ALOX15B

From Wikipedia, the free encyclopedia

Arachidonate 15-lipoxygenase, type B

Identifiers

External IDs

OMIM: 603697 MGI: 1098228 HomoloGene: 886

Gene ontology
Molecular Function:	• iron ion binding • lipoxygenase activity • oxidoreductase activity • metal ion binding • arachidonate 15-lipoxygenase activity
Cellular Component:	• intracellular
Biological Process:	• electron transport • lipid metabolic process • fatty acid metabolic process • induction of apoptosis • negative regulation of cell proliferation • leukotriene biosynthetic process • negative regulation of cell migration • prostate gland development • regulation of epithelial cell differentiation • negative regulation of progression through cell cycle • negative regulation of growth

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001039130 (mRNA)
NP_001034219 (protein)

NM_009661 (mRNA)
NP_033791 (protein)

Location

Chr 17: 7.88 - 7.89 Mb

Chr 11: 69 - 69.01 Mb

Pubmed search

[1]

[2]

Arachidonate 15-lipoxygenase, type B, also known as ALOX15B, is a human gene.^[1]

This gene encodes a member of the lipoxygenase family of structurally related nonheme iron dioxygenases involved in the production of fatty acid hydroperoxides. The encoded protein converts arachidonic acid exclusively to 15S-hydroperoxyeicosatetraenoic acid, while metabolizing linoleic acid less effectively. This gene is located in a cluster of related genes and a pseudogene that spans approximately 100 kilobases on the short arm of chromosome 17. Alternatively spliced transcript variants encoding different isoforms have been described.^[1]

[edit] References

^ ^a ^b Entrez Gene: ALOX15B arachidonate 15-lipoxygenase, type B.

[edit] Further reading

Sigal E, Grunberger D, Highland E, et al. (1990). "Expression of cloned human reticulocyte 15-lipoxygenase and immunological evidence that 15-lipoxygenases of different cell types are related.". J. Biol. Chem. 265 (9): 5113–20. PMID 2318885.
Brash AR, Boeglin WE, Chang MS (1997). "Discovery of a second 15S-lipoxygenase in humans.". Proc. Natl. Acad. Sci. U.S.A. 94 (12): 6148–52. PMID 9177185.
Kilty I, Logan A, Vickers PJ (2000). "Differential characteristics of human 15-lipoxygenase isozymes and a novel splice variant of 15S-lipoxygenase.". Eur. J. Biochem. 266 (1): 83–93. PMID 10542053.
Krieg P, Marks F, Fürstenberger G (2001). "A gene cluster encoding human epidermis-type lipoxygenases at chromosome 17p13.1: cloning, physical mapping, and expression.". Genomics 73 (3): 323–30. doi:10.1006/geno.2001.6519. PMID 11350124.
Tang S, Bhatia B, Maldonado CJ, et al. (2002). "Evidence that arachidonate 15-lipoxygenase 2 is a negative cell cycle regulator in normal prostate epithelial cells.". J. Biol. Chem. 277 (18): 16189–201. doi:10.1074/jbc.M111936200. PMID 11839751.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
Xu XC, Shappell SB, Liang Z, et al. (2003). "Reduced 15S-lipoxygenase-2 expression in esophageal cancer specimens and cells and upregulation in vitro by the cyclooxygenase-2 inhibitor, NS398.". Neoplasia 5 (2): 121–7. PMID 12659684.
Bhatia B, Maldonado CJ, Tang S, et al. (2003). "Subcellular localization and tumor-suppressive functions of 15-lipoxygenase 2 (15-LOX2) and its splice variants.". J. Biol. Chem. 278 (27): 25091–100. doi:10.1074/jbc.M301920200. PMID 12704195.
Tang S, Bhatia B, Zhou J, et al. (2004). "Evidence that Sp1 positively and Sp3 negatively regulate and androgen does not directly regulate functional tumor suppressor 15-lipoxygenase 2 (15-LOX2) gene expression in normal human prostate epithelial cells.". Oncogene 23 (41): 6942–53. doi:10.1038/sj.onc.1207913. PMID 15247906.
Suzuki Y, Yamashita R, Shirota M, et al. (2004). "Sequence comparison of human and mouse genes reveals a homologous block structure in the promoter regions.". Genome Res. 14 (9): 1711–8. doi:10.1101/gr.2435604. PMID 15342556.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
Limor R, Kaplan M, Sawamura T, et al. (2005). "Angiotensin II increases the expression of lectin-like oxidized low-density lipoprotein receptor-1 in human vascular smooth muscle cells via a lipoxygenase-dependent pathway.". Am. J. Hypertens. 18 (3): 299–307. doi:10.1016/j.amjhyper.2004.09.008. PMID 15797645.
Subbarayan V, Xu XC, Kim J, et al. (2005). "Inverse relationship between 15-lipoxygenase-2 and PPAR-gamma gene expression in normal epithelia compared with tumor epithelia.". Neoplasia 7 (3): 280–93. doi:10.1593/neo.04457. PMID 15799828.
Jiang WG, Watkins G, Douglas-Jones A, Mansel RE (2006). "Reduction of isoforms of 15-lipoxygenase (15-LOX)-1 and 15-LOX-2 in human breast cancer.". Prostaglandins Leukot. Essent. Fatty Acids 74 (4): 235–45. doi:10.1016/j.plefa.2006.01.009. PMID 16556493.
Subbarayan V, Krieg P, Hsi LC, et al. (2006). "15-Lipoxygenase-2 gene regulation by its product 15-(S)-hydroxyeicosatetraenoic acid through a negative feedback mechanism that involves peroxisome proliferator-activated receptor gamma.". Oncogene 25 (44): 6015–25. doi:10.1038/sj.onc.1209617. PMID 16682954.
Lesueur F, Bouadjar B, Lefèvre C, et al. (2007). "Novel mutations in ALOX12B in patients with autosomal recessive congenital ichthyosis and evidence for genetic heterogeneity on chromosome 17p13.". J. Invest. Dermatol. 127 (4): 829–34. doi:10.1038/sj.jid.5700640. PMID 17139268.