Expression and Function of Murine WFDC2 in the Respiratory Tract
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Combined Human Epididymis 4 and Carbohydrate Antigen 125 Serum Protein Levels Diagnostic Value in Ovarian Cancer
ISSN: 2640-5180 Madridge Journal of Cancer Study & Research Research Article Open Access Combined Human Epididymis 4 and Carbohydrate Antigen 125 Serum Protein Levels Diagnostic value in Ovarian Cancer Salwa Hassan Teama1*, Reham El Shimy2 and Hebatallah Gamal3 1Department of Molecular Biology, Medical Ain Shams Research Institute (MASRI), Faculty of Medicine, Ain Shams University, Cairo, Egypt 2Department of Clinical and Chemical Pathology, National Cancer Institute, Faculty of Medicine, Cairo University, Cairo, Egypt 3Departement of Surgical Oncology, National Cancer Institute, Faculty of Medicine, Cairo University, Cairo, Egypt Article Info Abstract *Corresponding author: Objective: Human Epididymis 4 (HE-4) protein, a new candidate for ovarian cancer Salwa Hassan Teama detection shows promising diagnostic value for ovarian cancer diagnosis, this study aimed Department of Molecular Biology Medical Ain Shams Research Institute to assess the diagnostic significance of combined Human Epididymis 4 and Carbohydrate (MASRI) Antigen 125 (CA-125) serum protein levels in ovarian cancer detection. Faculty of Medicine Ain Shams University Subjects and Methods: A clinical case control study include; forty nine subjects; patients Abbasia, Cairo with ovarian cancer (n=33), non-cancer control group (n=16). Serum protein levels of Egypt HE-4 were measured using an enzyme linked immune sorbent assay (ELISA). All data were Tel: 0020-1005293116 E-mail: [email protected] analyzed by SPSS software (version 21.0.0; IPM SPSS, Chicago, IL, USA). Results: The results showed that increased serum protein concentration of HE-4 (pMol/L) and Received: July 25, 2018 CA-125 (U/ml) in the ovarian cancer group mean (SD)/median (range) 329.61±336.55/199 Accepted: August 13, 2018 Published: August 17, 2018 (28.72-1064) and 521.36±572.60/287 (10.50-2377), than non-cancer control group 64.80±38.51/54.53 (21 -160) and 28.35±10.80/28 (10-50) respectively (p<0.05). -
WFDC2 Control Peptide
AP10066CP-N OriGene Technologies Inc. OriGene EU Acris Antibodies GmbH 9620 Medical Center Drive, Ste 200 Schillerstr. 5 Rockville, MD 20850 32052 Herford UNITED STATES GERMANY Phone: +1-888-267-4436 Phone: +49-5221-34606-0 Fax: +1-301-340-8606 Fax: +49-5221-34606-11 [email protected] [email protected] WFDC2 control peptide Alternate names: ESPE4, Epidydimal Secretory Protein E4, HE4, Major Epididymis-Specific protein E4, WAP four-disulfide core domain protein 2, WAP5, WFDC2 Catalog No.: AP10066CP-N Quantity: 0.25 mg Concentration: 2.5 mg/ml Background: The whey acidic protein (WAP) domain is a conserved motif, containing eight cysteines found in a characteristic 4-disulphide core arrangement, that is present in a number of otherwise unrelated proteins. One of these proteins, which contains two WAP domains, is HE4 (also known as WFDC2), originally described as an epididymis specific protein but more recently suggested to be a putative serum tumour marker for ovarian cancer and a presumptive role in natural immunity. The HE4 protein expression is not only confined to epidydimis but is expressed in a number of normal human tissues out side the reproductive system, including regions of the respiratory tract and nasopharynx and in a subset of lung tumor cell lines. HE4 gene expression was highest in normal human trachea and salivary gland, and to a lesser extent, lung, prostate, pituitary gland, thyroid, and kidney. Highest level of expression of ESPE4 was observed in adenocarcinomas of the lung, and occasional breast, transitional cell and pancreatic carcinomas (1). The WFDC2 gene under goes extensive splicing in malignant tissues that give rise to five WAP domain containing iso forms (2). -
