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ALOX15 (Arachidonate 15-Lipoxygenase)

Identity

Other names15-LOX
EC 1.13.11.33
arachidonate omega 6-lipoxygenase
LOG15
HGNC (Hugo) ALOX15
LocusID (NCBI) 246
Location 17p13.2
Location_base_pair Starts at 4534214 and ends at 4544960 bp from pter ( according to hg19-Feb_2009)  [Mapping]
Local_order Genes flanking ALOX15 in centromere to telomere direction on 17p13 are:
  • MYBBP1A 17p13.3 MYB binding protein (P160) 1a.
  • GGT6 17p13.2 homolog of gamma-glutamyltransferase 6
  • LOC12497417p13.2,thioredoxin 1 pseudogene 4.
  • SMTNL2 17p13.2 smoothelin-like 2
  • ALOX15 17p13.2 arachidonate 15-lipoxygenase (Homo sapiens)
  • PELP1 17p13.2 proline, glutamic acid and leucine rich protein 1.
  • ARRB2 17p13 arrestin, beta 2.
  • Note Arachidonate 15-Lipoxygenase (15-LOX-1) is one of several LOX isoforms that oxygenates polyunsaturated fatty acids as well as complex substrates such as biomembranes. Its expression is associated with the development of inflammatory diseases such as atherosclerosis, asthma, cancer and osteoporosis.

    DNA/RNA

    Note With the exception of ALOX5, all human LOX genes, including ALOX15, are clustered on the short arm of chromosome 17 within a few megabases of each other. ALOX12, which has 86% sequence homology to ALOX15 is in closest proximity (17p13.1). Since chromosome 17 is known for gene duplications, the multiple LOX genes on the same chromosome may be as a result of such duplications.
     
      ALOX15Fig. Diagram of the ALOX15 gene. Exons are represented by red boxes (in scale) untranscribed sequences in black, with exon numbers on the bottom. The arrows show the ATG and the stop codons respectively.
    Description ALOX15 gene spans a region of 10.7 kilo bases. and has 14 exons, the sizes being 149, 202, 82, 123, 104, 161, 144, 210, 87, 170, 122, 101, 108 and 859 bps.
    Transcription ALOX15 mRNA has 2702 bps.
    TH2 cytokines IL-4 ID: 40960 and IL-13 have been shown to transcriptionally upregulate 15-LOX-1 expression via phosphorylation of Signal Transducer and Activator of transcription (STAT) proteins, particularly STAT-1, STAT-3 and STAT-6 and their translocation to the nucleus. Acetylation of histones, which block STAT6 binding at the 15-LOX-1 promoter if they are present as nonacetylated proteins, enables promoter binding of phosphorylated and acetylated STAT6, which in turn may lead to transcriptional activation of the 15-LOX gene. TRANSCRIPTION NSAIDS have been reported to upregulate 15-LOX-1 expression through GATA-6. Ku70/ lupus autoantigen transcription factors have also been reported to be induced by IL-4 and IL-13 in the upregulation of ALOX15. In addition, demethylation of the 5 CpG islands in the promoter region of ALOX15 has been shown to transcriptionally upregulate the gene.
    ALOX15 mRNA is expressed in bone marrow, spleen, thymus, spinal cord, heart, skeletal muscle, liver, prostate, kidney and lung.
    Pseudogene The arachidonate 15-lipoxygenase pseudogene (ALOX15P) is located on 17p13.1.

