Adaptive Evolution and Divergence of SERPINB3: a Young Duplicate in Great Apes
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Polygenic Risk Score of SERPINA6/SERPINA1 Associates with Diurnal and Stress-Induced HPA Axis Activity in Children
Edinburgh Research Explorer Polygenic risk score of SERPINA6/SERPINA1 associates with diurnal and stress-induced HPA axis activity in children Citation for published version: Utge, S, Räikkönen, K, Kajantie, E, Lipsanen, J, Andersson, S, Strandberg, T, Reynolds, R, Eriksson, JG & Lahti, J 2018, 'Polygenic risk score of SERPINA6/SERPINA1 associates with diurnal and stress-induced HPA axis activity in children', Psychoneuroendocrinology. https://doi.org/10.1016/j.psyneuen.2018.04.009 Digital Object Identifier (DOI): 10.1016/j.psyneuen.2018.04.009 Link: Link to publication record in Edinburgh Research Explorer Document Version: Publisher's PDF, also known as Version of record Published In: Psychoneuroendocrinology General rights Copyright for the publications made accessible via the Edinburgh Research Explorer is retained by the author(s) and / or other copyright owners and it is a condition of accessing these publications that users recognise and abide by the legal requirements associated with these rights. Take down policy The University of Edinburgh has made every reasonable effort to ensure that Edinburgh Research Explorer content complies with UK legislation. If you believe that the public display of this file breaches copyright please contact [email protected] providing details, and we will remove access to the work immediately and investigate your claim. Download date: 29. Sep. 2021 Psychoneuroendocrinology 93 (2018) 1–7 Contents lists available at ScienceDirect Psychoneuroendocrinology journal homepage: www.elsevier.com/locate/psyneuen Polygenic risk score of SERPINA6/SERPINA1 associates with diurnal and T stress-induced HPA axis activity in children Siddheshwar Utgea,b, Katri Räikkönena, Eero Kajantiec,d,e, Jari Lipsanena, Sture Anderssond, ⁎ Timo Strandbergf,g, Rebecca M. -
Biomarkers of Neonatal Skin Barrier Adaptation Reveal Substantial Differences Compared to Adult Skin
www.nature.com/pr CLINICAL RESEARCH ARTICLE OPEN Biomarkers of neonatal skin barrier adaptation reveal substantial differences compared to adult skin Marty O. Visscher1,2, Andrew N. Carr3, Jason Winget3, Thomas Huggins3, Charles C. Bascom3, Robert Isfort3, Karen Lammers1 and Vivek Narendran1 BACKGROUND: The objective of this study was to measure skin characteristics in premature (PT), late preterm (LPT), and full-term (FT) neonates compared with adults at two times (T1, T2). METHODS: Skin samples of 61 neonates and 34 adults were analyzed for protein biomarkers, natural moisturizing factor (NMF), and biophysical parameters. Infant groups were: <34 weeks (PT), 34–<37 weeks (LPT), and ≥37 weeks (FT). RESULTS: Forty proteins were differentially expressed in FT infant skin, 38 in LPT infant skin, and 12 in PT infant skin compared with adult skin at T1. At T2, 40 proteins were differentially expressed in FT infants, 38 in LPT infants, and 54 in PT infants compared with adults. All proteins were increased at both times, except TMG3, S100A7, and PEBP1, and decreased in PTs at T1. The proteins are involved in filaggrin processing, protease inhibition/enzyme regulation, and antimicrobial function. Eight proteins were decreased in PT skin compared with FT skin at T1. LPT and FT proteins were generally comparable at both times. Total NMF was lower in infants than adults at T1, but higher in infants at T2. CONCLUSIONS: Neonates respond to the physiological transitions at birth by upregulating processes that drive the production of lower pH of the skin and water-binding NMF components, prevent protease activity leading to desquamation, and increase the 1234567890();,: barrier antimicrobial properties. -
