Table S1. 103 Ferroptosis-Related Genes Retrieved from the Genecards
Total Page:16
File Type:pdf, Size:1020Kb
Load more
Recommended publications
-
Acteoside from Ligustrum Robustum (Roxb.) Blume Ameliorates Lipid Metabolism and Synthesis in a Hepg2 Cell Model of Lipid Accumulation
ORIGINAL RESEARCH published: 24 May 2019 doi: 10.3389/fphar.2019.00602 Acteoside From Ligustrum robustum (Roxb.) Blume Ameliorates Lipid Metabolism and Synthesis in a HepG2 Cell Model of Lipid Accumulation Le Sun 1,2†, Fan Yu 1,2†, Fan Yi 3, Lijia Xu 1,2*, Baoping Jiang 1,2*, Liang Le 1,2 and Peigen Xiao 1,2 1 Institute of Medicinal Plant Development, Chinese Academy of Medical Sciences, Peking Union Medical College, Beijing, China, 2 Key Laboratory of Bioactive Substances and Resources Utilization of Chinese Herbal Medicine, Ministry of Education, Beijing, China, 3 Key Laboratory of Cosmetics, China National Light Industry, Beijing Technology and Business Edited by: University, Beijing, China Min Ye, Peking University, China We aimed to ascertain the mechanism underlying the effects of acteoside (ACT) from Reviewer: Wei Song, Ligustrum robustum (Roxb.) Blume (Oleaceae) on lipid metabolism and synthesis. ACT, Peking Union Medical College a water-soluble phenylpropanoid glycoside, is the most abundant and major active Hospital (CAMS), component of L. robustum; the leaves of L. robustum, known as kudingcha (bitter tea), China Shuai Ji, have long been used in China as an herbal tea for weight loss. Recently, based on previous Xuzhou Medical University, studies, our team reached a preliminary conclusion that phenylpropanoid glycosides from China L. robustum most likely contribute substantially to reducing lipid levels, but the mechanism *Correspondence: Lijia Xu remains unclear. Here, we conducted an in silico screen of currently known phenylethanoid [email protected] glycosides from L. robustum and attempted to explore the hypolipidemic mechanism of Baoping Jiang ACT, the representative component of phenylethanoid glycosides in L. -
Cell Death Via Lipid Peroxidation and Protein Aggregation Diseases
biology Review Cell Death via Lipid Peroxidation and Protein Aggregation Diseases Katsuya Iuchi * , Tomoka Takai and Hisashi Hisatomi Department of Materials and Life Science, Faculty of Science and Technology, Seikei University, 3-3-1 Kichijojikitamachi, Musashino-shi, Tokyo 180-8633, Japan; [email protected] (T.T.); [email protected] (H.H.) * Correspondence: [email protected] or [email protected]; Tel.: +81-422-37-3523 Simple Summary: It is essential for cellular homeostasis that biomolecules, such as DNA, proteins, and lipids, function properly. Disturbance of redox homeostasis produces aberrant biomolecules, including oxidized lipids and misfolded proteins, which increase in cells. Aberrant biomolecules are removed by excellent cellular clearance systems. However, when excess aberrant biomolecules remain in the cell, they disrupt organelle and cellular functions, leading to cell death. These aberrant molecules aggregate and cause apoptotic and non-apoptotic cell death, leading to various protein aggregation diseases. Thus, we investigated the cell-death cross-linking between lipid peroxidation and protein aggregation. Abstract: Lipid peroxidation of cellular membranes is a complicated cellular event, and it is both the cause and result of various diseases, such as ischemia-reperfusion injury, neurodegenerative diseases, and atherosclerosis. Lipid peroxidation causes non-apoptotic cell death, which is associated with cell fate determination: survival or cell death. During the radical chain reaction of lipid peroxidation, Citation: Iuchi, K.; Takai, T.; various oxidized lipid products accumulate in cells, followed by organelle dysfunction and the Hisatomi, H. Cell Death via Lipid induction of non-apoptotic cell death. Highly reactive oxidized products from unsaturated fatty acids Peroxidation and Protein are detected under pathological conditions. -
Implications in Parkinson's Disease
