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Datasheet Version: 2.0.0 Revision date: 12 Nov 2020 Human Acetyl-coenzyme A synthetase, cytoplasmic (ACSS2) ELISA Kit Catalogue No.:abx500866 For the in vitro quantitative measurement of Human Acetyl-coenzyme A synthetase, cytoplasmic (ACSS2) concentrations in tissue homogenates, cell lysates and other biological fluids. Target: Acetyl-coenzyme A synthetase, cytoplasmic (ACSS2) Reactivity: Human Tested Applications: ELISA Recommended dilutions: Optimal dilutions/concentrations should be determined by the end user. Storage: Shipped at 4 °C. Upon receipt, store the kit according to the storage instruction in the kit's manual. Validity: The validity for this kit is 6 months. Stability: The stability of the kit is determined by the rate of activity loss. The loss rate is less than 5% within the expiration date under appropriate storage conditions. To minimize performance fluctuations, operation procedures and lab conditions should be strictly controlled. It is also strongly suggested that the whole assay is performed by the same user throughout. UniProt Primary AC: Q9NR19 (UniProt, ExPASy) Gene Symbol: ForACSS2 Reference Only KEGG: hsa:55902 Test Range: 0.78 ng/ml - 50 ng/ml Sensitivity: < 0.38 ng/ml Standard Form: Lyophilized v1.0.0 Abbexa Ltd, Cambridge, UK · Phone: +44 1223 755950 · Fax: +44 1223 755951 1 Abbexa LLC, Houston, TX, USA · Phone: +1 832 327 7413 www.abbexa.com · Email: [email protected] Datasheet Version: 2.0.0 Revision date: 12 Nov 2020 ELISA Detection: Colorimetric ELISA Data: Quantitative Sample Type: Tissue homogenates, cell lysates and other biological fluids. Note: This product is for research use only. The range and sensitivity is subject to change. Please contact us for the latest product information. For accurate results, sample concentrations must be diluted to mid-range of the kit. If you require a specific range, please contact us in advance or write your request in your order comments. Please note that our ELISA and CLIA kits are optimised for detection of native samples, rather than recombinant proteins. We are unable to guarantee detection of recombinant proteins, as they may have different sequences or tertiary structures to the native protein. For Reference Only v1.0.0 Abbexa Ltd, Cambridge, UK · Phone: +44 1223 755950 · Fax: +44 1223 755951 2 Abbexa LLC, Houston, TX, USA · Phone: +1 832 327 7413 www.abbexa.com · Email: [email protected].

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Acetyl-Coa Synthetase 3 Promotes Bladder Cancer Cell Growth Under Metabolic Stress Jianhao Zhang1, Hongjian Duan1, Zhipeng Feng1,Xinweihan1 and Chaohui Gu2
Zhang et al. Oncogenesis (2020) 9:46 https://doi.org/10.1038/s41389-020-0230-3 Oncogenesis ARTICLE Open Access Acetyl-CoA synthetase 3 promotes bladder cancer cell growth under metabolic stress Jianhao Zhang1, Hongjian Duan1, Zhipeng Feng1,XinweiHan1 and Chaohui Gu2 Abstract Cancer cells adapt to nutrient-deprived tumor microenvironment during progression via regulating the level and function of metabolic enzymes. Acetyl-coenzyme A (AcCoA) is a key metabolic intermediate that is crucial for cancer cell metabolism, especially under metabolic stress. It is of special signiﬁcance to decipher the role acetyl-CoA synthetase short chain family (ACSS) in cancer cells confronting metabolic stress. Here we analyzed the generation of lipogenic AcCoA in bladder cancer cells under metabolic stress and found that in bladder urothelial carcinoma (BLCA) cells, the proportion of lipogenic AcCoA generated from glucose were largely reduced under metabolic stress. Our results revealed that ACSS3 was responsible for lipogenic AcCoA synthesis in BLCA cells under metabolic stress. Interestingly, we found that ACSS3 was required for acetate utilization and histone acetylation. Moreover, our data illustrated that ACSS3 promoted BLCA cell growth. In addition, through analyzing clinical samples, we found that both mRNA and protein levels of ACSS3 were dramatically upregulated in BLCA samples in comparison with adjacent controls and BLCA patients with lower ACSS3 expression were entitled with longer overall survival. Our data revealed an oncogenic role of ACSS3 via regulating AcCoA generation in BLCA and provided a promising target in metabolic pathway for BLCA treatment. 1234567890():,; 1234567890():,; 1234567890():,; 1234567890():,; Introduction acetyl-CoA synthetase short chain family (ACSS), which In cancer cells, considerable number of metabolic ligates acetate and CoA6.