Pediatric Primitive Neuroectodermal Tumors of the Central Nervous System Differentially Express Granzyme Inhibitors
RESEARCH ARTICLE Pediatric Primitive Neuroectodermal Tumors of the Central Nervous System Differentially Express Granzyme Inhibitors Jeroen F. Vermeulen1, Wim van Hecke1, Wim G. M. Spliet1, José Villacorta Hidalgo3, Paul Fisch3, Roel Broekhuizen1, Niels Bovenschen1,2* 1 Department of Pathology, University Medical Center Utrecht, 3584CX, Utrecht, The Netherlands, 2 Laboratory of Translational Immunology, University Medical Center Utrecht, 3584CX, Utrecht, The Netherlands, 3 Institute of Pathology, University Medical Center Freiburg, 79106, Freiburg, Germany * [email protected] Abstract Background OPEN ACCESS Central nervous system (CNS) primitive neuroectodermal tumors (PNETs) are malignant Citation: Vermeulen JF, van Hecke W, Spliet WGM, primary brain tumors that occur in young infants. Using current standard therapy, up to 80% Villacorta Hidalgo J, Fisch P, Broekhuizen R, et al. of the children still dies from recurrent disease. Cellular immunotherapy might be key to (2016) Pediatric Primitive Neuroectodermal Tumors improve overall survival. To achieve efficient killing of tumor cells, however, immunotherapy of the Central Nervous System Differentially Express Granzyme Inhibitors. PLoS ONE 11(3): e0151465. has to overcome cancer-associated strategies to evade the cytotoxic immune response. doi:10.1371/journal.pone.0151465 Whether CNS-PNETs can evade the immune response remains unknown. Editor: Javier S Castresana, University of Navarra, SPAIN Methods Received: September 3, 2015 We examined by immunohistochemistry the immune response and immune evasion strate- Accepted: February 29, 2016 gies in pediatric CNS-PNETs. Published: March 10, 2016 Copyright: © 2016 Vermeulen et al. This is an open Results access article distributed under the terms of the Creative Commons Attribution License, which permits Here, we show that CD4+, CD8+, γδ-T-cells, and Tregs can infiltrate pediatric CNS-PNETs, unrestricted use, distribution, and reproduction in any although the activation status of cytotoxic cells is variable. -
Low P66shc with High Serpinb3 Levels Favors Necroptosis and Better Survival in Hepatocellular Carcinoma
biology Article Low P66shc with High SerpinB3 Levels Favors Necroptosis and Better Survival in Hepatocellular Carcinoma Silvano Fasolato 1, Mariagrazia Ruvoletto 1 , Giorgia Nardo 2, Andrea Rasola 3, Marco Sciacovelli 3, Giacomo Zanus 4,5, Cristian Turato 6 , Santina Quarta 1 , Liliana Terrin 1, Gian Paolo Fadini 1 , Giulio Ceolotto 1, Maria Guido 1, Umberto Cillo 4,7, Stefano Indraccolo 2,4, Paolo Bernardi 3 and Patrizia Pontisso 1,* 1 Department of Medicine, University of Padua, Via Giustiniani, 2, 35128 Padua, Italy; [email protected] (S.F.); [email protected] (M.R.); [email protected] (S.Q.); [email protected] (L.T.); [email protected] (G.P.F.); [email protected] (G.C.); [email protected] (M.G.) 2 Istituto Oncologico Veneto IOV- IRCCS, 35128 Padua, Italy; [email protected] (G.N.); [email protected] (S.I.) 3 Department of Biomedical Sciences, University of Padua, 35131 Padua, Italy; [email protected] (A.R.); [email protected] (M.S.); [email protected] (P.B.) 4 Department of Surgical, Oncological and Gastroenterological Sciences-DISCOG, University of Padua, 35128 Padua, Italy; [email protected] (G.Z.); [email protected] (U.C.); [email protected] (S.I) 5 Hepatobiliary and Pancreatic Surgery Unit-Treviso Hospital, 31100 Treviso, Italy 6 Department of Molecular Medicine, University of Pavia, 27100 Pavia, Italy; [email protected] 7 Unit of Hepatobiliary Surgery and Liver Transplantation, Padua University Hospital, 35128 Padua, Italy * Correspondence: [email protected]; Tel.: +39-049-821-7872; Fax: +39-049-875-4179 Citation: Fasolato, S.; Ruvoletto, M.; Simple Summary: Cell proliferation and escape from apoptosis are important pathological features Nardo, G.; Rasola, A.; Sciacovelli, M.; of hepatocellular carcinoma, one of the tumors with the highest mortality rate worldwide. -
