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Molecular Mechanism of ACAD9 in Mitochondrial Respiratory Complex 1 Assembly
bioRxiv preprint doi: https://doi.org/10.1101/2021.01.07.425795; this version posted January 9, 2021. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. Molecular mechanism of ACAD9 in mitochondrial respiratory complex 1 assembly Chuanwu Xia1, Baoying Lou1, Zhuji Fu1, Al-Walid Mohsen2, Jerry Vockley2, and Jung-Ja P. Kim1 1Department of Biochemistry, Medical College of Wisconsin, Milwaukee, Wisconsin, 53226, USA 2Department of Pediatrics, University of Pittsburgh School of Medicine, University of Pittsburgh, Children’s Hospital of Pittsburgh of UPMC, Pittsburgh, PA 15224, USA Abstract ACAD9 belongs to the acyl-CoA dehydrogenase family, which catalyzes the α-β dehydrogenation of fatty acyl-CoA thioesters. Thus, it is involved in fatty acid β-oxidation (FAO). However, it is now known that the primary function of ACAD9 is as an essential chaperone for mitochondrial respiratory complex 1 assembly. ACAD9 interacts with ECSIT and NDUFAF1, forming the mitochondrial complex 1 assembly (MCIA) complex. Although the role of MCIA in the complex 1 assembly pathway is well studied, little is known about the molecular mechanism of the interactions among these three assembly factors. Our current studies reveal that when ECSIT interacts with ACAD9, the flavoenzyme loses the FAD cofactor and consequently loses its FAO activity, demonstrating that the two roles of ACAD9 are not compatible. ACAD9 binds to the carboxy-terminal half (C-ECSIT), and NDUFAF1 binds to the amino-terminal half of ECSIT. Although the binary complex of ACAD9 with ECSIT or with C-ECSIT is unstable and aggregates easily, the ternary complex of ACAD9-ECSIT-NDUFAF1 (i.e., the MCIA complex) is soluble and extremely stable. -
Supplementary Table 1. in Vitro Side Effect Profiling Study for LDN/OSU-0212320. Neurotransmitter Related Steroids
Supplementary Table 1. In vitro side effect profiling study for LDN/OSU-0212320. Percent Inhibition Receptor 10 µM Neurotransmitter Related Adenosine, Non-selective 7.29% Adrenergic, Alpha 1, Non-selective 24.98% Adrenergic, Alpha 2, Non-selective 27.18% Adrenergic, Beta, Non-selective -20.94% Dopamine Transporter 8.69% Dopamine, D1 (h) 8.48% Dopamine, D2s (h) 4.06% GABA A, Agonist Site -16.15% GABA A, BDZ, alpha 1 site 12.73% GABA-B 13.60% Glutamate, AMPA Site (Ionotropic) 12.06% Glutamate, Kainate Site (Ionotropic) -1.03% Glutamate, NMDA Agonist Site (Ionotropic) 0.12% Glutamate, NMDA, Glycine (Stry-insens Site) 9.84% (Ionotropic) Glycine, Strychnine-sensitive 0.99% Histamine, H1 -5.54% Histamine, H2 16.54% Histamine, H3 4.80% Melatonin, Non-selective -5.54% Muscarinic, M1 (hr) -1.88% Muscarinic, M2 (h) 0.82% Muscarinic, Non-selective, Central 29.04% Muscarinic, Non-selective, Peripheral 0.29% Nicotinic, Neuronal (-BnTx insensitive) 7.85% Norepinephrine Transporter 2.87% Opioid, Non-selective -0.09% Opioid, Orphanin, ORL1 (h) 11.55% Serotonin Transporter -3.02% Serotonin, Non-selective 26.33% Sigma, Non-Selective 10.19% Steroids Estrogen 11.16% 1 Percent Inhibition Receptor 10 µM Testosterone (cytosolic) (h) 12.50% Ion Channels Calcium Channel, Type L (Dihydropyridine Site) 43.18% Calcium Channel, Type N 4.15% Potassium Channel, ATP-Sensitive -4.05% Potassium Channel, Ca2+ Act., VI 17.80% Potassium Channel, I(Kr) (hERG) (h) -6.44% Sodium, Site 2 -0.39% Second Messengers Nitric Oxide, NOS (Neuronal-Binding) -17.09% Prostaglandins Leukotriene, -
TLR2 Signaling Pathway Combats Streptococcus Uberis Infection by Inducing Mitochondrial Reactive Oxygen Species Production
