Correlation of Serpin–Protease Expression by Comparative Analysis of Real-Time PCR Profiling Data
Total Page:16
File Type:pdf, Size:1020Kb
Load more
Recommended publications
-
Supplementary Information Changes in the Plasma Proteome At
Supplementary Information Changes in the plasma proteome at asymptomatic and symptomatic stages of autosomal dominant Alzheimer’s disease Julia Muenchhoff1, Anne Poljak1,2,3, Anbupalam Thalamuthu1, Veer B. Gupta4,5, Pratishtha Chatterjee4,5,6, Mark Raftery2, Colin L. Masters7, John C. Morris8,9,10, Randall J. Bateman8,9, Anne M. Fagan8,9, Ralph N. Martins4,5,6, Perminder S. Sachdev1,11,* Supplementary Figure S1. Ratios of proteins differentially abundant in asymptomatic carriers of PSEN1 and APP Dutch mutations. Mean ratios and standard deviations of plasma proteins from asymptomatic PSEN1 mutation carriers (PSEN1) and APP Dutch mutation carriers (APP) relative to reference masterpool as quantified by iTRAQ. Ratios that significantly differed are marked with asterisks (* p < 0.05; ** p < 0.01). C4A, complement C4-A; AZGP1, zinc-α-2-glycoprotein; HPX, hemopexin; PGLYPR2, N-acetylmuramoyl-L-alanine amidase isoform 2; α2AP, α-2-antiplasmin; APOL1, apolipoprotein L1; C1 inhibitor, plasma protease C1 inhibitor; ITIH2, inter-α-trypsin inhibitor heavy chain H2. 2 A) ADAD)CSF) ADAD)plasma) B) ADAD)CSF) ADAD)plasma) (Ringman)et)al)2015)) (current)study)) (Ringman)et)al)2015)) (current)study)) ATRN↓,%%AHSG↑% 32028% 49% %%%%%%%%HC2↑,%%ApoM↓% 24367% 31% 10083%% %%%%TBG↑,%%LUM↑% 24256% ApoC1↓↑% 16565% %%AMBP↑% 11738%%% SERPINA3↓↑% 24373% C6↓↑% ITIH2% 10574%% %%%%%%%CPN2↓%% ↓↑% %%%%%TTR↑% 11977% 10970% %SERPINF2↓↑% CFH↓% C5↑% CP↓↑% 16566% 11412%% 10127%% %%ITIH4↓↑% SerpinG1↓% 11967% %%ORM1↓↑% SerpinC1↓% 10612% %%%A1BG↑%%% %%%%FN1↓% 11461% %%%%ITIH1↑% C3↓↑% 11027% 19325% 10395%% %%%%%%HPR↓↑% HRG↓% %%% 13814%% 10338%% %%% %ApoA1 % %%%%%%%%%GSN↑% ↓↑ %%%%%%%%%%%%ApoD↓% 11385% C4BPA↓↑% 18976%% %%%%%%%%%%%%%%%%%ApoJ↓↑% 23266%%%% %%%%%%%%%%%%%%%%%%%%%%ApoA2↓↑% %%%%%%%%%%%%%%%%%%%%%%%%%%%%A2M↓↑% IGHM↑,%%GC↓↑,%%ApoB↓↑% 13769% % FGA↓↑,%%FGB↓↑,%%FGG↓↑% AFM↓↑,%%CFB↓↑,%% 19143%% ApoH↓↑,%%C4BPA↓↑% ApoA4↓↑%%% LOAD/MCI)plasma) LOAD/MCI)plasma) LOAD/MCI)plasma) LOAD/MCI)plasma) (Song)et)al)2014)) (Muenchhoff)et)al)2015)) (Song)et)al)2014)) (Muenchhoff)et)al)2015)) Supplementary Figure S2. -
Ige-Mediated Mast Cell Activation Promotes Inflammation And
RESEARCH COMMUNICATION IgE-mediated mast cell activation promotes inflammation and cartilage destruction in osteoarthritis Qian Wang1,2†, Christin M Lepus1,2†, Harini Raghu1,2†, Laurent L Reber3‡, Mindy M Tsai3, Heidi H Wong1,2, Ericka von Kaeppler1,2, Nithya Lingampalli1,2, Michelle S Bloom1,2, Nick Hu1,2, Eileen E Elliott1,2, Francesca Oliviero4, Leonardo Punzi4, Nicholas J Giori1,5, Stuart B Goodman5, Constance R Chu1,5, Jeremy Sokolove1,2, Yoshihiro Fukuoka6, Lawrence B Schwartz6, Stephen J Galli3,7, William H Robinson1,2* 1GRECC, VA Palo Alto Health Care System, Palo Alto, United States; 2Division of Immunology and Rheumatology, Stanford University School of Medicine, Stanford, United States; 3Department of Pathology, Stanford University School of Medicine, Stanford, United States; 4Rheumatology Unit, Department of Medicine, University of Padova, Padova, Italy; 5Department of Orthopedic Surgery, Stanford University School of Medicine, Stanford, United States; 6Department of Internal Medicine, Virginia Commonwealth University School of Medicine, Richmond, United States; 7Department of Microbiology