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Metabolic Intermediates in Tumorigenesis and Progression Yuchen He 1,2,3*, Menghui Gao1,2,3*, Haosheng Tang1,2,3, Yiqu Cao1,2,3, Shuang Liu4, Yongguang Tao1,2,3
Int. J. Biol. Sci. 2019, Vol. 15 1187 Ivyspring International Publisher International Journal of Biological Sciences 2019; 15(6): 1187- 1199. doi: 10.7150/ijbs.33496 Review Metabolic Intermediates in Tumorigenesis and Progression Yuchen He 1,2,3*, Menghui Gao1,2,3*, Haosheng Tang1,2,3, Yiqu Cao1,2,3, Shuang Liu4, Yongguang Tao1,2,3 1. Key Laboratory of Carcinogenesis and Cancer Invasion, Ministry of Education, Xiangya Hospital, Central South University, 87 Xiangya Road, Changsha, Hunan, 410008 China 2. Cancer Research Institute, Key Laboratory of Carcinogenesis, Ministry of Health, School of Basic Medicine, Central South University, 110 Xiangya Road, Changsha, Hunan, 410078 China 3. Department of Thoracic Surgery, Second Xiangya Hospital, Central South University, Changsha, China 4. Institute of Medical Sciences, Xiangya Hospital, Central South University, 87 Xiangya Road, Changsha, Hunan, 410008 China *Equal contribution Corresponding authors: Liu, S. Email: [email protected]; Tao, YG. Email: [email protected]; Tel. +(86) 731-84805448; Fax. +(86) 731-84470589. © Ivyspring International Publisher. This is an open access article distributed under the terms of the Creative Commons Attribution (CC BY-NC) license (https://creativecommons.org/licenses/by-nc/4.0/). See http://ivyspring.com/terms for full terms and conditions. Received: 2019.01.25; Accepted: 2019.03.18; Published: 2019.05.07 Abstract Traditional antitumor drugs inhibit the proliferation and metastasis of tumour cells by restraining the replication and expression of DNA. These drugs are usually highly cytotoxic. They kill tumour cells while also cause damage to normal cells at the same time, especially the hematopoietic cells that divide vigorously.
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Identification of Expression Qtls Targeting Candidate Genes For
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The British Journal of Psychiatry (2016) 208, 128–137. doi: 10.1192/bjp.bp.114.156976 Impact of a cis-associated gene expression SNP on chromosome 20q11.22 on bipolar disorder susceptibility, hippocampal structure and cognitive performance Ming Li,* Xiong-jian Luo,* Mikael Lande´ n, Sarah E. Bergen, Christina M. Hultman, Xiao Li, Wen Zhang, Yong-Gang Yao, Chen Zhang, Jiewei Liu, Manuel Mattheisen, Sven Cichon, Thomas W. Mu¨ hleisen, Franziska A. Degenhardt, Markus M. No¨ then, Thomas G. Schulze, Maria Grigoroiu-Serbanescu, Hao Li, Chris K. Fuller, Chunhui Chen, Qi Dong, Chuansheng Chen, Ste´ phane Jamain, Marion Leboyer, Frank Bellivier, Bruno Etain, Jean-Pierre Kahn, Chantal Henry, Martin Preisig, Zolta´ n Kutalik, Enrique Castelao, Adam Wright, Philip B. Mitchell, Janice M. Fullerton, Peter R. Schofield, Grant W. Montgomery, Sarah E. Medland, Scott D. Gordon, Nicholas G. Martin, MooDS Consortium,a The Swedish Bipolar Study Group,a Marcella Rietschel, Chunyu Liu, Joel E. Kleinman, Thomas M. Hyde, Daniel R. Weinberger and Bing Su Background Bipolar disorder is a highly heritable polygenic disorder. between a brain eQTL rs6088662 on chromosome 20q11.22 Recent enrichment analyses suggest that there may and bipolar disorder (log Bayes factor = 5.48; bipolar disorder be true risk variants for bipolar disorder in the expression P = 5.8561075). Follow-up studies across multiple quantitative trait loci (eQTL) in the brain. independent samples confirmed the association of the risk SNP (rs6088662) with gene expression and bipolar Aims disorder susceptibility (P = 3.5461078). Further exploratory We sought to assess the impact of eQTL variants on bipolar analysis revealed that rs6088662 is also associated with disorder risk by combining data from both bipolar disorder hippocampal volume and cognitive performance in healthy genome-wide association studies (GWAS) and brain eQTL.