    Protein

    Note Two different 15-Lipoxygenases exist, 15-LOX-1 (reticulocyte type) and 15-LOX-2 (epidermis type), differentiated by their tissue expression and a 40% homology at the amino acid level. 15-LOX-1 preferentially oxygenates linoleic acid into 13(S)-hydroxyoctadecadienoic acid (13(S)-HPODE) whereas 15-LOX-2 preferentially metabolizes arachidonic acid (AA) to 15S- hydroperoxyeicosatetraenoic acid (15-HETE) with poor activity with linoleic acid (LA).
    Description 15-LOX-1 protein consists of 661 amino acids and is 74.7 kDa. It contains 1 gram atom of non-haem non-sulphur bound iron per mole of the enzyme. Conserved domain search, the presence of a polycystin/lipoxygenase/alpha-toxin (PLAT) domain in the 15-LOX-1 protein allows it access and enables it to catalyze enzymatic lipid peroxidation in complex biological structures via direct dioxygenation of phospholipids and cholesterol esters of biomembranes and plasma lipoproteins. The membrane binding domain of the rabbit reticulocyte 15-LOX are determined by a concerted action of the N-terminal beta-barrel and the C-terminal catalytic domain.
    Expression 15-LOX-1 was first purified in rabbit reticulocytes and was subsequently found to be specifically expressed or induced in mast cells, eosinophils, activated monocytes or dendritic cells, and bronchial epithelial cells.
    Localisation Located in the cytoplasm.
    Function 15-LOX-1 is a member of the inflammatory leukotriene biosynthesis pathway where, in presence of molecular oxygen, it converts arachidonic acid to(15-HETE). Also acts on C-12 of arachidonate forming products (12-HETE) at a ratio of 12:1 (15-HETE:12-HETE). Preferentially converts linoleic acid to 13(S)-HODE.
    Homology C. familiaris LOC4894581 similar to Arachidonate 15-lipoxygenase;
    R. norvegicus: Alox15 arachidonate 12-lipoxygenase;
    M. musculus: Alox15 arachidonate 15-lipoxygenase (12/15LOX);
    A. thaliana: F12B7.11, F12B7_111 iron ion binding / lipoxygenase;

    Mutations

    Note No mutations have been reported for ALOX15 that cause congenital anomalies. Single nucleotide polymorphism (SNP) studies have revealed that a C-to-T base exchange (-292C/T) enhances the transcriptional activity of the ALOX15 promoter in macrophages through the generation of a novel SPI1 transcription factor binding site. In addition, a G to A base exchange (-5229G/A) in the ALOX15 promoter region has been associated with low bone mineral density.

    Implicated in

    Entity Prostate cancer
    Note Genechip study of the mRNA levels of key enzymes involved in the LA and AA pathways in 18 human donor (normal) prostates compared to 60 prostate tumours showed a lower level of 15-LOX-1 expression (the key enzyme in the LA pathway) in contrast to a higher 15-lipoxygenase-2 expression in donor (normal) prostates. On the other hand, significantly high levels of 15-LOX-1 and low levels of 15-LOX-2/ALOX15B were observed in prostate carcinoma tissues.
      
    Entity Colorectal cancer
    Note The role of 15-LOX-1 in colorectal cancer is controversial with some researchers claiming a mitogenic role through up-regulation of the EGF signaling pathway as well as activation of ERK and down regulation of anti-inflammatory PPAR-gamma transcriptional activity. Its upregulation by mutant TP53 has been reported. On the other hand, in recent years others have shown that 15-LOX-1 expression is reduced in colorectal cancer and implicated 13(S)-HPODE in the pro-apoptotic functions of 15-LOX-1. 15-LOX-1 expression was shown to be down-regulated in colorectal adenomas (compared with non neoplastic epithelial mucosa) in 87% (13 of 15) of patients with familial adenomatous polyposis resulting in an escape from apoptosis. Ectopic restoration of 15-LOX-1 expression re-established apoptosis in Caco-2 colon cancer cells. A proapoptotic function ascribed to 15-LOX-1 and 15-LOX-2 in colon cancer is said to be through the activation of the anti-tumorigenic PPAR-gamma and down-regulation of the pro-tumorigenic PPAR-delta/beta. In addition, the apoptotic functions of NSAIDS are reported to be via an upregulation of 15-LOX-1.
      
    Entity Breast cancer
    Note An immunoblot analysis of metastatic human breast carcinoma cells with antibodies to 15-LOX-1 and 15-LOX-2 indicated that it is the 15(S)-LOX-2 isoform that generates 15-HETE and activates specific growth factor receptor-related signalling pathways, thereby initiating signal transduction events resulting in enhanced cell adhesion to the extracellular matrix. However, a second study indicated that both 15-LOX-2 and 15-LOX-1 were expressed at significantly lower levels in metastatic tumours and in patients who died of breast cancer related causes. This reduction is correlated with the disease progression of breast cancer and a poor clinical outcome.
      
    Entity Atherosclerosis
    Disease Atherosclerosis is a chronic proliferative disease of the arterial wall that is associated with aberrant immune reactions. A proatherogenic activity of 12/15LOX via oxidation of low density lipoproteins and formation of foam cells in various rodent atherosclerosis models has been shown. A similar extrapolation to humans has not been convincingly proven, particularly since significantly lower expression of 15-LOX-1 was detected in diseased and normal human arteries when compared to 5-LOX.
      