Journal of Clinical Medicine Review Lysosomal Ceramide Metabolism Disorders: Implications in Parkinson’s Disease Silvia Paciotti 1,2 , Elisabetta Albi 3 , Lucilla Parnetti 1 and Tommaso Beccari 3,* 1 Laboratory of Clinical Neurochemistry, Department of Medicine, University of Perugia, Sant’Andrea delle Fratte, 06132 Perugia, Italy; [email protected] (S.P.); [email protected] (L.P.) 2 Section of Physiology and Biochemistry, Department of Experimental Medicine, University of Perugia, Sant’Andrea delle Fratte, 06132 Perugia, Italy 3 Department of Pharmaceutical Sciences, University of Perugia, Via Fabretti, 06123 Perugia, Italy; [email protected] * Correspondence: [email protected] Received: 29 January 2020; Accepted: 20 February 2020; Published: 21 February 2020 Abstract: Ceramides are a family of bioactive lipids belonging to the class of sphingolipids. Sphingolipidoses are a group of inherited genetic diseases characterized by the unmetabolized sphingolipids and the consequent reduction of ceramide pool in lysosomes. Sphingolipidoses include several disorders as Sandhoff disease, Fabry disease, Gaucher disease, metachromatic leukodystrophy, Krabbe disease, Niemann Pick disease, Farber disease, and GM2 gangliosidosis. In sphingolipidosis, lysosomal lipid storage occurs in both the central nervous system and visceral tissues, and central nervous system pathology is a common hallmark for all of them. Parkinson’s disease, the most common neurodegenerative movement disorder, is characterized by the accumulation and aggregation of misfolded α-synuclein that seem associated to some lysosomal disorders, in particular Gaucher disease. This review provides evidence into the role of ceramide metabolism in the pathophysiology of lysosomes, highlighting the more recent findings on its involvement in Parkinson’s disease. Keywords: ceramide metabolism; Parkinson’s disease; α-synuclein; GBA; GLA; HEX A-B; GALC; ASAH1; SMPD1; ARSA * Correspondence [email protected] 1. -
ACAT) in Cholesterol Metabolism: from Its Discovery to Clinical Trials and the Genomics Era
H OH metabolites OH Review Acyl-Coenzyme A: Cholesterol Acyltransferase (ACAT) in Cholesterol Metabolism: From Its Discovery to Clinical Trials and the Genomics Era Qimin Hai and Jonathan D. Smith * Department of Cardiovascular & Metabolic Sciences, Cleveland Clinic, Cleveland, OH 44195, USA; [email protected] * Correspondence: [email protected]; Tel.: +1-216-444-2248 Abstract: The purification and cloning of the acyl-coenzyme A: cholesterol acyltransferase (ACAT) enzymes and the sterol O-acyltransferase (SOAT) genes has opened new areas of interest in cholesterol metabolism given their profound effects on foam cell biology and intestinal lipid absorption. The generation of mouse models deficient in Soat1 or Soat2 confirmed the importance of their gene products on cholesterol esterification and lipoprotein physiology. Although these studies supported clinical trials which used non-selective ACAT inhibitors, these trials did not report benefits, and one showed an increased risk. Early genetic studies have implicated common variants in both genes with human traits, including lipoprotein levels, coronary artery disease, and Alzheimer’s disease; however, modern genome-wide association studies have not replicated these associations. In contrast, the common SOAT1 variants are most reproducibly associated with testosterone levels. Keywords: cholesterol esterification; atherosclerosis; ACAT; SOAT; inhibitors; clinical trial Citation: Hai, Q.; Smith, J.D. Acyl-Coenzyme A: Cholesterol Acyltransferase (ACAT) in Cholesterol Metabolism: From Its 1. Introduction Discovery to Clinical Trials and the The acyl-coenzyme A:cholesterol acyltransferase (ACAT; EC 2.3.1.26) enzyme family Genomics Era. Metabolites 2021, 11, consists of membrane-spanning proteins, which are primarily located in the endoplasmic 543. https://doi.org/10.3390/ reticulum [1]. -
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. -
ABCC12 Monoclonal Antibody, Clone M9II-3