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SAN TA C RUZ BI OTEC HNOL OG Y, INC . ACSS1 (N-20): sc-85255 BACKGROUND PRODUCT ACSS1 (acyl-CoA synthetase short-chain family member 1), also known as Each vial contains 100 µg IgG in 1.0 ml of PBS with < 0.1% sodium azide ACAS2L or AceCS2L, is a 689 amino acid protein that localizes to the mito - and 0.1% gelatin. chondrial matrix and belongs to the ATP-dependent AMP-binding enzyme Blocking peptide available for competition studies, sc-85255 P, (100 µg family. Functioning primarily as a cardiac enzyme, ACSS1 catalyzes the ATP- pep tide in 0.5 ml PBS containing < 0.1% sodium azide and 0.2% BSA). dependent conversion of acetate and CoA (coenzyme A) to acetyl-CoA, which is then utilized for the oxidation of acetate within the tricarboxylic acid cycle . APPLICATIONS ACSS1 is expressed as two alternatively spliced isoforms and is encoded by a gene which maps to chromosome 20. Comprising approximately 2% of the ACSS1 (N-20) is recommended for detection of ACSS1 of mouse, rat and human genome, chromosome 20 contains nearly 63 million bases that encode human origin by Western Blotting (starting dilution 1:200, dilution range over 600 genes, some of which are associated with Creutzfeldt-Jakob disease , 1:100-1:1000), immunoprecipitation [1-2 µg per 100-500 µg of total protein amyotrophic lateral sclerosis, spinal muscular atrophy, ring chromosome 20 (1 ml of cell lysate)], immunofluorescence (starting dilution 1:50, dilution epilepsy syndrome and Alagille syndrome. range 1:50-1:500) and solid phase ELISA (starting dilution 1:30, dilution range 1:30-1:3000); non cross-reactive with ACSS2.
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Title of Dissertation Goes Here in All Caps
METABOLIC REGULATION OF PROTEIN PHOSPHORYLATION AND ACETYLATION APPROVED BY SUPERVISORY COMMITTEE Benjamin P. Tu, Ph.D. Jennifer J. Kohler, Ph.D. Deepak Nijhawan, M.D., Ph.D. Hongtao Yu, Ph.D. DEDICATION To my parents for their love and support. To my mentor and committee members for their guidance. i METABOLIC REGULATION OF PROTEIN PHOSPHORYLATION AND ACETYLATION by MENGLU ZHANG DISSERTATION Presented to the Faculty of the Graduate School of Biomedical Sciences The University of Texas Southwestern Medical Center at Dallas In Partial Fulfillment of the Requirements For the Degree of DOCTOR OF PHILOSOPHY The University of Texas Southwestern Medical Center at Dallas Dallas, Texas August, 2018 ii Copyright by Menglu Zhang, 2018 All Rights Reserved iii METABOLIC REGULATION OF PROTEIN PHOSPHORYLATION AND ACETYLATION Menglu Zhang The University of Texas Southwestern Medical Center at Dallas, 2018 Supervising Professor: Benjamin P. Tu, Ph.D. Celluar metabolism can influence phosphorylation and acetylation modifications on proteins as part of an intricate network of cellular and organismal regulation. We have investigated one molecular mechanism through which protein phosphorylation and acetylation can be regulated based on metabolic status and how metabolic enzymes are regulated by nutrient availability. In the first part of this study, we report that a simple enzyme involved in acetate utilization, Acetyl-CoA synthetase 2 (ACSS2), promotes systemic fat storage and utilization through selective regulation of genes involved in lipid metabolism. We reveal that mice vii lacking ACSS2 exhibit a significant reduction in body weight and hepatic steatosis in a diet- induced obesity model. ACSS2 deficiency reduces dietary lipid absorption by the intestine, and perturbs repartitioning and utilization of triglycerides from adipose tissue to the liver due to lowered expression of lipid transporters and fatty acid oxidation genes.