cells Article TLR2 Signaling Pathway Combats Streptococcus uberis Infection by Inducing Mitochondrial Reactive Oxygen Species Production 1, 1, 1 1,2 1 2 Bin Li y, Zhixin Wan y, Zhenglei Wang , Jiakun Zuo , Yuanyuan Xu , Xiangan Han , Vanhnaseng Phouthapane 3 and Jinfeng Miao 1,* 1 MOE Joint International Research Laboratory of Animal Health and Food Safty, Key Laboratory of Animal Physiology and Biochemistry, College of Veterinary Medicine, Nanjing Agricultural University, Nanjing 210095, China; [email protected] (B.L.); [email protected] (Z.W.); [email protected] (Z.W.); [email protected] (J.Z.); [email protected] (Y.X.) 2 Shanghai Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Shanghai 200241, China; [email protected] 3 Biotechnology and Ecology Institute, Ministry of Science and Technology (MOST), Vientiane 22797, Laos; [email protected] * Correspondence: [email protected]; Fax: +86-25-8439-8669 These authors contributed equally to this work. y Received: 6 January 2020; Accepted: 19 February 2020; Published: 21 February 2020 Abstract: Mastitis caused by Streptococcus uberis (S. uberis) is a common and difficult-to-cure clinical disease in dairy cows. In this study, the role of Toll-like receptors (TLRs) and TLR-mediated signaling pathways in mastitis caused by S. uberis was investigated using mouse models and mammary / epithelial cells (MECs). We used S. uberis to infect mammary glands of wild type, TLR2− − and / TLR4− − mice and quantified the adaptor molecules in TLR signaling pathways, proinflammatory cytokines, tissue damage, and bacterial count. When compared with TLR4 deficiency, TLR2 deficiency induced more severe pathological changes through myeloid differentiation primary response 88 (MyD88)-mediated signaling pathways during S. -
Anti-Eph Receptor A1 Antibody Catalog # ABO10887
10320 Camino Santa Fe, Suite G San Diego, CA 92121 Tel: 858.875.1900 Fax: 858.622.0609 Anti-Eph Receptor A1 Antibody Catalog # ABO10887 Specification Anti-Eph Receptor A1 Antibody - Product Information Application WB, IHC Primary Accession P21709 Host Rabbit Reactivity Human, Mouse, Rat Clonality Polyclonal Format Lyophilized Description Rabbit IgG polyclonal antibody for Ephrin type-A receptor 1(EPHA1) detection. Tested with WB, IHC-P in Human;Mouse;Rat. Reconstitution Anti-Eph receptor A1 antibody, ABO10887, Add 0.2ml of distilled water will yield a Western blottingLane 1: Rat Liver Tissue concentration of 500ug/ml. LysateLane 2: Rat Lung Tissue LysateLane 3: Rat Intestine Tissue LysateLane 4: Rat Ovary Tissue LysateLane 5: U87 Cell LysateLane 6: Anti-Eph Receptor A1 Antibody - Additional A549 Cell LysateLane 7: COLO320 Cell Information LysateLane 8: SW620 Cell LysateLane 9: HELA Cell Lysate Gene ID 2041 Other Names Ephrin type-A receptor 1, hEpha1, 2.7.10.1, EPH tyrosine kinase, EPH tyrosine kinase 1, Erythropoietin-producing hepatoma receptor, Tyrosine-protein kinase receptor EPH, EPHA1, EPH, EPHT, EPHT1 Calculated MW 108127 MW KDa Application Details Immunohistochemistry(Paraffin-embedded Anti-Eph receptor A1 antibody, ABO10887, Section), 0.5-1 µg/ml, Human, Rat, Mouse, IHC(P)IHC(P): Rat Brain Tissue By Heat<br>Western blot, 0.1-0.5 µg/ml, Human, Rat, Mouse<br> Subcellular Localization Cell membrane ; Single-pass type I membrane protein . Tissue Specificity Overexpressed in several carcinomas. Page 1/3 10320 Camino Santa Fe, Suite G San Diego, CA 92121 Tel: 858.875.1900 Fax: 858.622.0609 Protein Name Ephrin type-A receptor 1(hEpha1) Contents Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg Thimerosal, 0.05mg NaN3. -
Ecsit Is Required for Bmp Signaling and Mesoderm Formation During Mouse Embryogenesis