ABCC12 monoclonal antibody, Gene Symbol: ABCC12 clone M9II-3 Gene Alias: MGC27071, MRP9 Catalog Number: MAB6675 Gene Summary: This gene is a member of the superfamily of ATP-binding cassette (ABC) transporters Regulatory Status: For research use only (RUO) and the encoded protein contains two ATP-binding domains and 12 transmembrane regions. ABC proteins Product Description: Rat monoclonal antibody raised transport various molecules across extra- and against partial recombinant ABCC12. intracellular membranes. ABC genes are divided into Clone Name: M9II-3 seven distinct subfamilies: ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, and White. This gene is a member of Immunogen: Recombinant protein corresponding to the MRP subfamily which is involved in multi-drug amino acids 690-734 of human ABCC12. resistance. This gene and another subfamily member are arranged head-to-tail on chromosome 16q12.1. Host: Rat Increased expression of this gene is associated with breast cancer. [provided by RefSeq] Reactivity: Human References: Applications: ICC, IHC-Fr, WB 1. Multidrug resistance-associated protein 9 (ABCC12) is (See our web site product page for detailed applications present in mouse and boar sperm. Ono N, Van der information) Heijden I, Scheffer GL, Van de Wetering K, Van Deemter E, De Haas M, Boerke A, Gadella BM, De Rooij Protocols: See our web site at DG, Neefjes JJ, Groothuis TA, Oomen L, Brocks L, http://www.abnova.com/support/protocols.asp or product Ishikawa T, Borst P. Ono N, Van der Heijden I, Scheffer page for detailed protocols GL, Van de Wetering K, Van Deemter E, De Haas M, Boerke A, Gadella BM, De Rooij DG, Neefjes JJ, Specificity: M9II-3 reacts with an internal epitope of Groothuis TA, Oomen L, Brocks L, Ishikawa T, Borst P. -
Loss of Fam60a, a Sin3a Subunit, Results in Embryonic Lethality and Is Associated with Aberrant Methylation at a Subset of Gene
RESEARCH ARTICLE Loss of Fam60a, a Sin3a subunit, results in embryonic lethality and is associated with aberrant methylation at a subset of gene promoters Ryo Nabeshima1,2, Osamu Nishimura3,4, Takako Maeda1, Natsumi Shimizu2, Takahiro Ide2, Kenta Yashiro1†, Yasuo Sakai1, Chikara Meno1, Mitsutaka Kadota3,4, Hidetaka Shiratori1†, Shigehiro Kuraku3,4*, Hiroshi Hamada1,2* 1Developmental Genetics Group, Graduate School of Frontier Biosciences, Osaka University, Suita, Japan; 2Laboratory for Organismal Patterning, RIKEN Center for Developmental Biology, Kobe, Japan; 3Phyloinformatics Unit, RIKEN Center for Life Science Technologies, Kobe, Japan; 4Laboratory for Phyloinformatics, RIKEN Center for Biosystems Dynamics Research, Kobe, Japan Abstract We have examined the role of Fam60a, a gene highly expressed in embryonic stem cells, in mouse development. Fam60a interacts with components of the Sin3a-Hdac transcriptional corepressor complex, and most Fam60a–/– embryos manifest hypoplasia of visceral organs and die in utero. Fam60a is recruited to the promoter regions of a subset of genes, with the expression of these genes being either up- or down-regulated in Fam60a–/– embryos. The DNA methylation level of the Fam60a target gene Adhfe1 is maintained at embryonic day (E) 7.5 but markedly reduced at –/– *For correspondence: E9.5 in Fam60a embryos, suggesting that DNA demethylation is enhanced in the mutant. [email protected] (SK); Examination of genome-wide DNA methylation identified several differentially methylated regions, [email protected] (HH) which were preferentially hypomethylated, in Fam60a–/– embryos. Our data suggest that Fam60a is †These authors contributed required for proper embryogenesis, at least in part as a result of its regulation of DNA methylation equally to this work at specific gene promoters. -
Mergeomics: Multidimensional Data Integration to Identify Pathogenic Perturbations to Biological Systems