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Supplementary Information
SUPPLEMENTARY INFORMATION 1. SUPPLEMENTARY FIGURE LEGENDS Supplementary Figure 1. Long-term exposure to sorafenib increases the expression of progenitor cell-like features. A) mRNA expression levels of PROM-1 (CD133), THY-1 (CD90), EpCAM, KRT19, and VIM assessed by quantitative real-time PCR. Data represent the mean expression value for a gene in each phenotypic type of cells, displayed as fold-changes normalized to 1 (expression value of its corresponding parental non-treated cell line). Expression level is relative to the GAPDH gene. Bars indicate standard deviation. Significant statistical differences are set at p<0.05. B) Immunocitochemical staining of CD90 and vimentin in Hep3B sorafenib resistant cell line and its parental cell line. C) Western blot analysis comparing protein levels in resistant Hu6 and Hep3B cells vs their corresponding parental cells lines. Supplementary Figure 2. Efficacy of gene silencing of IGF1R and FGFR1 and evaluation of MAPK14 signaling activation. IGF1R and FGFR1 knockdown expression 48h after transient transfection with siRNAs (50 nM), in non-treated parental cells and sorafenib-acquired resistant tumor derived cells was assessed by quantitative RT-PCR (A) and western blot (B). C) Activation status of MAPK14 signaling was evaluated by western blot analysis in vivo, in tumors with acquired resistance to sorafenib in comparison to non-treated tumors (right panel), as well as in in vitro, in sorafenib resistant cell lines vs parental non-treated. Supplementary Figure 3. Gene expression levels of several pro-angiogenic factors. mRNA expression levels of FGF1, FGF2, VEGFA, IL8, ANGPT2, KDR, FGFR3, FGFR4 assessed by quantitative real-time PCR in tumors harvested from mice.
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Supplemental Material
Supplemental Material Acute TNF-induced repression of cell identity genes is mediated by NFκB-directed redistribution of cofactors from super-enhancers Søren Fisker Schmidt,1,3 Bjørk Ditlev Larsen,1,3 Anne Loft,1 Ronni Nielsen,1 Jesper Grud Skat Madsen,1,2 and Susanne Mandrup1 1 University of Southern Denmark, Department of Biochemistry and Molecular Biology, Campusvej 55, 5230 Odense M, Denmark; 2 The Novo Nordisk Foundation Center for Basic Metabolic Research, University of Copenhagen, DK-2200 Copenhagen, Denmark. 3 Equal contribution Corresponding author: Susanne Mandrup ([email protected]) Content of Supplemental Material Supplemental Figures and Tables Figures Related to Figure S1 Figure 1 Figure S2 Figure 2 Figure S3 Figure 3 Figure S4 Figure 4 Figure S5 Figure 5 Figure S6 Figure 6 Tables Related to Table S1 Figure 1 Table S2 Figure S1, Figure 2, and Figure S2 Table S3 Figure S4 and Figure 6 Supplemental Methods Supplemental References Fig. S1 A B TNF time course TNF dosis response 1.2 1.2 IL1A 1.5hrs PPARG mature * IL1A 1.2 PPARG mature 24hrs * 1.4 TNF 1.5hrs 1 PPARG nascent 1 TNF PPARG nascent 1.5hrs * * * * * 1.0 1.2 * * * * 0.8 * 0.8 1.0 * 0.8 * **** 0.8 0.6 0.6 0.6 * * 0.6 0.4 * * 0.4 0.4 * * * 0.4 * * Relative expresion Relative expresion Relative expresion 0.2 Relative expresion 0.2 * 0.2 0.2 * 0 0 0.0 0.0 0 31.5 6 12 24 0 31.5 6 12 24 0 0.1 1 10 100 0 0.1 1 10 100 Hours Hours TNF Conc.