    Entity Asthma
    Disease Patients with severe asthma with persistent airway eosinophils have been shown to manifest high levels of 15(S)-HETE in bronchoalveolar lavage (BALF), which may be associated with airway fibrosis. In addition, IL-4-induced apoptosis via upregulation of 15-LOX-1 and PPAR-gamma may contribute to severe loss of alveolar structures and infiltration of eosinophils, mononuclear phagocytes, etc., into the lung tissue of chronic asthma patients.
      

    External links

    Nomenclature
    HGNC (Hugo)ALOX15   433
    Cards
    AtlasALOX15ID42986ch17p13
    Entrez_Gene (NCBI)ALOX15  246  arachidonate 15-lipoxygenase
    GeneCards (Weizmann)ALOX15
    Ensembl (Hinxton)ENSG00000161905 [Gene_View]  chr17:4534214-4544960 [Contig_View]  ALOX15 [Vega]
    ICGC DataPortalENSG00000161905
    cBioPortalALOX15
    AceView (NCBI)ALOX15
    Genatlas (Paris)ALOX15
    WikiGenes246
    SOURCE (Princeton)NM_001140
    Genomic and cartography
    GoldenPath (UCSC)ALOX15  -  17p13.2   chr17:4534214-4544960 -  17p13.3   [Description]    (hg19-Feb_2009)
    EnsemblALOX15 - 17p13.3 [CytoView]
    Mapping of homologs : NCBIALOX15 [Mapview]
    OMIM152392   
    Gene and transcription
    Genbank (Entrez)AK290309 AK296792 AK296821 AK296904 AK312557
    RefSeq transcript (Entrez)NM_001140
    RefSeq genomic (Entrez)AC_000149 NC_000017 NC_018928 NT_010718 NW_001838403 NW_004929405
    Consensus coding sequences : CCDS (NCBI)ALOX15
    Cluster EST : UnigeneHs.73809 [ NCBI ]
    CGAP (NCI)Hs.73809
    Alternative Splicing : Fast-db (Paris)GSHG0013008
    Alternative Splicing GalleryENSG00000161905
    Gene ExpressionALOX15 [ NCBI-GEO ]     ALOX15 [ SEEK ]   ALOX15 [ MEM ]
    Protein : pattern, domain, 3D structure
    UniProt/SwissProtP16050 (Uniprot)
    NextProtP16050  [Medical]
    With graphics : InterProP16050
    Splice isoforms : SwissVarP16050 (Swissvar)
    Catalytic activity : Enzyme1.13.11.33 [ Enzyme-Expasy ]   1.13.11.331.13.11.33 [ IntEnz-EBI ]   1.13.11.33 [ BRENDA ]   1.13.11.33 [ KEGG ]   
    Domaine pattern : Prosite (Expaxy)LIPOXYGENASE_1 (PS00711)    LIPOXYGENASE_2 (PS00081)    LIPOXYGENASE_3 (PS51393)    PLAT (PS50095)   
    Domains : Interpro (EBI)Lipase_LipOase [organisation]   LipOase [organisation]   LipOase_C [organisation]   LipOase_CS [organisation]   LipOase_Fe_BS [organisation]   LipOase_mml [organisation]   PLAT/LH2_dom [organisation]  
    Related proteins : CluSTrP16050
    Domain families : Pfam (Sanger)Lipoxygenase (PF00305)    PLAT (PF01477)   
    Domain families : Pfam (NCBI)pfam00305    pfam01477   
    Domain families : Smart (EMBL)LH2 (SM00308)  
    DMDM Disease mutations246
    Blocks (Seattle)P16050
    PDB (SRS)2ABT   
    PDB (PDBSum)2ABT   
    PDB (IMB)2ABT   
    PDB (RSDB)2ABT   
    Human Protein AtlasENSG00000161905 [gene] [tissue] [antibody] [cell] [cancer]
    Peptide AtlasP16050
    HPRD01067
    IPIIPI01016011   IPI00221221   IPI00719802   
    Protein Interaction databases
    DIP (DOE-UCLA)P16050
    IntAct (EBI)P16050
    FunCoupENSG00000161905
    BioGRIDALOX15
    InParanoidP16050
    Interologous Interaction database P16050
    IntegromeDBALOX15
    STRING (EMBL)ALOX15
    Ontologies - Pathways