Human Epididymis Protein 4 (HE4)
Human Epididymis Protein 4 (HE4) Monitoring Patients With Epithelial Ovarian Carcinoma Introduction cancer patients.5 This group found that measurement Human epididymis protein 4 (HE4), or WAP four- of HE4 showed sensitivity and specificity comparable disulphide core domain protein 2 (WFDC2), was first to that of CA125 for differentiating postmenopausal identified in the epithelium of the distal epididymis women with ovarian cancer from normal controls.5 They and was originally predicted to be a protease inhibitor suggested that the HE4 assay may have an advantage involved in sperm maturation.1,2 HE4 is the gene over CA125 in that it is less frequently positive in product of the WFDC2 gene that is located on patients with nonmalignant disease.5 chromosome 20q12-13.1.3 The WFDC2 gene is one of 14 homologous genes on this chromosome that encode Expression of HE4 in EOC proteins with WAP-type four-disulphide core (WFDC2) Drapkin and colleagues used immunohistochemical domains.3 techniques to show that cortical inclusion cysts (CIC) lined by metaplastic Mullerian epithelium abundantly HE4 belongs to the family of whey acidic four-disulfide expresses HE4 relative to normal surface epithelium.3 core (WFDC2) proteins with suspected trypsin inhibitor Using tissue microarrays, they showed that HE4 properties3,4; however, no biological function has so far expression was restricted to certain histologic subtypes been identified for HE4.5,6 The HE4 gene codes for a of epithelial ovarian carcinomas (EOC).3 13-kD protein, although in its mature glycosylated -
Identification of Ovarian Cancer Gene Expression Patterns Associated
ORIG I NAL AR TI CLE JOURNALSECTION IdentifiCATION OF Ovarian Cancer Gene Expression PATTERNS Associated WITH Disease Progression AND Mortality Md. Ali Hossain1,2 | Sheikh Muhammad Saiful Islam3 | Julian Quinn4 | Fazlul Huq5 | Mohammad Ali Moni4,5 1Dept OF CSE, ManarAT International UnivERSITY, Dhaka-1212, Bangladesh Ovarian CANCER (OC) IS A COMMON CAUSE OF DEATH FROM can- 2Dept OF CSE, Jahangirnagar UnivERSITY, CER AMONG WOMEN worldwide, SO THERE IS A PRESSING NEED SaVAR, Dhaka, Bangladesh TO IDENTIFY FACTORS INflUENCING MORTALITY. Much OC PATIENT 3Dept. OF Pharmacy, ManarAT International UnivERSITY, Dhaka-1212, Bangladesh CLINICAL DATA IS NOW PUBLICALLY ACCESSIBLE (including PATIENT 4Bone BIOLOGY divisions, Garvan Institute OF age, CANCER SITE STAGE AND SUBTYPE), AS ARE LARGE DATASETS OF Medical Research, SyDNEY, NSW 2010, OC GENE TRANSCRIPTION PROfiles. These HAVE ENABLED STUDIES AustrALIA CORRELATING OC PATIENT SURVIVAL WITH CLINICAL VARIABLES AND 5The UnivERSITY OF SyDNEY, SyDNEY Medical School, School OF Medical Science, WITH GENE EXPRESSION BUT IT IS NOT WELL UNDERSTOOD HOW THESE Discipline OF Biomedical Sciences, NSW TWO ASPECTS INTERACT TO INflUENCE MORTALITY. TO STUDY THIS 1825, AustrALIA WE INTEGRATED CLINICAL AND TISSUE TRANSCRIPTOME DATA FROM Correspondence THE SAME PATIENTS AVAILABLE FROM THE Broad Institute Cancer Dept OF CSE, Jahangirnagar UnivERSITY, Dhaka, Bangladesh Genome Atlas (TCGA) portal. WE INVESTIGATED OC mRNA The UnivERSITY OF SyDNEY, SyDNEY Medical EXPRESSION LEVELS (relativE TO NORMAL PATIENT TISSUE) OF 26 School, School OF Medical Science, Discipline OF Biomedical Sciences, NSW GENES ALREADY STRONGLY IMPLICATED IN OC, ASSESSED HOW THEIR 1825, AustrALIA EXPRESSION IN OC TISSUE PREDICTS PATIENT SURVIVAL THEN em- Email: al i :hossai n@manarat :ac:bd , mohammad :moni @sydney :eduau PLOYED CoX Proportional Hazard REGRESSION MODELS TO anal- YSE BOTH CLINICAL FACTORS AND TRANSCRIPTOMIC INFORMATION TO FUNDING INFORMATION DETERMINE RELATIVE RISK OF DEATH ASSOCIATED WITH EACH FACTOR. -
