[{"@context":"http:\/\/schema.org\/","@type":"BlogPosting","@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/acer1-wikipedia\/#BlogPosting","mainEntityOfPage":"https:\/\/wiki.edu.vn\/en\/wiki24\/acer1-wikipedia\/","headline":"ACER1 – Wikipedia","name":"ACER1 – Wikipedia","description":"before-content-x4 From Wikipedia, the free encyclopedia after-content-x4 Protein-coding gene in the species Homo sapiens Not to be confused with ACE1.","datePublished":"2017-07-15","dateModified":"2017-07-15","author":{"@type":"Person","@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/author\/lordneo\/#Person","name":"lordneo","url":"https:\/\/wiki.edu.vn\/en\/wiki24\/author\/lordneo\/","image":{"@type":"ImageObject","@id":"https:\/\/secure.gravatar.com\/avatar\/c9645c498c9701c88b89b8537773dd7c?s=96&d=mm&r=g","url":"https:\/\/secure.gravatar.com\/avatar\/c9645c498c9701c88b89b8537773dd7c?s=96&d=mm&r=g","height":96,"width":96}},"publisher":{"@type":"Organization","name":"Enzyklop\u00e4die","logo":{"@type":"ImageObject","@id":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","url":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","width":600,"height":60}},"image":{"@type":"ImageObject","@id":"https:\/\/en.wikipedia.org\/wiki\/Special:CentralAutoLogin\/start?type=1x1","url":"https:\/\/en.wikipedia.org\/wiki\/Special:CentralAutoLogin\/start?type=1x1","height":"1","width":"1"},"url":"https:\/\/wiki.edu.vn\/en\/wiki24\/acer1-wikipedia\/","about":["Wiki"],"wordCount":4269,"articleBody":"     (adsbygoogle = window.adsbygoogle || []).push({});before-content-x4From Wikipedia, the free encyclopedia       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4Protein-coding gene in the species Homo sapiensNot to be confused with ACE1.Alkaline ceramidase 1 also known as ACER1 is a ceramidase enzyme which in humans is encoded by the ACER1 gene.[5]       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4Table of ContentsFunction[edit]Model organisms[edit]References[edit]External links[edit]Further reading[edit]Function[edit]ACER1 mediates cellular differentiation by controlling the generation of sphingosine (SPH) and sphingosine-1-phosphate (S1P).[5]Model organisms[edit]Acer1 knockout mouse phenotypeCharacteristicPhenotypeAll data available at.[6][7][8]Peripheral blood leukocytes 6 WeeksNormalHaematology 6 WeeksNormalInsulinNormalHomozygous viability at P14NormalHomozygous FertilityNormalGeneral ObservationsAbnormalBody weightNormalNeurological assessmentNormalGrip strengthNormalDysmorphologyAbnormalIndirect calorimetryAbnormalGlucose tolerance testNormalAuditory brainstem responseNormalDEXANormalRadiographyNormalEye morphologyNormalClinical chemistryNormalHaematology 16 WeeksNormalPeripheral blood leukocytes 16 WeeksNormalHeart weightNormalSalmonella infectionNormalCytotoxic T Cell FunctionNormalSpleen ImmunophenotypingNormalMesenteric Lymph Node ImmunophenotypingNormalAnti-nuclear Antibody AssayNormalInfluenza ChallengeNormalModel organisms have been used in the study of ACER1 function. A conditional knockout mouse line called Acer1tm1a(EUCOMM)Wtsi was generated at the Wellcome Trust Sanger Institute.[9] Male and female animals underwent a standardized phenotypic screen[6] to determine the effects of deletion.[10][11][12][13] Additional screens performed:  – In-depth immunological phenotyping[7] – in-depth bone and cartilage phenotyping[8]       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4References[edit]^ a b c GRCh38: Ensembl release 89: ENSG00000167769 – Ensembl, May 2017^ a b c GRCm38: Ensembl release 89: ENSMUSG00000045019 – Ensembl, May 2017^ “Human PubMed Reference:”. National Center for Biotechnology Information, U.S. National Library of Medicine.