and Immunology, Stanford University School of Medicine, Stanford, United States *For correspondence: [email protected] Abstract Osteoarthritis is characterized by articular cartilage breakdown, and emerging †These authors contributed evidence suggests that dysregulated innate immunity is likely involved. Here, we performed equally to this work proteomic, transcriptomic, and electron microscopic analyses to demonstrate that mast cells are Present address: ‡Center for aberrantly activated in human and murine osteoarthritic joint tissues. Using genetic models of mast Physiopathology of Toulouse- cell deficiency, we demonstrate that lack of mast cells attenuates osteoarthritis in mice. Using Purpan (CPTP), UMR 1043, genetic and pharmacologic approaches, we show that the IgE/FceRI/Syk signaling axis is critical for University of Toulouse, INSERM, the development of osteoarthritis. -
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. -
Propranolol-Mediated Attenuation of MMP-9 Excretion in Infants with Hemangiomas
Supplementary Online Content Thaivalappil S, Bauman N, Saieg A, Movius E, Brown KJ, Preciado D. Propranolol-mediated attenuation of MMP-9 excretion in infants with hemangiomas. JAMA Otolaryngol Head Neck Surg. doi:10.1001/jamaoto.2013.4773 eTable. List of All of the Proteins Identified by Proteomics This supplementary material has been provided by the authors to give readers additional information about their work. © 2013 American Medical Association. All rights reserved. Downloaded From: https://jamanetwork.com/ on 10/01/2021 eTable. List of All of the Proteins Identified by Proteomics Protein Name Prop 12 mo/4 Pred 12 mo/4 Δ Prop to Pred mo mo Myeloperoxidase OS=Homo sapiens GN=MPO 26.00 143.00 ‐117.00 Lactotransferrin OS=Homo sapiens GN=LTF 114.00 205.50 ‐91.50 Matrix metalloproteinase‐9 OS=Homo sapiens GN=MMP9 5.00 36.00 ‐31.00 Neutrophil elastase OS=Homo sapiens GN=ELANE 24.00 48.00 ‐24.00 Bleomycin hydrolase OS=Homo sapiens GN=BLMH 3.00 25.00 ‐22.00 CAP7_HUMAN Azurocidin OS=Homo sapiens GN=AZU1 PE=1 SV=3 4.00 26.00 ‐22.00 S10A8_HUMAN Protein S100‐A8 OS=Homo sapiens GN=S100A8 PE=1 14.67 30.50 ‐15.83 SV=1 IL1F9_HUMAN Interleukin‐1 family member 9 OS=Homo sapiens 1.00 15.00 ‐14.00 GN=IL1F9 PE=1 SV=1 MUC5B_HUMAN Mucin‐5B OS=Homo sapiens GN=MUC5B PE=1 SV=3 2.00 14.00 ‐12.00 MUC4_HUMAN Mucin‐4 OS=Homo sapiens GN=MUC4 PE=1 SV=3 1.00 12.00 ‐11.00 HRG_HUMAN Histidine‐rich glycoprotein OS=Homo sapiens GN=HRG 1.00 12.00 ‐11.00 PE=1 SV=1 TKT_HUMAN Transketolase OS=Homo sapiens GN=TKT PE=1 SV=3 17.00 28.00 ‐11.00 CATG_HUMAN Cathepsin G OS=Homo -
Biological Function of Mast Cell Chymase
Biological Function of Mast Cell Chymase In vitro and in vivo studies: a thorny pathway Elena Chugunova Department of Molecular Biosciences Uppsala Doctoral thesis Swedish University of Agricultural Sciences Uppsala 2004 Acta Universitatis Agriculturae Sueciae Veterinaria 181 ISSN 1401-6257 ISBN 91-576-6680-6 © 2004 Elena Chugunova, Uppsala Tryck: SLU Service/Repro, Uppsala 2004 Abstract Chugunova, E., 2004. Biological function of mast cell chymase mMCP-4. In vitro and in vivo studies: a thorny pathway. Doctor's dissertation. ISSN 1401-6257, ISBN 91-576-6680-6 Mast cells (MCs) are key effector cells in various types of inflammatory conditions. The MC secretory granules contain inflammatory mediators such as histamine, heparin proteoglycan (PG), cytokines and various heparin-binding proteases, including tryptases, chymases and carboxypeptidase A. Previously, a mouse strain