    Ontology : AmiGOossification  negative regulation of adaptive immune response  arachidonate 12-lipoxygenase activity  iron ion binding  protein binding  phosphatidylinositol-4,5-bisphosphate binding  lipid particle  cytosol  cytosol  cytosol  plasma membrane  phosphatidylethanolamine biosynthetic process  leukotriene metabolic process  inflammatory response  positive regulation of cell-substrate adhesion  membrane  arachidonic acid metabolic process  arachidonic acid metabolic process  arachidonic acid metabolic process  lipoxygenase pathway  lipoxygenase pathway  bone mineralization  positive regulation of actin filament polymerization  extrinsic component of cytoplasmic side of plasma membrane  response to endoplasmic reticulum stress  regulation of peroxisome proliferator activated receptor signaling pathway  cellular response to interleukin-13  wound healing  apoptotic cell clearance  small molecule metabolic process  arachidonate 15-lipoxygenase activity  arachidonate 15-lipoxygenase activity  hepoxilin biosynthetic process  oxidation-reduction process  positive regulation of ERK1 and ERK2 cascade  cellular response to calcium ion  eoxin A4 synthase activity  regulation of engulfment of apoptotic cell  lipoxin A4 biosynthetic process  
    Ontology : EGO-EBIossification  negative regulation of adaptive immune response  arachidonate 12-lipoxygenase activity  iron ion binding  protein binding  phosphatidylinositol-4,5-bisphosphate binding  lipid particle  cytosol  cytosol  cytosol  plasma membrane  phosphatidylethanolamine biosynthetic process  leukotriene metabolic process  inflammatory response  positive regulation of cell-substrate adhesion  membrane  arachidonic acid metabolic process  arachidonic acid metabolic process  arachidonic acid metabolic process  lipoxygenase pathway  lipoxygenase pathway  bone mineralization  positive regulation of actin filament polymerization  extrinsic component of cytoplasmic side of plasma membrane  response to endoplasmic reticulum stress  regulation of peroxisome proliferator activated receptor signaling pathway  cellular response to interleukin-13  wound healing  apoptotic cell clearance  small molecule metabolic process  arachidonate 15-lipoxygenase activity  arachidonate 15-lipoxygenase activity  hepoxilin biosynthetic process  oxidation-reduction process  positive regulation of ERK1 and ERK2 cascade  cellular response to calcium ion  eoxin A4 synthase activity  regulation of engulfment of apoptotic cell  lipoxin A4 biosynthetic process  
    Pathways : KEGGArachidonic acid metabolism    Linoleic acid metabolism    Serotonergic synapse   
    Protein Interaction DatabaseALOX15
    Wikipedia pathwaysALOX15
    Gene fusion - rearrangments
    Polymorphisms : SNP, mutations, diseases
    SNP Single Nucleotide Polymorphism (NCBI)ALOX15
    snp3D : Map Gene to Disease246
    SNP (GeneSNP Utah)ALOX15
    SNP : HGBaseALOX15
    Genetic variants : HAPMAPALOX15
    Exome VariantALOX15
    1000_GenomesALOX15 
    ICGC programENSG00000161905 
    Somatic Mutations in Cancer : COSMICALOX15 
    CONAN: Copy Number AnalysisALOX15 
    Mutations and Diseases : HGMDALOX15
    Mutations and Diseases : intOGenALOX15
    Genomic VariantsALOX15  ALOX15 [DGVbeta]
    dbVarALOX15
    ClinVarALOX15
    Pred. of missensesPolyPhen-2  SIFT(SG)  SIFT(JCVI)  Align-GVGD  MutAssessor  Mutanalyser  
    Pred. splicesGeneSplicer  Human Splicing Finder  MaxEntScan  
    Diseases
    OMIM152392   
    MedgenALOX15
    GENETestsALOX15
    Disease Genetic AssociationALOX15
    Huge Navigator ALOX15 [HugePedia]  ALOX15 [HugeCancerGEM]
    General knowledge
    Homologs : HomoloGeneALOX15
    Homology/Alignments : Family Browser (UCSC)ALOX15
    Phylogenetic Trees/Animal Genes : TreeFamALOX15
    Chemical/Protein Interactions : CTD246
    Chemical/Pharm GKB GenePA48
    Clinical trialALOX15
    Cancer Resource (Charite)ENSG00000161905
    Other databases
    Probes
    Litterature
    PubMed155 Pubmed reference(s) in Entrez
    CoreMineALOX15
    iHOPALOX15
    OncoSearchALOX15