^ “Mouse PubMed Reference:”. National Center for Biotechnology Information, U.S. National Library of Medicine.^ a b Mao C, Xu R, Szulc ZM, Bielawski J, Becker KP, Bielawska A, Galadari SH, Hu W, Obeid LM (Aug 2003). “Cloning and characterization of a mouse endoplasmic reticulum alkaline ceramidase: an enzyme that preferentially regulates metabolism of very long chain ceramides”. The Journal of Biological Chemistry. 278 (33): 31184\u201391. doi:10.1074\/jbc.M303875200. PMID\u00a012783875.^ a b “International Mouse Phenotyping Consortium”.^ a b “Infection and Immunity Immunophenotyping (3i) Consortium”.^ a b “OBCD Consortium”.^ Gerdin AK (Sep 2010). “The Sanger Mouse Genetics Programme: high throughput characterisation of knockout mice”. Acta Ophthalmologica. 88 (Supplement s246): 4142. doi:10.1111\/j.1755-3768.2010.4142.x. S2CID\u00a085911512.^ Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A (Jun 2011). “A conditional knockout resource for the genome-wide study of mouse gene function”. Nature. 474 (7351): 337\u201342. doi:10.1038\/nature10163. PMC\u00a03572410. PMID\u00a021677750.^ Dolgin E (Jun 2011). “Mouse library set to be knockout”. Nature. 474 (7351): 262\u20133. doi:10.1038\/474262a. PMID\u00a021677718.^ Collins FS, Rossant J, Wurst W (Jan 2007). “A mouse for all reasons”. Cell. 128 (1): 9\u201313. doi:10.1016\/j.cell.2006.12.018. PMID\u00a017218247. S2CID\u00a018872015.^ White JK, Gerdin AK, Karp NA, Ryder E, Buljan M, Bussell JN, Salisbury J, Clare S, Ingham NJ, Podrini C, Houghton R, Estabel J, Bottomley JR, Melvin DG, Sunter D, Adams NC, Sanger Institute Mouse Genetics Project, Tannahill D, Logan DW, Macarthur DG, Flint J, Mahajan VB, Tsang SH, Smyth I, Watt FM, Skarnes WC, Dougan G, Adams DJ, Ramirez-Solis R, Bradley A, Steel KP (2013). “Genome-wide generation and systematic phenotyping of knockout mice reveals new roles for many genes”. Cell. 154 (2): 452\u201364. doi:10.1016\/j.cell.2013.06.022. PMC\u00a03717207. PMID\u00a023870131.External links[edit]Further reading[edit]Sun W, Xu R, Hu W, Jin J, Crellin HA, Bielawski J, Szulc ZM, Thiers BH, Obeid LM, Mao C (Feb 2008). “Upregulation of the human alkaline ceramidase 1 and acid ceramidase mediates calcium-induced differentiation of epidermal keratinocytes”. The Journal of Investigative Dermatology. 128 (2): 389\u201397. doi:10.1038\/sj.jid.5701025. PMID\u00a017713573.Toulza E, Mattiuzzo NR, Galliano MF, Jonca N, Dossat C, Jacob D, de Daruvar A, Wincker P, Serre G, Guerrin M (2007). “Large-scale identification of human genes implicated in epidermal barrier function”. Genome Biology. 8 (6): R107. doi:10.1186\/gb-2007-8-6-r107. PMC\u00a02394760. PMID\u00a017562024.Ito M, Okino N, Tani M, Mitsutake S, Mori K (Mar 2002). “[Molecular evolution of neutral ceramidase: signalling molecule and virulence factor]”. Tanpakushitsu Kakusan Koso. Protein, Nucleic Acid, Enzyme. 47 (4 Suppl): 455\u201362. PMID\u00a011915342.Houben E, Holleran WM, Yaginuma T, Mao C, Obeid LM, Rogiers V, Takagi Y, Elias PM, Uchida Y (May 2006). “Differentiation-associated expression of ceramidase isoforms in cultured keratinocytes and epidermis”. Journal of Lipid Research. 47 (5): 1063\u201370. doi:10.1194\/jlr.M600001-JLR200. PMID\u00a016477081.       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