with a defect in its heparin biosynthesis was produced by targeting the gene for NDST-2 (N-deacetylase/N-sulfotransferase-2). These mice showed reduced levels of MC inflammatory mediators such as histamine and various heparin- binding proteases, including chymases, tryptases, and carboxypeptidase A. By using this mouse strain, we found that chymase in complex with heparin PG degraded fibronectin, suggesting a role for chymase in the regulation of connective tissue composition. Further, we found that chymase/heparin PG complexes degraded and thereby inactivated both thrombin and plasmin, suggesting an additional role for chymase in regulation of extravascular coagulation and fibrinolysis. However, although our findings implicated chymase in these processes, it was not possible to exclude the contribution to the observed activities by other MC components that are influenced by the knockout of NDST-2. -
Acinar Cell Apoptosis in Serpini2-Deficient Mice Models Pancreatic Insufficiency
Acinar Cell Apoptosis in Serpini2-Deficient Mice Models Pancreatic Insufficiency Stacie K. Loftus1*, Jennifer L. Cannons1, Arturo Incao1, Evgenia Pak1, Amy Chen1, Patricia M. Zerfas2, Mark A. Bryant2, Leslie G. Biesecker1, Pamela L. Schwartzberg1, William J. Pavan1 1 Genetic Disease Research Branch, National Human Genome Research Institute, National Institutes of Health, Bethesda, Maryland, United States of America, 2 Division of Veterinary Resources, Office of Research Services, National Institutes of Health, Bethesda, Maryland, United States of America Pancreatic insufficiency (PI) when left untreated results in a state of malnutrition due to an inability to absorb nutrients. Frequently, PI is diagnosed as part of a larger clinical presentation in cystic fibrosis or Shwachman–Diamond syndrome. In this study, a mouse model for isolated exocrine PI was identified in a mouse line generated by a transgene insertion. The trait is inherited in an autosomal recessive pattern, and homozygous animals are growth retarded, have abnormal immunity, and have reduced life span. Mice with the disease locus, named pequen˜o (pq), exhibit progressive apoptosis of pancreatic acinar cells with severe exocrine acinar cell loss by 8 wk of age, while the islets and ductal tissue persist. The mutation in pq/pq mice results from a random transgene insertion. Molecular characterization of the transgene insertion site by fluorescent in situ hybridization and genomic deletion mapping identified an approximately 210-kb deletion on Chromosome 3, deleting two genes. One of these genes, Serpini2, encodes a protein that is a member of the serpin family of protease inhibitors. Reintroduction of only the Serpini2 gene by bacterial artificial chromosome transgenic complementation corrected the acinar cell defect as well as body weight and immune phenotypes, showing that deletion of Serpini2 causes the pequen˜o phenotype. -
Mechanisms Governing Anaphylaxis: Inflammatory Cells, Mediators
International Journal of Molecular Sciences Review Mechanisms Governing Anaphylaxis: Inflammatory Cells, Mediators, Endothelial Gap Junctions and Beyond Samantha Minh Thy Nguyen 1, Chase Preston Rupprecht 2, Aaisha Haque 3, Debendra Pattanaik 4, Joseph Yusin 5 and Guha Krishnaswamy 1,3,* 1 Department of Medicine, Wake Forest School of Medicine, Winston-Salem, NC 27106, USA; [email protected] 2 The Rowan School of Osteopathic Medicine, Stratford, NJ 08084, USA; [email protected] 3 The Bill Hefner VA Medical Center, Salisbury, NC 