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Role of Acetyl-Coa Synthetase 2 and Acetyl-Coa Precursors, Acetate and Ethanol, on Hepatocyte Gene Expression
University of Nebraska - Lincoln DigitalCommons@University of Nebraska - Lincoln UCARE: Undergraduate Creative Activities & UCARE Research Products Research Experiences Spring 2016 Role of Acetyl-CoA Synthetase 2 and Acetyl-CoA Precursors, Acetate and Ethanol, on Hepatocyte Gene Expression Noel Bruner University of Nebraska - Lincoln, [email protected] Anjeza Erickson, University of Nebraska-Lincoln Mengna Xia University of Nebraska-Lincoln Bo He University of Nebraska-Lincoln Regis Moreau University of Nebraska–Lincoln, [email protected] Follow this and additional works at: https://digitalcommons.unl.edu/ucareresearch Part of the Molecular, Genetic, and Biochemical Nutrition Commons Bruner, Noel; Erickson,, Anjeza; Xia, Mengna; He, Bo; and Moreau, Regis, "Role of Acetyl-CoA Synthetase 2 and Acetyl-CoA Precursors, Acetate and Ethanol, on Hepatocyte Gene Expression" (2016). UCARE Research Products. 5. https://digitalcommons.unl.edu/ucareresearch/5 This Poster is brought to you for free and open access by the UCARE: Undergraduate Creative Activities & Research Experiences at DigitalCommons@University of Nebraska - Lincoln. It has been accepted for inclusion in UCARE Research Products by an authorized administrator of DigitalCommons@University of Nebraska - Lincoln. Role of acetyl-CoA synthetase 2 and acetyl-CoA precursors, acetate and ethanol, on hepatocyte gene expression Noel Bruner, Anjeza Erickson, Mengna Xia, Bo He, and Regis Moreau Department of Nutrition & Health Sciences, University of Nebraska-Lincoln, Lincoln, NE Introduction Results Abnormally high blood and tissue lipid levels observed in the setting of metabolic disorders and cardiovascular diseases are associated with extensive gene expression changes. Gene expression is modulated by epigenetic mechanisms, which include modifications of DNA-bound protein histones without alteration of DNA sequence.
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Hsa‑Mir‑15B‑5P Regulates the Proliferation and Apoptosis of Human Vascular Smooth Muscle Cells by Targeting the ACSS2/PTGS2 Axis
EXPERIMENTAL AND THERAPEUTIC MEDICINE 22: 1208, 2021 hsa‑miR‑15b‑5p regulates the proliferation and apoptosis of human vascular smooth muscle cells by targeting the ACSS2/PTGS2 axis SHUJIE GAN1, JIEQI MAO1, YUQIN PAN2, JINGDONG TANG3 and ZHENGJUN QIU1 Departments of 1Vascular Surgery and 2Nursing, Shanghai General Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai 200080; 3Department of Vascular Surgery, Shanghai Pudong Hospital Affiliated to Fudan University, Shanghai 201399, P.R. China Received October 16, 2020; Accepted May 12, 2021 DOI: 10.3892/etm.2021.10642 Abstract. A previous bioinformatic analysis from our group promoted cell apoptosis; silencing of miR‑15b‑5p obtained the predicted that the interaction of microRNA (miRNA/miR)‑15b opposite results. ACSS2 may be a direct target of miR‑15b‑5p, with the acyl‑CoA synthetase short chain family member 2 since the luciferase activity of a ACSS2 wild‑type vector, (ACSS2) gene was important for the development of abdominal but not that of a ACSS2 mutant reporter, was significantly aortic aneurysm (AAA). Apoptosis of aortic vascular smooth inhibited by miR‑15b‑5p mimics compared with controls. muscle cells (VSMCs) is a pathological feature of AAA. The Additionally, the expression levels of ACSS2 and its down‑ present study aimed to explain the roles of miR‑15b/ACSS2 in stream gene PTGS2 were significantly reduced or increased AAA by exploring their effects on the proliferation and apop‑ following transfection with miR‑15b‑5p mimics or inhibitors, tosis of aortic VSMCs. Human aortic VSMCs (T/G HA‑VSMC respectively. Furthermore, overexpression of ACSS2 reversed cell line) were divided into six groups and were transfected with the antiproliferative and proapoptotic effects of miR‑15b‑5p miR‑15b‑5p mimics, mimic negative control (NC), miR‑15b‑5p mimics by blocking the production of PTGS2 protein.
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