SERPINB3/4 Polyclonal Antibody
PRODUCT DATA SHEET Bioworld Technology,Inc. SERPINB3/4 polyclonal antibody Catalog: BS60990 Host: Rabbit Reactivity: Human,Mouse,Rat BackGround: Swiss-Prot: Metastasis of a primary tumor to a distant site is deter- P29508/P48594 mined through signaling cascades that break down inter- Purification&Purity: actions between the cell and extracellular matrix proteins. The antibody was affinity-purified from rabbit antiserum Among the proteins mediating metastasis are serine by affinity-chromatography using epitope-specific im- prote-ases, such as neutrophil elastase. In 1985, Dr. Jim munogen and the purity is > 95% (by SDS-PAGE). Travis and Dr. R.W. Carrell designated an emerging fam- Applications: ily of serine protease inhibitors as the serpin fam-ily, WB: 1:500~1:1000 which share homology in both primary amino acid se- Storage&Stability: quence and tertiary structure. Serpins contain a stretch of Store at 4°C short term. Aliquot and store at -20°C long peptide that mimics a true substrate for a corresponding term. Avoid freeze-thaw cycles. serine protease. Serine proteases bind to this substrate Specificity: mimic in a 1:1 stoichiometric fashion and become cata- SERPINB3/4 polyclonal antibody detects endogenous lytically inactive. Aberrant ex-pression of serpin family levels of SERPINB3/4 protein. members can contribute to a number of conditions, in- DATA: cluding emphysema (a-1 antitrypsin deficiency), fatal bleeding (elastase to thrombin specificity) and thrombosis (antithrombin deficiency), and are indicators of cancer stage phenotypes (circulating levels of squamous cell car- cinoma antigen, known as SCCA1, increase in advancing stages of some cervical, lung, esophageal and head and neck cancers). -
Tissue-Type Plasminogen Activator Is a Target of the Tumor Suppressor Gene Maspin
Proc. Natl. Acad. Sci. USA Vol. 95, pp. 499–504, January 1998 Biochemistry Tissue-type plasminogen activator is a target of the tumor suppressor gene maspin SHIJIE SHENG*†,BINH TRUONG*, DEREK FREDRICKSON*, RUILIAN WU*, ARTHUR B. PARDEE‡, AND RUTH SAGER* *Division of Cancer Genetics and ‡Division of Cell Growth and Regulation, Dana–Farber Cancer Institute, Harvard Medical School, 44 Binney Street, Boston, MA 02115 Contributed by Arthur B. Pardee, November 10, 1997§ ABSTRACT The maspin protein has tumor suppressor that PAI-1 also inhibits cell motility via an integrin-mediated activity in breast and prostate cancers. It inhibits cell motility pathway by its interaction with cell surface-bound uPA and and invasion in vitro and tumor growth and metastasis in nude vitronectin (8, 9). mice. Maspin is structurally a member of the serpin (serine The RSL of maspin is shorter than that of other serpins (1), protease inhibitors) superfamily but deviates somewhat from casting doubt on its ability to act as a classical inhibitory serpin. classical serpins. We find that single-chain tissue plasmino- Pemberton et al. (10) reported that purified rMaspin(i) is a gen activator (sctPA) specifically interacts with the maspin substrate instead of an inhibitor to an array of serine proteases, reactive site loop peptide and forms a stable complex with including uPA and tissue-type plasminogen activator (tPA). recombinant maspin [rMaspin(i)]. Major effects of rMas- However, our evidence that the RSL is crucial for the biolog- pin(i) are observed on plasminogen activation by sctPA. First, ical activity of maspin would be consistent with maspin acting rMaspin(i) activates free sctPA. -