27106, USA; [email protected] 4 Division of Allergy and Immunology, UT Memphis College of Medicine, Memphis, TN 38103, USA; [email protected] 5 The Division of Allergy and Immunology, Greater Los Angeles VA Medical Center, Los Angeles, CA 90011, USA; [email protected] * Correspondence: [email protected] Abstract: Anaphylaxis is a severe, acute, life-threatening multisystem allergic reaction resulting from the release of a plethora of mediators from mast cells culminating in serious respiratory, cardiovascular and mucocutaneous manifestations that can be fatal. Medications, foods, latex, exercise, hormones (progesterone), and clonal mast cell disorders may be responsible. More recently, novel syndromes such as delayed reactions to red meat and hereditary alpha tryptasemia have been described. Anaphylaxis manifests as sudden onset urticaria, pruritus, flushing, erythema, Citation: Nguyen, S.M.T.; Rupprecht, angioedema (lips, tongue, airways, periphery), myocardial dysfunction (hypovolemia, distributive -
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. -
A Computational Approach for Defining a Signature of Β-Cell Golgi Stress in Diabetes Mellitus
Page 1 of 781 Diabetes A Computational Approach for Defining a Signature of β-Cell Golgi Stress in Diabetes Mellitus Robert N. Bone1,6,7, Olufunmilola Oyebamiji2, Sayali Talware2, Sharmila Selvaraj2, Preethi Krishnan3,6, Farooq Syed1,6,7, Huanmei Wu2, Carmella Evans-Molina 1,3,4,5,6,7,8* Departments of 1Pediatrics, 3Medicine, 4Anatomy, Cell Biology & Physiology, 5Biochemistry & Molecular Biology, the 6Center for Diabetes & Metabolic Diseases, and the 7Herman B. Wells Center for Pediatric Research, Indiana University School of Medicine, Indianapolis, IN 46202; 2Department of BioHealth Informatics, Indiana University-Purdue University Indianapolis, Indianapolis, IN, 46202; 8Roudebush VA Medical Center, Indianapolis, IN 46202. *Corresponding Author(s): Carmella Evans-Molina, MD, PhD ([email protected]) Indiana University School of Medicine, 635 Barnhill Drive, MS 2031A, Indianapolis, IN 46202, Telephone: (317) 274-4145, Fax (317) 274-4107 Running Title: Golgi Stress Response in Diabetes Word Count: 4358 Number of Figures: 6 Keywords: Golgi apparatus stress, Islets, β cell, Type 1 diabetes, Type 2 diabetes 1 Diabetes Publish Ahead of Print, published online August 20, 2020 Diabetes Page 2 of 781 ABSTRACT The Golgi apparatus (GA) is an important site of insulin processing and granule maturation, but whether GA organelle dysfunction and GA stress are present in the diabetic β-cell has not been tested. We utilized an informatics-based approach to develop a transcriptional signature of β-cell GA stress using existing RNA sequencing and microarray datasets generated using human islets from donors with diabetes and islets where type 1(T1D) and type 2 diabetes (T2D) had been modeled ex vivo. To narrow our results to GA-specific genes, we applied a filter set of 1,030 genes accepted as GA associated. -
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. -
Mechanism of Interleukin-1- and Tumor Necrosis Factor Α-Dependent Regulation of the Α1-Antichymotrypsin Gene in Human Astrocyt