Downloaded from genesdev.cshlp.org on September 30, 2021 - Published by Cold Spring Harbor Laboratory Press Ecsit is required for Bmp signaling and mesoderm formation during mouse embryogenesis Changchun Xiao,1 Jae-hyuck Shim,1,6 Michael Klüppel,5,6 Samuel Shao-Min Zhang,3,6 Chen Dong,1,7 Richard A. Flavell,1 Xin-Yuan Fu,3 Jeffrey L. Wrana,5 Brigid L.M. Hogan,4 and Sankar Ghosh1,2,8 1Section of Immunobiology, 2Department of Molecular Biophysics and Biochemistry, Howard Hughes Medical Institute, and 3Department of Pathology, Yale University School of Medicine, New Haven, Connecticut 06520, USA; 4Department of Cell Biology, Duke University Medical Center, Durham, North Carolina 27710, USA; 5Programme in Molecular Biology and Cancer, Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ontario M5G 1X5, Canada Bone morphogenetic proteins (Bmps) are members of the transforming growth factor  (TGF) superfamily that play critical roles during mouse embryogenesis. Signaling by Bmp receptors is mediated mainly by Smad proteins. In this study, we show that a targeted null mutation of Ecsit, encoding a signaling intermediate of the Toll pathway, leads to reduced cell proliferation, altered epiblast patterning, impairment of mesoderm formation, and embryonic lethality at embryonic day 7.5 (E7.5), phenotypes that mimic the Bmp receptor type1a (Bmpr1a) null mutant. In addition, specific Bmp target gene expression is abolished in the absence of Ecsit. Biochemical analysis demonstrates that Ecsit associates constitutively with Smad4 and associates with Smad1 in a Bmp-inducible manner. Together with Smad1 and Smad4, Ecsit binds to the promoter of specific Bmp target genes. Finally, knock-down of Ecsit with Ecsit-specific short hairpin RNA inhibits both Bmp and Toll signaling. -
Mitochondrial Medicine in the Omics Era
Mitochondrial Medicine in the Omics Era Joyeeta Rahman1 and Shamima Rahman1,2* 1 Mitochondrial Research Group, UCL Great Ormond Street Institute of Child Health and 2 Metabolic Unit, Great Ormond Street Hospital NHS Foundation Trust, London, UK *Correspondence to: Professor Shamima Rahman Mitochondrial Research Group Genetics and Genomic Medicine UCL Great Ormond Street Institute of Child Health London WC1N 1EH, UK. Telephone: +44 (0)2079052608 [email protected] Keywords: Mitochondrial disease, OXPHOS, signalling, omics, genomics, transcriptomics, proteomics, metabolomics, mitochondrial stress response, treatment 1 Abstract Mitochondria are dynamic bioenergetic organelles whose maintenance requires ~1500 proteins from two genomes. Mutations in either the mitochondrial or nuclear genome can disrupt a plethora of cellular metabolic and homeostatic functions. Mitochondrial diseases represent one the most common and severe groups of inherited genetic disorders, characterised by clinical, biochemical, and genetic heterogeneity, diagnostic odysseys, and lack of curative therapies. This review aims to discuss recent advances in mitochondrial biology and medicine arising from widespread utilisation of high-throughput omics technologies, and also includes a broad discussion of emerging therapies for mitochondrial disease. New insights into both bioenergetic and biosynthetic mitochondrial functionalities have expedited the genetic diagnosis of primary mitochondrial disorders, and identified novel mitochondrial pathomechanisms and new targets -
6 Signaling and BMP Antagonist Noggin in Prostate Cancer
