ACER1

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
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RefSeq (mRNA)

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RefSeq (protein)

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Alkaline ceramidase 1 also known as ACER1 is a ceramidase enzyme which in humans is encoded by the ACER1 gene.[1]

Function

ACER1 mediates cellular differentiation by controlling the generation of sphingosine (SPH) and sphingosine-1-phosphate (S1P).[1]

Model organisms

Model 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.[5] Male and female animals underwent a standardized phenotypic screen[2] to determine the effects of deletion.[6][7][8][9] Additional screens performed: - In-depth immunological phenotyping[3] - in-depth bone and cartilage phenotyping[4]

References

  1. 1.0 1.1 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): 31184–91. doi:10.1074/jbc.M303875200. PMID 12783875.
  2. 2.0 2.1 "International Mouse Phenotyping Consortium".
  3. 3.0 3.1 "Infection and Immunity Immunophenotyping (3i) Consortium".
  4. 4.0 4.1 "OBCD Consortium".
  5. 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.
  6. 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): 337–42. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
  7. Dolgin E (Jun 2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
  8. Collins FS, Rossant J, Wurst W (Jan 2007). "A mouse for all reasons". Cell. 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247.
  9. 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): 452–64. doi:10.1016/j.cell.2013.06.022. PMC 3717207. PMID 23870131.

External links

Further reading

  • 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): 389–97. doi:10.1038/sj.jid.5701025. PMID 17713573.
  • 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 2394760. PMID 17562024.
  • 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): 455–62. PMID 11915342.
  • 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): 1063–70. doi:10.1194/jlr.M600001-JLR200. PMID 16477081.