Regulatory Function of Whey Acidic Protein in the Proliferation of Mouse Mammary Epithelial Cells in Vivo and in Vitro
View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Elsevier - Publisher Connector Developmental Biology 274 (2004) 31–44 www.elsevier.com/locate/ydbio Regulatory function of whey acidic protein in the proliferation of mouse mammary epithelial cells in vivo and in vitro Naoko Nukumi, Kayoko Ikeda, Megumi Osawa, Tokuko Iwamori, Kunihiko Naito, Hideaki Tojo* Laboratory of Applied Genetics, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo 113-8657, Japan Received for publication 14 October 2003, revised 30 March 2004, accepted 28 April 2004 Available online 10 August 2004 Abstract Although possible biological functions of whey acidic protein (WAP) have been suggested, few studies have focused on investigating the function of WAP. This paper describes evidence for WAP function in lobulo-alveolar development in mammary glands in vivo and in the cell cycle progression of mammary epithelial cells in vitro. Ubiquitous overexpression of WAP transgene impaired only lobulo-alveolar development in the mammary glands of transgenic female mice but not other physiological functions, indicating that the inhibitory function of WAP is specific to mammary alveolar cells. The forced expression of WAP significantly inhibited the proliferation of mouse mammary epithelial cells (HC11 cells and EpH4/K6 cells), whereas it did not affect that of NIH3T3 cells. Co-culturing of WAP-clonal cells and control cells using a transwell insert demonstrated that WAP inhibited the proliferation of HC11 cells through a paracrine action but not that of NIH3T3 cells, and that WAP was able to bind to HC11 cells but not to NIH3T3 cells. -
Characterisation of Eppin Function: Expression and Activity in the Lung
ORIGINAL ARTICLE LUNG BIOLOGY Characterisation of eppin function: expression and activity in the lung Aaron Scott1,7, Arlene Glasgow1,7, Donna Small1, Simon Carlile1, Maelíosa McCrudden2, Denise McLean2, Ryan Brown1, Declan Doherty1, Fionnuala T. Lundy2, Umar I. Hamid2, Cecilia M. O’Kane2, Daniel F. McAuley2, Malcolm Brodlie3, Michael Tunney4, J. Stuart Elborn2, Chris R. Irwin5, David J. Timson 6, Clifford C. Taggart1 and Sinéad Weldon1 Affiliations: 1Airway Innate Immunity Research Group, Centre for Experimental Medicine, Wellcome-Wolfson Institute for Experimental Medicine, Queen’s University Belfast, Belfast, UK. 2Centre for Experimental Medicine, Wellcome-Wolfson Institute for Experimental Medicine, Queen’s University Belfast, Belfast, UK. 3Paediatric Respiratory Unit, Great North Children’s Hospital and Institute of Cellular Medicine, Newcastle University, Newcastle upon Tyne, UK. 4Halo, School of Pharmacy, Queen’s University Belfast, Belfast, UK. 5Centre for Dentistry, Queen’s University Belfast, Belfast, UK. 6School of Pharmacy and Biomolecular Sciences, University of Brighton, Brighton, UK. 7Joint first authors. Correspondence: Cliff Taggart, Airway Innate Immunity Research Group, Centre for Infection and Immunity, Wellcome-Wolfson Institute for Experimental Medicine, Queen’s University Belfast, Belfast, BT9 7BL, UK. E-mail: [email protected] @ERSpublications Eppin is a