[CANCER RESEARCH 64, 8276–8284, November 15, 2004] Bone Morphogenetic Protein (BMP)-6 Signaling and BMP Antagonist Noggin in Prostate Cancer Dominik R. Haudenschild, Sabrina M. Palmer, Timothy A. Moseley, Zongbing You, and A. Hari Reddi Center for Tissue Regeneration and Repair, Department of Orthopedic Surgery, School of Medicine, University of California, Davis, Sacramento, California ABSTRACT antagonists has recently been discovered. These are secreted proteins that bind to BMPs and reduce their bioavailability for interactions It has been proposed that the osteoblastic nature of prostate cancer with the BMP receptors. Extracellular BMP antagonists include nog- skeletal metastases is due in part to elevated activity of bone morphoge- gin, follistatin, sclerostatin, chordin, DCR, BMPMER, cerberus, netic proteins (BMPs). BMPs are osteoinductive morphogens, and ele- vated expression of BMP-6 correlates with skeletal metastases of prostate gremlin, DAN, and others (refs. 11–16; reviewed in ref. 17). There are cancer. In this study, we investigated the expression levels of BMPs and several type I and type II receptors that bind to BMPs with different their modulators in prostate, using microarray analysis of cell cultures affinities. BMP activity is also regulated at the cell membrane level by and gene expression. Addition of exogenous BMP-6 to DU-145 prostate receptor antagonists such as BAMBI (18), which acts as a kinase- cancer cell cultures inhibited their growth by up-regulation of several deficient receptor. Intracellularly, the regulation of BMP activity at cyclin-dependent kinase inhibitors such as p21/CIP, p18, and p19. Expres- the signal transduction level is even more complex. There are inhib- sion of noggin, a BMP antagonist, was significantly up-regulated by itory Smads (Smad-6 and Smad-7), as well as inhibitors of inhibitory BMP-6 by microarray analysis and was confirmed by quantitative reverse Smads (AMSH and Arkadia). -
Supp Tables.Pdf
Supplementary Table 1. Complete list of 1,628 human samples included in the study Normal Tissues Tumorigenic Samples Non-cancerous diseases n n n (n: 424) (n: 1054) (n: 150) Primary tissues (n: 390) Solid tumors (n: 611) Aorta (n: 18) Aorta 2 Bladder 44 Atherosclerotic lesions 18 Apheresis 4 Breast 76 Bladder 8 Cervix 4 Blood (n: 86) Blood 180 Colon 110 Lupus 7 Bone marrow 14 Endometrium 68 Autism 30 Brain 6 Esophagus 13 Alzheimer 35 Breast 2 Ganglioneurom 1 Primary biliary cirrhosis (PBC) 4 Buccal epithelium 21 Glioma 90 Systemic sclerosis (SSc) 10 Cerebellum 1 Head-neck 9 Cervix 1 Kidney 5 Brain (n: 26) Colon 97 Liver 19 Alzheimer 11 Endometrium 2 Melanoma 21 Dementia (with Lewy bodies) 13 Esophagus 5 Neuroblastoma 16 Parkinson 1 Fetal brain 1 Non-small Cell Lung Carcinoma 23 Heart 2 Ovarian 30 Muscle (n: 17) Liver 5 Pancreas* 29 Myopathies 17 Lung 3 Prostate 14 Muscle 5 Stomach 16 Ovary 2 Testis 23 Immunodeficiency, Centromere Pancreas 7 instability and Facial anomalies Prostate 5 Hematologic malignancies (n: 244) syndrome (ICF syndrome) 4 Skin 5 Acute lymphoblastic leukemia (ALL) 58 Stomach 7 Acute myeloblastic leukemia (AML) 34 Suprarenal gland 1 Chronic lymphocytic leukemia (CLL) 25 Testis 4 Diffuse large B-cell lymphoma (DLBCL) 49 Follicular lymphoma (FL) 14 Normal cell lines (n: 7) Mantle cell lymphoma (MCL) 10 Lymphoblastoid 6 Molecular Burkitt's lymphoma (mBL) 18 Melanocyte 1 Multiple myeloma (MM) 14 Myeloproliferative syndromes (MDS/MPS) 13 Stem Cells (n: 27) Mixed lineage leukemia 9 Adult 19 Embryonic 8 Metastases (n:50) Colon to Liver 32 Colon to Brain 13 Kidney to Brain 5 Premalignant lesions (n: 25) Adenomas (colon) 12 Breast 7 Endometrium hyperplasia 6 Cancer cell lines (n: 82) Breast 6 Cervix 4 Colon 10 Esophagus 2 Head-neck 2 Leukemia 3 Liver 3 Lung 10 Lymphoma 23 Melanocyte 2 Neuroblastoma 2 Pancreas 12 Prostate 3 Carcinoma of unknow primary (CUP) 42 Supplementary Table 2. -
The Human Gene Connectome As a Map of Short Cuts for Morbid Allele Discovery