The Surface of Prostate Carcinoma DU145 Cells Mediates the Inhibition of Urokinase-Type Plasminogen Activator by Maspin1
[CANCER RESEARCH 60, 4771–4778, September 1, 2000] The Surface of Prostate Carcinoma DU145 Cells Mediates the Inhibition of Urokinase-type Plasminogen Activator by Maspin1 Richard McGowen, Hector Biliran, Jr., Ruth Sager,2 and Shijie Sheng3 Department of Pathology, Wayne State University School of Medicine, Detroit, Michigan 48201 [R. M., H. B., S. S.], and Division of Cancer Genetics, Dana-Farber Cancer Institute, Boston, Massachusetts 02115 [R. S.] ABSTRACT relation between maspin expression and the progression of breast cancer (1, 4). In addition, maspin expression is down-regulated in Maspin is a novel serine protease inhibitor (serpin) with tumor prostate carcinoma cells compared with that in immortalized normal suppressive potential in breast and prostate cancer, acting at the level of tumor invasion and metastasis. It was subsequently demonstrated prostate epithelial cells (5, 6). that maspin inhibits tumor invasion, at least in part, by inhibiting cell Biological studies demonstrate a tumor-suppressive role of maspin, motility. Interestingly, in cell-free solutions, maspin does not inhibit acting at the levels of tumor invasion and metastases. Mammary several serine proteases including tissue-type plasminogen activator carcinoma MDA-MB-435 cells transfected with maspin cDNA are and urokinase-type plasminogen activator (uPA). Despite the recent significantly inhibited in invasion and motility assays in vitro and are biochemical evidence that maspin specifically inhibits tissue-type plas- inhibited in tumor growth and metastasis in nude mice (1, 5, 7). It has minogen activator that is associated with fibrinogen or poly-L-lysine, been shown independently that induction of maspin expression in four the molecular mechanism underlying the tumor-suppressive effect of different breast tumor cell lines by ␥-linolenic acid dramatically maspin remains elusive. -
Characterisation of Serpinb2 As a Stress Response Modulator
University of Wollongong Research Online University of Wollongong Thesis Collection 1954-2016 University of Wollongong Thesis Collections 2015 Characterisation of SerpinB2 as a stress response modulator Jodi Anne Lee University of Wollongong Follow this and additional works at: https://ro.uow.edu.au/theses University of Wollongong Copyright Warning You may print or download ONE copy of this document for the purpose of your own research or study. The University does not authorise you to copy, communicate or otherwise make available electronically to any other person any copyright material contained on this site. You are reminded of the following: This work is copyright. Apart from any use permitted under the Copyright Act 1968, no part of this work may be reproduced by any process, nor may any other exclusive right be exercised, without the permission of the author. Copyright owners are entitled to take legal action against persons who infringe their copyright. A reproduction of material that is protected by copyright may be a copyright infringement. A court may impose penalties and award damages in relation to offences and infringements relating to copyright material. Higher penalties may apply, and higher damages may be awarded, for offences and infringements involving the conversion of material into digital or electronic form. Unless otherwise indicated, the views expressed in this thesis are those of the author and do not necessarily represent the views of the University of Wollongong. Recommended Citation Lee, Jodi Anne, Characterisation of SerpinB2 as a stress response modulator, Doctor of Philosophy thesis, School of Biological Sciences, University of Wollongong, 2015. https://ro.uow.edu.au/theses/4538 Research Online is the open access institutional repository for the University of Wollongong. -