    Bibliography

    Discovery of a second 15S-lipoxygenase in humans.
    Brash AR, Boeglin WE, Chang MS
    Proceedings of the National Academy of Sciences of the United States of America. 1997 ; 94 (12) : 6148-6152.
    PMID 9177185
     
    Expression of 15-lipoxygenase-1 in human colorectal cancer.
    Ikawa H, Kamitani H, Calvo BF, Foley JF, Eling TE
    Cancer research. 1999 ; 59 (2) : 360-366.
    PMID 9927047
     
    Effects of mutant p53 expression on human 15-lipoxygenase-promoter activity and murine 12/15-lipoxygenase gene expression: evidence that 15-lipoxygenase is a mutator gene.
    Kelavkar UP, Badr KF
    Proceedings of the National Academy of Sciences of the United States of America. 1999 ; 96 (8) : 4378-4383.
    PMID 10200270
     
    Acetylation by histone acetyltransferase CREB-binding protein/p300 of STAT6 is required for transcriptional activation of the 15-lipoxygenase-1 gene.
    Shankaranarayanan P, Chaitidis P, Khn H, Nigam S
    The Journal of biological chemistry. 2001 ; 276 (46) : 42753-42760.
    PMID 11509556
     
    Nonsteroidal anti-inflammatory drugs induce apoptosis in esophageal cancer cells by restoring 15-lipoxygenase-1 expression.
    Shureiqi I, Xu X, Chen D, Lotan R, Morris JS, Fischer SM, Lippman SM
    Cancer research. 2001 ; 61 (12) : 4879-4884.
    PMID 11406566
     
    15-lipoxygenase: a Janus enzyme?
    Chanez P, Bonnans C, Chavis C, Vachier I
    American journal of respiratory cell and molecular biology. 2002 ; 27 (6) : 655-658.
    PMID 12444024
     
    15-lipoxygenase-1 overexpression in prostate adenocarcinoma.
    Kelavkar U, Cohen C, Eling T, Badr K
    Advances in experimental medicine and biology. 2002 ; 507 : 133-145.
    PMID 12664577
     
    KU 70/80 lupus autoantigen is the transcription factor induced by interleukins (IL)-13 and -4 leading to induction of 15-lipoxygenase (15-LO) in human cells.
    Kelavkar U, Wang S, Badr K
    Advances in experimental medicine and biology. 2002 ; 507 : 469-481.
    PMID 12664628
     
    GATA-6 transcriptional regulation of 15-lipoxygenase-1 during NSAID-induced apoptosis in colorectal cancer cells.
    Shureiqi I, Jiang W, Fischer SM, Xu X, Chen D, Lee JJ, Lotan R, Lippman SM
    Cancer research. 2002 ; 62 (4) : 1178-1183.
    PMID 11861401
     
    The N-terminal domain of the reticulocyte-type 15-lipoxygenase is not essential for enzymatic activity but contains determinants for membrane binding.
    Walther M, Anton M, Wiedmann M, Fletterick R, Kuhn H
    The Journal of biological chemistry. 2002 ; 277 (30) : 27360-27366.
    PMID 12004065
     
    15-hydroxy-eicosatetraenoic acid arrests growth of colorectal cancer cells via a peroxisome proliferator-activated receptor gamma-dependent pathway.
    Chen GG, Xu H, Lee JF, Subramaniam M, Leung KL, Wang SH, Chan UP, Spelsberg TC
    International journal of cancer. Journal international du cancer. 2003 ; 107 (5) : 837-843.
    PMID 14566836
     
    IL-4 induces apoptosis in A549 lung adenocarcinoma cells: evidence for the pivotal role of 15-hydroxyeicosatetraenoic acid binding to activated peroxisome proliferator-activated receptor gamma transcription factor.
    Shankaranarayanan P, Nigam S
    Journal of immunology (Baltimore, Md. : 1950). 2003 ; 170 (2) : 887-894.
    PMID 12517954
     