low-molecular-weight protein which is expressed in the human lung during inflammation http://ow.ly/WZuQ30aELEI Cite this article as: Scott A, Glasgow A, Small D, et al. Characterisation of eppin function: expression and activity in the lung. Eur Respir J 2017; 50: 1601937 [https://doi.org/10.1183/13993003.01937-2016]. ABSTRACT Eppin is a serine protease inhibitor expressed in male reproductive tissues. The aim of this study was to investigate the localisation and regulation of eppin expression in myeloid and epithelial cell lines, and explore its potential role as a multifunctional host defence protein. -
The DNA Sequence and Comparative Analysis of Human Chromosome 20
articles The DNA sequence and comparative analysis of human chromosome 20 P. Deloukas, L. H. Matthews, J. Ashurst, J. Burton, J. G. R. Gilbert, M. Jones, G. Stavrides, J. P. Almeida, A. K. Babbage, C. L. Bagguley, J. Bailey, K. F. Barlow, K. N. Bates, L. M. Beard, D. M. Beare, O. P. Beasley, C. P. Bird, S. E. Blakey, A. M. Bridgeman, A. J. Brown, D. Buck, W. Burrill, A. P. Butler, C. Carder, N. P. Carter, J. C. Chapman, M. Clamp, G. Clark, L. N. Clark, S. Y. Clark, C. M. Clee, S. Clegg, V. E. Cobley, R. E. Collier, R. Connor, N. R. Corby, A. Coulson, G. J. Coville, R. Deadman, P. Dhami, M. Dunn, A. G. Ellington, J. A. Frankland, A. Fraser, L. French, P. Garner, D. V. Grafham, C. Grif®ths, M. N. D. Grif®ths, R. Gwilliam, R. E. Hall, S. Hammond, J. L. Harley, P. D. Heath, S. Ho, J. L. Holden, P. J. Howden, E. Huckle, A. R. Hunt, S. E. Hunt, K. Jekosch, C. M. Johnson, D. Johnson, M. P. Kay, A. M. Kimberley, A. King, A. Knights, G. K. Laird, S. Lawlor, M. H. Lehvaslaiho, M. Leversha, C. Lloyd, D. M. Lloyd, J. D. Lovell, V. L. Marsh, S. L. Martin, L. J. McConnachie, K. McLay, A. A. McMurray, S. Milne, D. Mistry, M. J. F. Moore, J. C. Mullikin, T. Nickerson, K. Oliver, A. Parker, R. Patel, T. A. V. Pearce, A. I. Peck, B. J. C. T. Phillimore, S. R. Prathalingam, R. W. Plumb, H. Ramsay, C. M. -
ID AKI Vs Control Fold Change P Value Symbol Entrez Gene Name *In
ID AKI vs control P value Symbol Entrez Gene Name *In case of multiple probesets per gene, one with the highest fold change was selected. Fold Change 208083_s_at 7.88 0.000932 ITGB6 integrin, beta 6 202376_at 6.12 0.000518 SERPINA3 serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 3 1553575_at 5.62 0.0033 MT-ND6 NADH dehydrogenase, subunit 6 (complex I) 212768_s_at 5.50 0.000896 OLFM4 olfactomedin 4 206157_at 5.26 0.00177 PTX3 pentraxin 3, long 212531_at 4.26 0.00405 LCN2 lipocalin 2 215646_s_at 4.13 0.00408 VCAN versican 202018_s_at 4.12 0.0318 LTF lactotransferrin 203021_at 4.05 0.0129 SLPI secretory leukocyte peptidase inhibitor 222486_s_at 4.03 0.000329 ADAMTS1 ADAM metallopeptidase with thrombospondin type 1 motif, 1 1552439_s_at 3.82 0.000714 MEGF11 multiple EGF-like-domains 11 210602_s_at 3.74 0.000408 CDH6 cadherin 6, type 2, K-cadherin (fetal kidney) 229947_at 3.62 0.00843 PI15 peptidase inhibitor 15 204006_s_at 3.39 0.00241 FCGR3A Fc fragment of IgG, low affinity IIIa, receptor (CD16a) 202238_s_at 3.29 0.00492 NNMT nicotinamide N-methyltransferase 202917_s_at 3.20 0.00369 S100A8 S100 calcium binding protein A8 215223_s_at 3.17 0.000516 SOD2 superoxide dismutase 2, mitochondrial 204627_s_at 3.04 0.00619 ITGB3 integrin, beta 3 (platelet glycoprotein IIIa, antigen CD61) 223217_s_at 2.99 0.00397 NFKBIZ nuclear factor of kappa light polypeptide gene enhancer in B-cells inhibitor, zeta 231067_s_at 2.97 0.00681 AKAP12 A kinase (PRKA) anchor protein 12 224917_at 2.94 0.00256 VMP1/ mir-21likely ortholog -
Comprehensive Analysis of HE4 Expression in Normal and Malignant Human Tissues