The human gene connectome as a map of short cuts for morbid allele discovery Yuval Itana,1, Shen-Ying Zhanga,b, Guillaume Vogta,b, Avinash Abhyankara, Melina Hermana, Patrick Nitschkec, Dror Friedd, Lluis Quintana-Murcie, Laurent Abela,b, and Jean-Laurent Casanovaa,b,f aSt. Giles Laboratory of Human Genetics of Infectious Diseases, Rockefeller Branch, The Rockefeller University, New York, NY 10065; bLaboratory of Human Genetics of Infectious Diseases, Necker Branch, Paris Descartes University, Institut National de la Santé et de la Recherche Médicale U980, Necker Medical School, 75015 Paris, France; cPlateforme Bioinformatique, Université Paris Descartes, 75116 Paris, France; dDepartment of Computer Science, Ben-Gurion University of the Negev, Beer-Sheva 84105, Israel; eUnit of Human Evolutionary Genetics, Centre National de la Recherche Scientifique, Unité de Recherche Associée 3012, Institut Pasteur, F-75015 Paris, France; and fPediatric Immunology-Hematology Unit, Necker Hospital for Sick Children, 75015 Paris, France Edited* by Bruce Beutler, University of Texas Southwestern Medical Center, Dallas, TX, and approved February 15, 2013 (received for review October 19, 2012) High-throughput genomic data reveal thousands of gene variants to detect a single mutated gene, with the other polymorphic genes per patient, and it is often difficult to determine which of these being of less interest. This goes some way to explaining why, variants underlies disease in a given individual. However, at the despite the abundance of NGS data, the discovery of disease- population level, there may be some degree of phenotypic homo- causing alleles from such data remains somewhat limited. geneity, with alterations of specific physiological pathways under- We developed the human gene connectome (HGC) to over- come this problem. -
Instability in NAD Metabolism Leads to Impaired Cardiac Mitochondrial
RESEARCH ARTICLE Instability in NAD+ metabolism leads to impaired cardiac mitochondrial function and communication Knut H Lauritzen1*, Maria Belland Olsen1, Mohammed Shakil Ahmed2, Kuan Yang1, Johanne Egge Rinholm3, Linda H Bergersen4,5, Qin Ying Esbensen6, Lars Jansen Sverkeli7, Mathias Ziegler7, Ha˚ vard Attramadal2, Bente Halvorsen1,8, Pa˚ l Aukrust1,8,9, Arne Yndestad1,8 1Research Institute of Internal Medicine, Oslo University Hospital, Rikshospitalet and University of Oslo, Oslo, Norway; 2Institute for Surgical Research, Oslo University Hospital and University of Oslo, Oslo, Norway; 3Department of Microbiology, Oslo University Hospital, Oslo, Norway; 4Department of Oral Biology, University of Oslo, Oslo, Norway; 5Department of Neuroscience and Pharmacology, Center for Healthy Aging, University of Copenhagen, Copenhagen, Denmark; 6Department of Clinical Molecular Biology, University of Oslo and Akershus University Hospital, Nordbyhagen, Norway; 7Department of Biomedicine, University of Bergen, Bergen, Norway; 8Institute of Clinical Medicine, University of Oslo, Faculty of Medicine, Oslo, Norway; 9Section of Clinical Immunology and Infectious Diseases, Oslo University Hospital Rikshospitalet, Oslo, Norway Abstract Poly(ADP-ribose) polymerase (PARP) enzymes initiate (mt)DNA repair mechanisms and use nicotinamide adenine dinucleotide (NAD+) as energy source. Prolonged PARP activity can drain cellular NAD+ reserves, leading to de-regulation of important molecular processes. Here, we provide evidence of a pathophysiological mechanism that connects mtDNA damage to cardiac *For correspondence: dysfunction via reduced NAD+ levels and loss of mitochondrial function and communication. Using Knut.Huso.Lauritzen@rr-research. a transgenic model, we demonstrate that high levels of mice cardiomyocyte mtDNA damage cause no a reduction in NAD+ levels due to extreme DNA repair activity, causing impaired activation of Competing interests: The NAD+-dependent SIRT3. -
Anti-ECSIT Monoclonal Antibody (DCABH-15245) This Product Is for Research Use Only and Is Not Intended for Diagnostic Use
