term and post-term pregnancy. However, its relative amount significantly decreased in delivery groups and was significantly higher in the pregnancies with fetal postmaturity syndrome.","PeriodicalId":15987,"journal":{"name":"Journal of Immunoassay and Immunochemistry","volume":"155 1","pages":"299 - 306"},"PeriodicalIF":0.0,"publicationDate":"2008-06-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"79801789","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The Book Corner","authors":"J. Kutter","doi":"10.1080/15321810600862389","DOIUrl":"https://doi.org/10.1080/15321810600862389","url":null,"abstract":"Separation Methods in Microanalytical Systems is a well designed, organized, and written book which deals with a timely topic. In the last couple of decades scientists started talking about miniaturization of analytical instrumentation and lab-on-a-chip. This book concerns itself with certain aspects of microfluidics – the behavior of fluids in confined spaces and the manipulation of these fluids – namely, the possibility to perform chemical analyses, biochemical assays, and similar processes. The products of this kind of research are often dubbed micro-Total Analysis Systems (m-TAS) or, more generally, lab-on-a-chip (LOC) devices. As it is intended for a wide audience, it was also written by contributors from many of the disciplines that constitute the backbone of the LOC community. Of course, this book cannot attempt to cover the entire field of LOC. Instead it focuses on what has been one of the main driving forces behind the development of LOC for the last 15 years: miniaturized separation systems. Separation units are still at the heart of many micro-TAS and LOC devices, and modern separation techniques are indispensable tools for analytical chemists. This book gives an overview of separation techniques on micro-fabricated devices: theoretical background information, design and understanding, fabrication and material issues, implementations, and separation systems in relation to other parts of LOC applications (sample preparation, detection, etc.). It is intended as a one-stop shopping guide for questions concerning separation techniques in microanalytical devices. It is, however, not so much meant only as a quick reference guide, but rather as a place to linger and browse. It is very likely that the information is provided in several locations within the book. A multiauthor volume gives the reader different styles, different approaches, and different opinions. Many topics are so common that they reappear in different chapters, showing different angles to approach a given problem, reflecting the different backgrounds from which researchers attach the same issues. This excellent volume makes a good reference for all those interested in microfludics and can be a text for a graduate course. Journal of Immunoassay & Immunochemistry, 27: 379–386, 2006 Copyright # Taylor & Francis Group, LLC ISSN 1532-1819 print/1532-4230 online DOI: 10.1080/15321810600862389","PeriodicalId":15987,"journal":{"name":"Journal of Immunoassay and Immunochemistry","volume":"26 1","pages":"379 - 386"},"PeriodicalIF":0.0,"publicationDate":"2006-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"83440050","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The Book Corner","authors":"","doi":"10.1080/15321810600735007","DOIUrl":"https://doi.org/10.1080/15321810600735007","url":null,"abstract":"In the first chapter of the book, the author, Dr. Lundbad introduces and defines proteome and proteomics. For the benefit of the reader, we quote here the first part of the introduction with which we agree. “Proteomics is an increasingly complex area of study that is expected to yield results important for the development of therapeutics, diagnostics and for the emerging discipline of theranostics, which emphasizes patient-specific therapeutics. What, however, exactly is proteomics? The term proteome dates back to 1995 when Humphrey-Smith and colleagues defined the proteome as “the total protein content of a genome.” Genome is defined as “a complete single set of the genetic material of a cell or of an organism; the complete set of genes in a gamete.” It would follow that proteomics is the study of the proteome. A variety of other definitions have been proposed for proteomics. Morrison and coworkers define the proteome as “the entire complement of proteins expressed by a cell at a point in time.” In such cases, proteomics would be the study of the proteome; however, this definition would exclude extracellular collections of proteins such as those found in blood plasma, urine, and lymphatic fluid. These latter studies use some of the tools of proteomics, such as twodimensional electrophoresis and mass spectrometry, but are clearly different from studies where isotope-coded affinity tag (ICAT) technology is used to study differential protein expression and are used to identify biomarkers for diagnostics and therapeutics. Whatever the precise definition, proteomics involves the study of complex mixtures of proteins and their interactions. This somewhat broader definition might be useful in that it extends the application of proteomics to diagnostics. The technologies that underlie proteomics quite likely will improve sufficiently in analytical capability to be valuable in personalized medicine.” According to the author, “The overall intent of the current book is to address issues that are not discussed in detail by others and to avoid, where Journal of Immunoassay & Immunochemistry, 27: 289–290, 2006 Copyright # Taylor & Francis Group, LLC ISSN 1532-1819 print/1532-4230 online DOI: 10.1080/15321810600735007","PeriodicalId":15987,"journal":{"name":"Journal of Immunoassay and Immunochemistry","volume":"32 1","pages":"289 - 290"},"PeriodicalIF":0.0,"publicationDate":"2006-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"81609314","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The Book Corner","authors":"Peter L. McDermott","doi":"10.1080/15321810500220993","DOIUrl":"https://doi.org/10.1080/15321810500220993","url":null,"abstract":"Industrial Proteomics, Applications for Biotechnology and Pharmaceuticals is as the editor states “is a focused treatment of industrial applications of proteomics. Proteomics in industry is generally focused on application in target discovery and pharmaceutical pipelines, thereby requiring proteomic processes that are robust, well characterized, under quality control (QC) and producing statistically significant results. It also requires the capacity to handle significant amounts of samples. For example, a simple clinical proteomic study might require an analysis by expression proteomics from a minimum of 36 to hundreds of complex samples.” This book contains 11 chapters, each of which addresses specific aspects of industrial application of proteomics. The first chapter covers the basics of mass spectrometry (MS)-based proteomics. Functional proteomics is covered in Chapters 2 and 3. Chapter 2 discusses the MS-based approaches of mapping protein interactions. Chapter 3 discusses the protein posttranslational modifications, particularly, protein phosphorylations. Structural proteomics is covered in Chapters 4 and 5. Chapter 4 covers the use of high-throughput crystallography and in silico methods for structure-based drug design. Chapter 5 describes the use of hydrogen/deuterium exchange mass spectrometry for high-throughput protein structure studies. The first applications of proteomics were in target discovery. Chapter 6, a discussion of the utilization of proteomics technologies for the identification as well as the validation of protein targets is given. The latest application of proteomics has been for the discovery of disease or drug-related biomarkers. Chapter 7 provides an overview of biomarker discovery and validation while Chapter 8 details plasma biomarker discovery using proteomics. Proteomics can also be approached from the small-molecule worked (i.e., drugs), particularly, to find proteins that interact with drugs. Chapter 9 presents chemical genomics/chemical proteomics and discusses the different approaches. Journal of Immunoassay & Immunochemistry, 26: 357–364, 2005 Copyright # Taylor & Francis, Inc. ISSN 1532-1819 print/1532-4230 online DOI: 10.1080/15321810500220993","PeriodicalId":15987,"journal":{"name":"Journal of Immunoassay and Immunochemistry","volume":"100 1","pages":"357 - 364"},"PeriodicalIF":0.0,"publicationDate":"2005-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"81665825","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}