Pub Date : 2016-01-08DOI: 10.1080/15321819.2015.1135162
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
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.
{"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}
Pub Date : 2016-01-08DOI: 10.1080/15321819.2015.1135163
A. Attallah, M. El-Far, M. Omran, K. Farid, Ahmed A Attallah, Dalal Abd-Elaziz, M. Elbendary, I. El‐Dosoky, H. Ismail
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.
{"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}
Pub Date : 2016-01-02DOI: 10.1080/15321819.2015.1116009
C. Tanase, R. Albulescu, M. Neagu
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.
{"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}
Pub Date : 2008-06-02DOI: 10.1080/15321810802122103
L. Hirnle, I. Kątnik-Prastowska
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.
{"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}
Pub Date : 2006-12-01DOI: 10.1080/15321810600862389
J. Kutter
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
在微分析系统的分离方法是一个精心设计的，有组织的，并写的书，处理及时的主题。在过去的几十年里，科学家们开始讨论分析仪器和芯片实验室的小型化。本书关注微流体的某些方面-流体在密闭空间中的行为和对这些流体的操纵-即，进行化学分析，生化分析和类似过程的可能性。这类研究的产品通常被称为微型全分析系统(m-TAS)，或者更一般地称为芯片上的实验室(LOC)设备。由于它面向广泛的读者，它也是由许多学科的贡献者编写的，这些学科构成了LOC社区的骨干。当然，本书不可能试图涵盖LOC的整个领域。相反，它关注的是过去15年来LOC发展背后的主要驱动力之一:小型化分离系统。分离单元仍然是许多微型tas和LOC设备的核心，现代分离技术是分析化学家不可或缺的工具。本书概述了微制造设备的分离技术:理论背景信息，设计和理解，制造和材料问题，实现，以及与LOC应用(样品制备，检测等)的其他部分相关的分离系统。它的目的是作为一个一站式购物指南的问题，有关分离技术的微量分析设备。然而，它不仅仅是一个快速的参考指南，而是一个逗留和浏览的地方。这些信息很可能是在书中的几个地方提供的。一个多作者的卷给读者不同的风格，不同的方法，和不同的意见。许多主题是如此普遍，以至于它们在不同的章节中反复出现，展示了处理给定问题的不同角度，反映了研究人员对相同问题的不同背景。这个优秀的卷使所有那些感兴趣的微流体一个很好的参考，可以是一个研究生课程的文本。版权# Taylor & Francis Group, LLC ISSN 1532-1819 print/1532-4230 online DOI: 10.1080/15321810600862389
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Pub Date : 2006-09-01DOI: 10.1080/15321810600735007
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
在书的第一章中，作者伦巴德博士介绍了蛋白质组学和蛋白质组学。为了读者的利益，我们在这里引用我们同意的引言的第一部分。“蛋白质组学是一个日益复杂的研究领域，有望对治疗学、诊断学和新兴的治疗学学科(强调患者特异性治疗)的发展产生重要的结果。然而，蛋白质组学究竟是什么?蛋白质组这个术语可以追溯到1995年，当时汉弗莱-史密斯和他的同事将蛋白质组定义为“基因组的总蛋白质含量”。基因组被定义为“细胞或生物体的完整的单一遗传物质;配子中的全套基因。”因此，蛋白质组学就是对蛋白质组的研究。对于蛋白质组学，人们提出了许多其他的定义。莫里森和同事将蛋白质组定义为“细胞在某一时间点表达的全部蛋白质”。在这种情况下，蛋白质组学就是研究蛋白质组;然而，这一定义将排除细胞外的蛋白质集合，如在血浆、尿液和淋巴液中发现的蛋白质。后者的研究使用了蛋白质组学的一些工具，如二维电泳和质谱，但与使用同位素编码亲和标签(ICAT)技术研究差异蛋白表达并用于识别诊断和治疗的生物标志物的研究明显不同。无论精确的定义是什么，蛋白质组学涉及研究蛋白质的复杂混合物及其相互作用。这个更广泛的定义可能是有用的，因为它将蛋白质组学的应用扩展到诊断领域。蛋白质组学的基础技术很可能会充分提高分析能力，从而在个性化医疗中发挥重要作用。”根据作者的观点，“目前这本书的总体意图是解决其他人没有详细讨论和避免的问题，《免疫分析与免疫化学杂志》，27:289-290,2006版权# Taylor & Francis Group, LLC ISSN 1532-1819 print/1532-4230 online DOI: 10.1080/15321810600735007
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Pub Date : 2005-10-01DOI: 10.1080/15321810500220993
Peter L. McDermott
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
工业蛋白质组学，生物技术和制药的应用，正如编辑所说，是蛋白质组学的工业应用的重点治疗。蛋白质组学在工业上的应用通常集中在靶点发现和制药管道中，因此要求蛋白质组学过程是稳健的，具有良好的特征，在质量控制(QC)下，并产生统计上显著的结果。它还需要处理大量样品的能力。例如，一项简单的临床蛋白质组学研究可能需要对至少36到数百个复杂样本进行表达蛋白质组学分析。”本书包含11章，每一章都涉及蛋白质组学工业应用的具体方面。第一章涵盖了基于质谱(MS)的蛋白质组学的基础知识。功能蛋白质组学将在第2章和第3章中介绍。第2章讨论了基于质谱的蛋白质相互作用制图方法。第3章讨论了蛋白质的翻译后修饰，特别是蛋白质磷酸化。结构蛋白质组学将在第4章和第5章中介绍。第4章涵盖了高通量晶体学和基于结构的药物设计的硅方法的使用。第5章描述了氢/氘交换质谱法在高通量蛋白质结构研究中的应用。蛋白质组学的第一个应用是靶标发现。第六章讨论了蛋白质组学技术在蛋白质靶点鉴定和验证中的应用。蛋白质组学的最新应用是发现疾病或药物相关的生物标志物。第7章概述了生物标志物的发现和验证，而第8章详细介绍了使用蛋白质组学发现血浆生物标志物。蛋白质组学也可以从小分子工作(即药物)着手，特别是寻找与药物相互作用的蛋白质。第9章介绍了化学基因组学/化学蛋白质组学，并讨论了不同的方法。免疫分析与免疫化学杂志，26:357-364,2005版权所有# Taylor & Francis, Inc。ISSN 1532-1819 print/1532-4230 online DOI: 10.1080/15321810500220993
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