Anti-ECSIT monoclonal antibody (DCABH-15245) This product is for research use only and is not intended for diagnostic use. PRODUCT INFORMATION Antigen Description Adapter protein of the Toll-like and IL-1 receptor signaling pathway that is involved in the activation of NF-kappa-B via MAP3K1. Promotes proteolytic activation of MAP3K1. Involved in the BMP signaling pathway. Required for normal embryonic development (By similarity). Required for efficient assembly of mitochondrial NADH:ubiquinone oxidoreductase. Immunogen A synthetic peptide of human ECSIT is used for rabbit immunization. Isotype IgG Source/Host Rabbit Species Reactivity Human Purification Protein A Conjugate Unconjugated Applications Western Blot (Transfected lysate); ELISA Size 1 ea Buffer In 1x PBS, pH 7.4 Preservative None Storage Store at -20°C or lower. Aliquot to avoid repeated freezing and thawing. GENE INFORMATION Gene Name ECSIT ECSIT homolog (Drosophila) [ Homo sapiens ] Official Symbol ECSIT Synonyms ECSIT; ECSIT homolog (Drosophila); evolutionarily conserved signaling intermediate in Toll pathway, mitochondrial; signaling intermediate in Toll pathway evolutionarily conserved ortholog (mouse); SITPEC; likely ortholog of mouse signaling intermediate in Toll pathway evolutionarily conserved; Entrez Gene ID 51295 45-1 Ramsey Road, Shirley, NY 11967, USA Email: [email protected] Tel: 1-631-624-4882 Fax: 1-631-938-8221 1 © Creative Diagnostics All Rights Reserved Protein Refseq NP_001135936 UniProt ID Q9BQ95 Chromosome Location 19p13.2 Pathway Activated TLR4 signalling, organism-specific biosystem; Immune System, organism-specific biosystem; Innate Immune System, organism-specific biosystem; MAPK signaling pathway, organism-specific biosystem; MAPK signaling pathway, organism-specific biosystem Function oxidoreductase activity, acting on NADH or NADPH; protein binding; 45-1 Ramsey Road, Shirley, NY 11967, USA Email: [email protected] Tel: 1-631-624-4882 Fax: 1-631-938-8221 2 © Creative Diagnostics All Rights Reserved. -
Decreased Eph Receptor‑A1 Expression Is Related to Grade in Ovarian Serous Carcinoma
MOLECULAR MEDICINE REPORTS 17: 5409-5415, 2018 Decreased Eph receptor‑A1 expression is related to grade in ovarian serous carcinoma YUNFENG JIN1, YI ZOU1, LINLING WAN1, MINGMING LU1, YA LIU2, GUOQIN HUANG3, JIANDONG WANG4 and QINGHUA XI1 1Department of Obstetrics and Gynecology, Affiliated Hospital of Nantong University, Nantong, Jiangsu 226001; 2Department of Obstetrics and Gynecology, Affiliated Haian People's Hospital of Nantong University, Nantong, Jiangsu 226600; 3Department of Obstetrics and Gynecology, Affiliated Maternal and Child Health Care Hospital of Nantong University, Nantong, Jiangsu 226018; 4Department of Pathology, Jinling Hospital, Nanjing University School of Medicine, Nanjing, Jiangsu 210002, P.R. China Received June 28, 2017; Accepted October 9, 2017 DOI: 10.3892/mmr.2018.8528 Abstract. Eph receptor‑A1 (EphA1) was the first member of 100%) and ovarian benign serous cystadenomas (12/12, 100%) the erythropoietin producing hepatocellular carcinoma (Eph) as well as in some borderline serous tumors (9/15, 60%) and family of receptor tyrosine kinases. Although the roles of ovarian serous carcinomas (33/76, 43.42%). EphA1 expression EphA1 in the tumorigenesis of various human cancers have was associated with grade of ovarian serous carcinomas, with been investigated, few studies have focused on ovarian carci- loss of EphA1 more often observed in high‑grade tumors noma. The present study aimed to explore the profile of EphA1 (P=0.016) and high Ki67 index tumors (P=0.007). These data expression in ovarian carcinomas, to analyzed the association suggest that EphA1 might be a useful marker for distinguishing between EphA1 expression and clinicopathologic parameters, low grade from high‑grade ovarian serous carcinoma.