Modern Pathology (2006) 19, 847–853 & 2006 USCAP, Inc All rights reserved 0893-3952/06 $30.00 www.modernpathology.org Comprehensive analysis of HE4 expression in normal and malignant human tissues Mary T Galgano1, Garret M Hampton2 and Henry F Frierson Jr1 1Department of Pathology, Robert E. Fechner Laboratory of Surgical Pathology, University of Virginia Medical Center, Charlottesville, VA, USA and 2Genomics Institute of the Novartis Research Foundation, San Diego, CA, USA The HE4 (WFDC2) gene encodes a WAP-type four disulphide core domain-containing protein with a presumptive role in natural immunity. Multiple studies have consistently identified upregulation of HE4 gene expression in carcinomas of the ovary; however, the expression in normal and malignant adult tissues has not been examined in detail. Here, we examined the expression of the HE4 gene and protein in a large series of normal and malignant adult tissues by oligonucleotide microarray and tissue microarray, respectively. HE4 gene expression was highest in normal human trachea and salivary gland, and to a lesser extent, lung, prostate, pituitary gland, thyroid, and kidney. In a series of 175 human adult tumors, gene expression was highest in ovarian serous carcinomas. However, adenocarcinomas of the lung, and occasional breast, transitional cell and pancreatic carcinomas had moderate or high levels of HE4 expression. Using tissue microarrays and full tissue sections of normal and 448 neoplastic tissues, HE4 immunoreactivity was found in normal glandular epithelium of the female genital tract and breast, the epididymis and vas deferens, respiratory epithelium, distal renal tubules, colonic mucosa, and salivary glands, consistent with HE4 gene expression. -
An Investigation Into the Function of WFDC2
An investigation into the function of WFDC2 Hannah Armes A thesis submitted in partial fulfilment of the requirements for the degree of Doctor of Philosophy School of Clinical Dentistry The University of Sheffield January 2019 (This page is left blank intentionally) i Acknowledgments First and foremost, I would like to thank my supervisor Dr Lynne Bingle for her endless advice, encouragement and kind words. I have learnt so much from her extensive knowledge and experience. Under Lynne’s supervision I have become a confident and independent researcher and for that I cannot thank her enough. I would also like to thank Professor Colin Bingle for his support throughout both my PhD and my undergraduate degree. His guidance and encouragement made me realise that a career in science was something achievable for me. I would like to give a huge thank you to the technical staff who helped me to make so much progress in my three years at the School of Clinical Dentistry: the wonderful Brenka McCabe and Jason Heath for teaching me molecular biology and microbiology techniques and to Hayley Stanhope for teaching me histological techniques and processing my tissue samples. I would also like to thank Jessica-Leigh Tallis for being an excellent SURE scheme student and for generating some brilliant immunohistochemistry analysis. Thank you to the Bingle group for their support and kind words over the years (Apoorva, Priyanka, Renata, Debora, Chloe, Zulaiha and Esra). A huge thank you to my friends in the 3rd floor PGR office for making me laugh constantly for 3 years, even when faced with lab work disappointments: Amy Harding, Sven Niklander, Marianne Satur and Alex Bolger. -
Proteins at the Plasma Membrane: What Protein Domains Are on the Outside and What Domains Are on the Inside?