    Interleukin-13 induction of 15-lipoxygenase gene expression requires p38 mitogen-activated protein kinase-mediated serine 727 phosphorylation of Stat1 and Stat3.
    Xu B, Bhattacharjee A, Roy B, Xu HM, Anthony D, Frank DA, Feldman GM, Cathcart MK
    Molecular and cellular biology. 2003 ; 23 (11) : 3918-3928.
    PMID 12748293
     
    Transcriptional regulation of 15-lipoxygenase expression by promoter methylation.
    Liu C, Xu D, Sjberg J, Forsell P, Bjrkholm M, Claesson HE
    Experimental cell research. 2004 ; 297 (1) : 61-67.
    PMID 15194425
     
    15-Lipoxygenase-1 has anti-tumorigenic effects in colorectal cancer.
    Nixon JB, Kim KS, Lamb PW, Bottone FG, Eling TE
    Prostaglandins, leukotrienes, and essential fatty acids. 2004 ; 70 (1) : 7-15.
    PMID 14643174
     
    15-LOX-1 inhibits p21 (Cip/WAF 1) expression by enhancing MEK-ERK 1/2 signaling in colon carcinoma cells.
    Yoshinaga M, Buchanan FG, DuBois RN
    Prostaglandins & other lipid mediators. 2004 ; 73 (1-2) : 111-122.
    PMID 15165036
     
    15S-Lipoxygenase-2 mediates arachidonic acid-stimulated adhesion of human breast carcinoma cells through the activation of TAK1, MKK6, and p38 MAPK.
    Nony PA, Kennett SB, Glasgow WC, Olden K, Roberts JD
    The Journal of biological chemistry. 2005 ; 280 (36) : 31413-31419.
    PMID 16000313
     
    The role of lipoxygenase-isoforms in atherogenesis.
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    Molecular nutrition & food research. 2005 ; 49 (11) : 1014-1029.
    PMID 16270276
     
    The critical role of 15-lipoxygenase-1 in colorectal epithelial cell terminal differentiation and tumorigenesis.
    Shureiqi I, Wu Y, Chen D, Yang XL, Guan B, Morris JS, Yang P, Newman RA, Broaddus R, Hamilton SR, Lynch P, Levin B, Fischer SM, Lippman SM
    Cancer research. 2005 ; 65 (24) : 11486-11492.
    PMID 16357157
     
    Association of a single nucleotide polymorphism in the lipoxygenase ALOX15 5'-flanking region (-5229G/A) with bone mineral density.
    Urano T, Shiraki M, Fujita M, Hosoi T, Orimo H, Ouchi Y, Inoue S
    Journal of bone and mineral metabolism. 2005 ; 23 (3) : 226-230.
    PMID 15838625
     
    Reduction of isoforms of 15-lipoxygenase (15-LOX)-1 and 15-LOX-2 in human breast cancer.
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    The yin and yang of 15-lipoxygenase-1 and delta-desaturases: dietary omega-6 linoleic acid metabolic pathway in prostate.
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    Journal of carcinogenesis. 2006 ; 5 : page 9.
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    Inflammation and immune regulation by 12/15-lipoxygenases.
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    PMID 16678271
     
    Oxidative metabolism of linoleic acid modulates PPAR-beta/delta suppression of PPAR-gamma activity.
    Zuo X, Wu Y, Morris JS, Stimmel JB, Leesnitzer LM, Fischer SM, Lippman SM, Shureiqi I
    Oncogene. 2006 ; 25 (8) : 1225-1241.
    PMID 16288226
     
    Functional polymorphism in ALOX15 results in increased allele-specific transcription in macrophages through binding of the transcription factor SPI1.
    Wittwer J, Marti-Jaun J, Hersberger M
    Human mutation. 2006 ; 27 (1) : 78-87.
    PMID 16320347
     
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    Contributor(s)

    Written06-2006Sreeparna Banerjee
    Department of Biology, Office: Z-16/Lab: B-59, Middle East Technical University, 06531 Ankara, Turkey

    Citation

    This paper should be referenced as such :
    Banerjee, S
    ALOX15 (arachidonate 15-lipoxygenase)
    Atlas Genet Cytogenet Oncol Haematol. 2006;10(4):230-233.
    Free online version   Free pdf version   [Bibliographic record ]
    URL : http://AtlasGeneticsOncology.org/Genes/ALOX15ID42986ch17p13.html

    © Atlas of Genetics and Cytogenetics in Oncology and Haematology
    indexed on : Tue Sep 23 19:21:28 CEST 2014

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