The Journal of Neuroscience, October 15, 2000, 20(20):7510–7516 Mechanism of Interleukin-1- and Tumor Necrosis Factor ␣- ␣ Dependent Regulation of the 1-Antichymotrypsin Gene in Human Astrocytes Tomasz Kordula,1 Marcin Bugno,1 Russell E. Rydel,2 and James Travis3 1Institute of Molecular Biology, Jagiellonian University, 31-120 Krako´ w, Poland, 2Elan Pharmaceuticals, South San Francisco, California 94080, and 3Department of Biochemistry and Molecular Biology, The University of Georgia, Athens, Georgia 30602 ␣ The expression of 1-antichymotrypsin (ACT) is significantly en- which bind nuclear factor kB (NF-kB) and one that binds activat- hanced in affected brain regions in Alzheimer’s disease. This ing protein 1 (AP-1). All of these elements contribute to the full serine proteinase inhibitor specifically colocalizes with filamen- responsiveness of the ACT gene to both cytokines, as deter- tous -amyloid deposits and recently has been shown to influ- mined by deletion and mutational analysis. The 5Ј NF-kB high- ence both formation and destabilization of -amyloid fibrils. In affinity binding site and AP-1 element contribute most to the the brain, ACT is expressed in astrocytes, and interleukin-1 (IL-1), enhancement of gene transcription in response to TNF and IL-1. tumor necrosis factor ␣ (TNF), oncostatin M (OSM), and IL-6/ In addition, we demonstrate that the 5Ј untranslated region of the soluble IL-6 receptor complexes control synthesis of this inhibi- ACT mRNA does not contribute to cytokine-mediated activation. tor. Here, we characterize a molecular mechanism responsible Finally, we find that overexpression of the NF-kB inhibitor (IkB) for both IL-1 and TNF-induced expression of ACT gene in astro- totally inhibits any activation mediated by the newly identified cytes. -
Differential Gene Expression of Serine Protease Inhibitors in Bovine
Hayashi et al. Reproductive Biology and Endocrinology 2011, 9:72 http://www.rbej.com/content/9/1/72 RESEARCH Open Access Differential gene expression of serine protease inhibitors in bovine ovarian follicle: possible involvement in follicular growth and atresia Ken-Go Hayashi, Koichi Ushizawa, Misa Hosoe and Toru Takahashi* Abstract Background: SERPINs (serine protease inhibitors) regulate proteases involving fibrinolysis, coagulation, inflammation, cell mobility, cellular differentiation and apoptosis. This study aimed to investigate differentially expressed genes of members of the SERPIN superfamily between healthy and atretic follicles using a combination of microarray and quantitative real-time PCR (QPCR) analysis. In addition, we further determined mRNA and protein localization of identified SERPINs in estradiol (E2)-active and E2-inactive follicles by in situ hybridization and immunohistochemistry. Methods: We performed microarray analysis of healthy (10.7 +/- 0.7 mm) and atretic (7.8 +/- 0.2 mm) follicles using a custom-made bovine oligonucleotide microarray to screen differentially expressed genes encoding SERPIN superfamily members between groups. The expression profiles of six identified SERPIN genes were further confirmed by QPCR analysis. In addition, mRNA and protein localization of four SERPINs was investigated in E2- active and E2-inactive follicles using in situ hybridization and immunohistochemistry. Results: We have identified 11 SERPIN genes expressed in healthy and atretic follicles by microarray analysis. QPCR analysis confirmed that mRNA expression of four SERPINs (SERPINA5, SERPINB6, SERPINE2 and SERPINF2) was greater in healthy than in atretic follicles, while two SERPINs (SERPINE1 and SERPING1) had greater expression in atretic than in healthy follicles. In situ hybridization showed that SERPINA5, SERPINB6 and SERPINF2 mRNA were localized in GCs of E2-active follicles and weakly expressed in GCs of E2-inactive follicles.