Proteins at the plasma membrane: What protein domains are on the outside and what domains are on the inside? Kanthida Kusonmano Kwanjeera Wanichthanarak Natapol Pornputtapong Chalmers University of Technology, Sweden The cover image is adopted from http://4e.plantphys.net/image.php?id=80. 1 Introduction Membrane proteins are involved in a wide range of important biological processes, such as cell signaling, transport of membrane-impermeable molecules, cell adhesion and cell–cell communication, many of which are involved in disease mechanism and drug target discovery. Thus, an understanding of their structure and function is of great importance for biological and pharmacological research. Because of the experimental difficulties, i.e. not easy to crystallize, these membrane proteins are rarely found in structural databases. Sequence-based analysis is therefore an important approach for investigating such proteins [1]. Transmembrane proteins are a class of integral proteins which penetrate into or through the lipid bilayer of cell membrane or plasma membrane. There are three regions that can be defined: the region outside the membrane, the region inside the membrane and the region in the bilayer (Figure 1). Figure 1 Representation of a transmembrane (integral membrane) protein (figure adopted from [2]) Prediction of transmembrane helices from sequence is a key challenge for bioinformatics. In this study we used TMHMM, a hidden Markov model for predicting transmembrane helices in protein sequences [3], to predict the location and in/out orientation of human transmembrane helices. Then, we investigated further for the protein domains of in/out transmembrane regions using HMMER, a tool for searching protein homologs and for making sequence alignments [4]. -
Oncogenic HPV Promotes the Expression of the Long Noncoding RNA Lnc-FANCI-2 Through E7 and YY1
Oncogenic HPV promotes the expression of the long noncoding RNA lnc-FANCI-2 through E7 and YY1 Haibin Liua,1, Junfen Xua,b,1, Yanqin Yangc, Xiaohong Wanga, Ethan Wua, Vladimir Majerciaka, Tingting Zhanga,d, Renske D. M. Steenbergene, Hsu-Kun Wangf,2, Nilam S. Banerjeef, Yang Lib, Weiguo Lub, Craig Meyersg, Jun Zhuc, Xing Xieb, Louise T. Chowf,3, and Zhi-Ming Zhenga,3 aTumor Virus RNA Biology Section, HIV Dynamics and Replication Program, National Cancer Institute, National Institutes of Health, Frederick, MD 21702; bDepartment of Gynecologic Oncology, Women’s Hospital, Zhejiang University School of Medicine, Hangzhou, Zhejiang 310006, China; cGenome Technology Laboratory, Systems Biology Center, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892; dStomatological Hospital of Tianjin Medical University, Tianjin 300070, China; eAmsterdam Universitair Medische Centra, Pathology, Cancer Center Amsterdam, Vrije Universiteit Amsterdam, 1081 HV Amsterdam, The Netherlands; fDepartment of Biochemistry and Molecular Genetics, University of Alabama at Birmingham, Birmingham, AL 35294; and gDepartment of Microbiology and Immunology, Penn State University College of Medicine, Hershey, PA 17033 Contributed by Louise T. Chow, November 23, 2020 (sent for review July 7, 2020; reviewed by Lawrence Banks and Haifan Lin) Long noncoding RNAs (lncRNAs) play diverse roles in biological one class of noncoding RNAs in the size range of 19 to 23 nts (7), processes, but their expression profiles and functions in cervical in HPV-infected cells and cervical tissues and reported that a carcinogenesis remain unknown. By RNA-sequencing (RNA-seq) anal- subset of miRNAs are regulated by HR-HPV infections (8–13) yses of 18 clinical specimens and selective validation by RT-qPCR anal- and may serve as biomarkers for HR-HPV infections and cervical yses of 72 clinical samples, we provide evidence that, relative to cancer progression (12, 13).