Shu et al. BMC Genomics (2016) 17:874 DOI 10.1186/s12864-016-3198-9 METHODOLOGY ARTICLE Open Access Mergeomics: multidimensional data integration to identify pathogenic perturbations to biological systems Le Shu1, Yuqi Zhao1, Zeyneb Kurt1, Sean Geoffrey Byars2,3, Taru Tukiainen4, Johannes Kettunen4, Luz D. Orozco5, Matteo Pellegrini5, Aldons J. Lusis6, Samuli Ripatti4, Bin Zhang7, Michael Inouye2,3,8, Ville-Petteri Mäkinen1,9,10,11* and Xia Yang1,12* Abstract Background: Complex diseases are characterized by multiple subtle perturbations to biological processes. New omics platforms can detect these perturbations, but translating the diverse molecular and statistical information into testable mechanistic hypotheses is challenging. Therefore, we set out to create a public tool that integrates these data across multiple datasets, platforms, study designs and species in order to detect the most promising targets for further mechanistic studies. Results: We developed Mergeomics, a computational pipeline consisting of independent modules that 1) leverage multi-omics association data to identify biological processes that are perturbed in disease, and 2) overlay the disease- associated processes onto molecular interaction networks to pinpoint hubs as potential key regulators. Unlike existing tools that are mostly dedicated to specific data type or settings, the Mergeomics pipeline accepts and integrates datasets across platforms, data types and species. We optimized and evaluated the performance of Mergeomics using simulation and multiple independent datasets, and benchmarked the results against alternative methods. We also demonstrate the versatility of Mergeomics in two case studies that include genome-wide, epigenome-wide and transcriptome-wide datasets from human and mouse studies of total cholesterol and fasting glucose. -
Download Author Version (PDF)
Molecular BioSystems Accepted Manuscript This is an Accepted Manuscript, which has been through the Royal Society of Chemistry peer review process and has been accepted for publication. Accepted Manuscripts are published online shortly after acceptance, before technical editing, formatting and proof reading. Using this free service, authors can make their results available to the community, in citable form, before we publish the edited article. We will replace this Accepted Manuscript with the edited and formatted Advance Article as soon as it is available. You can find more information about Accepted Manuscripts in the Information for Authors. Please note that technical editing may introduce minor changes to the text and/or graphics, which may alter content. The journal’s standard Terms & Conditions and the Ethical guidelines still apply. In no event shall the Royal Society of Chemistry be held responsible for any errors or omissions in this Accepted Manuscript or any consequences arising from the use of any information it contains. www.rsc.org/molecularbiosystems Page 1 of 29 Molecular BioSystems Mutated Genes and Driver Pathways Involved in Myelodysplastic Syndromes—A Transcriptome Sequencing Based Approach Liang Liu1*, Hongyan Wang1*, Jianguo Wen2*, Chih-En Tseng2,3*, Youli Zu2, Chung-che Chang4§, Xiaobo Zhou1§ 1 Center for Bioinformatics and Systems Biology, Division of Radiologic Sciences, Wake Forest University Baptist Medical Center, Winston-Salem, NC 27157, USA. 2 Department of Pathology, the Methodist Hospital Research Institute, -
Usbiological Datasheet
ABI2 (ABI-2, ABI2B, AblBP3, AIP-1, argBPIA, SSH3BP2, ARGBPIA, Abl interactor 2) Catalog number 144114 Supplier United States Biological ABI2 (ABL Interactor 2), is a protein that in humans is encoded by the ABI2 gene. By analysis of a YAC and a BAC, Machado et al. (2000) mapped the ABI2 gene to 2q31-q33. ABI2 possesses a basic N terminus with homology to a homeodomain protein; a central serine-rich region; 3 PEST sequences, which are implicated in susceptibility to protein degradation; several proline-rich stretches; and an acidic C terminus with multiple phosphorylation sites and an SH3 domain. Dai and Pendergast (1995) suggested that the ABI proteins may function to coordinate the cytoplasmic and nuclear functions of the ABL1 tyrosine kinase. UniProt Number Q9NYB9 Gene ID ABI2 Applications Suitable for use in Western Blot. Recommended Dilution Optimal dilutions to be determined by the researcher. Storage and Handling Store at -20˚C for one year. After reconstitution, store at 4˚C for one month. Can also be aliquoted and stored frozen at -20˚C for long term. Avoid repeated freezing and thawing. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Immunogen A synthetic peptide corresponding to a sequence at the N-terminal of human ABI2, identical to the related mouse and rat sequences. Formulation Supplied as a lyophilized powder. Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg Thimerosal, 0.05mg NaN3. Reconstitution: Add 0.2ml of distilled water will yield a concentration of 500ug/ml. -