The Serpintine Solution
& Experim l e ca n i t in a l l C C f a Journal of Clinical & Experimental o r d l i a o n l o r g u Lucas et al., J Clin Exp Cardiolog 2017, 8:1 y o J Cardiology ISSN: 2155-9880 DOI: 10.4172/2155-9880.1000e150 Editorial Open Access The Serpintine Solution Alexandra Lucas, MD, FRCP(C)1,2,*, Sriram Ambadapadi, PhD1, Brian Mahon, PhD3, Kasinath Viswanathan, PhD4, Hao Chen, MD, PhD5, Liying Liu, MD6, Erbin Dai, MD6, Ganesh Munuswami-Ramanujam, PhD7, Jacek M. Kwiecien, DVM, MSc, PhD8, Jordan R Yaron, PhD1, Purushottam Shivaji Narute, BVSc & AH, MVSc, PhD1,9, Robert McKenna, PhD10, Shahar Keinan, PhD11, Westley Reeves, MD, PhD12, Mark Brantly, MD, PhD13, Carl Pepine, MD, FACC14 and Grant McFadden, PhD1 1Center for Personalized Diagnostics, Biodesign Institute, Arizona State University, Tempe AZ, USA 2Saint Josephs Hospital, Dignity Health Phoenix, Phoenix, AZ, USA 3NIH/ NIDDK, Bethesda MD, USA 4Zydus Research Centre, Ahmedabad, India 5Department of tumor surgery, The Second Hospital of Lanzhou University, Lanzhou, Gansu, P.R.China 6Beth Israel Deaconess Medical Center, Harvard, Boston, MA, USA 7Interdisciplinary Institute of Indian system of Medicine (IIISM), SRM University, Chennai, Tamil Nadu, India 8MacMaster University, Hamilton, ON, Canada 9Critical Care Medicine Department, Clinical Center, National Institutes of Health, Bethesda MD, USA 10Department of Molecular Genetics and Microbiology, University of Florida, Gainesville, FL, USA 11Cloud Pharmaceuticals, Durham, North Carolina, USA 12Division of Rheumatology, University of Florida, -
Gene Symbol Category ACAN ECM ADAM10 ECM Remodeling-Related ADAM11 ECM Remodeling-Related ADAM12 ECM Remodeling-Related ADAM15 E
Supplementary Material (ESI) for Integrative Biology This journal is (c) The Royal Society of Chemistry 2010 Gene symbol Category ACAN ECM ADAM10 ECM remodeling-related ADAM11 ECM remodeling-related ADAM12 ECM remodeling-related ADAM15 ECM remodeling-related ADAM17 ECM remodeling-related ADAM18 ECM remodeling-related ADAM19 ECM remodeling-related ADAM2 ECM remodeling-related ADAM20 ECM remodeling-related ADAM21 ECM remodeling-related ADAM22 ECM remodeling-related ADAM23 ECM remodeling-related ADAM28 ECM remodeling-related ADAM29 ECM remodeling-related ADAM3 ECM remodeling-related ADAM30 ECM remodeling-related ADAM5 ECM remodeling-related ADAM7 ECM remodeling-related ADAM8 ECM remodeling-related ADAM9 ECM remodeling-related ADAMTS1 ECM remodeling-related ADAMTS10 ECM remodeling-related ADAMTS12 ECM remodeling-related ADAMTS13 ECM remodeling-related ADAMTS14 ECM remodeling-related ADAMTS15 ECM remodeling-related ADAMTS16 ECM remodeling-related ADAMTS17 ECM remodeling-related ADAMTS18 ECM remodeling-related ADAMTS19 ECM remodeling-related ADAMTS2 ECM remodeling-related ADAMTS20 ECM remodeling-related ADAMTS3 ECM remodeling-related ADAMTS4 ECM remodeling-related ADAMTS5 ECM remodeling-related ADAMTS6 ECM remodeling-related ADAMTS7 ECM remodeling-related ADAMTS8 ECM remodeling-related ADAMTS9 ECM remodeling-related ADAMTSL1 ECM remodeling-related ADAMTSL2 ECM remodeling-related ADAMTSL3 ECM remodeling-related ADAMTSL4 ECM remodeling-related ADAMTSL5 ECM remodeling-related AGRIN ECM ALCAM Cell-cell adhesion ANGPT1 Soluble factors and receptors -
Pso P27, a SERPINB3/B4-Derived Protein, Is Most Likely a Common Autoantigen in Chronic Inflammatory Diseases
Clinical Immunology 174 (2017) 10–17 Contents lists available at ScienceDirect Clinical Immunology journal homepage: www.elsevier.com/locate/yclim Pso p27, a SERPINB3/B4-derived protein, is most likely a common autoantigen in chronic inflammatory diseases Ole-Jan Iversen a,⁎,HildeLysvanda, Geir Slupphaug b a Department of Laboratory Medicine, Children's and Women's Health, Faculty of Medicine, Norwegian University of Science and Technology, NTNU, Trondheim, Norway b Department of Cancer Research and Molecular Medicine, Faculty of Medicine and PROMEC Core Facility for Proteomics and Metabolomics, Norwegian University of Science and Technology, NTNU, Trondheim, Norway article info abstract Article history: Autoimmune diseases are characterized by chronic inflammatory reactions localized to an organ or organ- Received 17 October 2016 system. They are caused by loss of immunologic tolerance toward self-antigens, causing formation of autoanti- Received in revised form 1 November 2016 bodies that mistakenly attack their own body. Psoriasis is a chronic inflammatory autoimmune skin disease in accepted with revision 13 November 2016 which the underlying molecular mechanisms remain elusive. In this review, we present evidence accumulated Available online 15 November 2016 through more than three decades that the serpin-derived protein Pso p27 is an autoantigen in psoriasis and prob- ably also in other chronic inflammatory diseases. Keywords: Autoimmune diseases Pso p27 is derived from the serpin molecules SERPINB3 and SERPINB4 through non-canonical cleavage by mast Pso p27 cell chymase. In psoriasis, it is exclusively found in skin lesions and not in uninvolved skin. The serpins are cleaved SERPINB3/B4 into three fragments that remain associated as a Pso p27 complex with novel immunogenic properties and in- Mast cells creased tendency to form large aggregates compared to native SERPINB3/B4. -
Re-Activation of a Dormant Tumor Suppressor Gene Maspin by Designed Transcription Factors
Oncogene (2007) 26, 2791–2798 & 2007 Nature Publishing Group All rights reserved 0950-9232/07 $30.00 www.nature.com/onc SHORT COMMUNICATION Re-activation of a dormant tumor suppressor gene maspin by designed transcription factors A Beltran1, S Parikh1, Y Liu1, BD Cuevas1, GL Johnson1, BW Futscher2 and P Blancafort1 1Department of Pharmacology and the Lineberger Comprehensive Cancer Center, The University of North Carolina at Chapel Hill, Chapel Hill, NC, USA and 2Department of Pharmacology and Toxicology, Arizona Cancer Center and College of Pharmacy, University of Arizona, Tucson, AZ, USA The controlled and specific re-activation of endogenous Tumor progression is a dynamic process controlled by tumor suppressors in cancer cells represents an important multiple genetic factors, including oncogenes, which therapeutic strategy to block tumor growth and subse- facilitate tumor growth, and tumor suppressors, which quent progression. Other than ectopic delivery of tumor negatively regulate tumor growth and progression. Since suppressor-encoded cDNA, there are no therapeutic tools the discovery of the tumor suppressor p53, more than 15 able to specifically re-activate tumor suppressor genes that different tumor suppressor genes have been identified are silenced in tumor cells. Herein, we describe a novel (Sherr, 2003; McGarvey et al., 2006). The expression of approach to specifically regulate dormant tumor sup- tumor suppressors is downregulated in tumor cells by pressors in aggressive cancer cells. We have targeted means of genetic and epigenetic mechanisms (Baylin, the Mammary Serine Protease Inhibitor (maspin) 2005; Zardo et al., 2005). Given the importance of (SERPINB5) tumor suppressor, which is silenced by tumor suppressors in controlling primary tumor growth, transcriptionaland aberrant promoter methylation in many therapeutic strategies aim to restore their expres- aggressive epithelial tumors.