DYSREGULATION of LONG-CHAIN ACYL-Coa SYNTHETASES in CANCER and THEIR TARGETING STRATEGIES in ANTICANCER THERAPY Md Amir Hossain1, Jun Ma2, Yong Yang1 1
Hossain et al RJLBPCS 2020 www.rjlbpcs.com Life Science Informatics Publications Original Review Article DOI: 10.26479/2020.0603.06 DYSREGULATION OF LONG-CHAIN ACYL-CoA SYNTHETASES IN CANCER AND THEIR TARGETING STRATEGIES IN ANTICANCER THERAPY Md Amir Hossain1, Jun Ma2, Yong Yang1 1. Academic Institute of Pharmaceutical Science, China Pharmaceutical University, Nanjing, China. 2. Ningxia Baoshihua Hospital, Ningxia, China. ABSTRACT: Cancer is a leading cause of death worldwide, and the number of cases globally continues to increase. Cancer is caused by certain changes in genes that are involved in controlling cell functions and cell division. Notably, metabolic dysregulation is one the hallmarks of cancer, and increases in fatty acid metabolism have been demonstrated to promote the growth and survival of a variety of cancers. In human, fatty acids either can be breakdown into acetyl-CoA through catabolic metabolism and aid in ATP generation or in the anabolic metabolism they can incorporate into triacylglycerol and phospholipid. Importantly, both of these pathways need activation of fatty acids, and the key players in this activation of fatty acids are the long-chain acyl-CoA synthetases (ACSLs) that are commonly dysregulated in cancer and associated with oncogenesis and survival. Therefore, it provides a rationale to target ACSLs in cancer. This review summarizes the current understanding of long-chain acyl-CoA synthetases in cancer and their targeting opportunities. KEYWORDS: Acyl-CoA synthetases, cancer, fatty acid, lipid metabolism. Article History: Received: April 15, 2020; Revised: May 10, 2020; Accepted: May 30, 2020. Corresponding Author: Prof. Yong Yang* Academic Institute of Pharmaceutical Science, China Pharmaceutical University, Nanjing, China. -
Supplementary Materials
Supplementary materials Supplementary Table S1: MGNC compound library Ingredien Molecule Caco- Mol ID MW AlogP OB (%) BBB DL FASA- HL t Name Name 2 shengdi MOL012254 campesterol 400.8 7.63 37.58 1.34 0.98 0.7 0.21 20.2 shengdi MOL000519 coniferin 314.4 3.16 31.11 0.42 -0.2 0.3 0.27 74.6 beta- shengdi MOL000359 414.8 8.08 36.91 1.32 0.99 0.8 0.23 20.2 sitosterol pachymic shengdi MOL000289 528.9 6.54 33.63 0.1 -0.6 0.8 0 9.27 acid Poricoic acid shengdi MOL000291 484.7 5.64 30.52 -0.08 -0.9 0.8 0 8.67 B Chrysanthem shengdi MOL004492 585 8.24 38.72 0.51 -1 0.6 0.3 17.5 axanthin 20- shengdi MOL011455 Hexadecano 418.6 1.91 32.7 -0.24 -0.4 0.7 0.29 104 ylingenol huanglian MOL001454 berberine 336.4 3.45 36.86 1.24 0.57 0.8 0.19 6.57 huanglian MOL013352 Obacunone 454.6 2.68 43.29 0.01 -0.4 0.8 0.31 -13 huanglian MOL002894 berberrubine 322.4 3.2 35.74 1.07 0.17 0.7 0.24 6.46 huanglian MOL002897 epiberberine 336.4 3.45 43.09 1.17 0.4 0.8 0.19 6.1 huanglian MOL002903 (R)-Canadine 339.4 3.4 55.37 1.04 0.57 0.8 0.2 6.41 huanglian MOL002904 Berlambine 351.4 2.49 36.68 0.97 0.17 0.8 0.28 7.33 Corchorosid huanglian MOL002907 404.6 1.34 105 -0.91 -1.3 0.8 0.29 6.68 e A_qt Magnogrand huanglian MOL000622 266.4 1.18 63.71 0.02 -0.2 0.2 0.3 3.17 iolide huanglian MOL000762 Palmidin A 510.5 4.52 35.36 -0.38 -1.5 0.7 0.39 33.2 huanglian MOL000785 palmatine 352.4 3.65 64.6 1.33 0.37 0.7 0.13 2.25 huanglian MOL000098 quercetin 302.3 1.5 46.43 0.05 -0.8 0.3 0.38 14.4 huanglian MOL001458 coptisine 320.3 3.25 30.67 1.21 0.32 0.9 0.26 9.33 huanglian MOL002668 Worenine