LOXL4

From Wikipedia, the free encyclopedia

Lysyl oxidase-like 4

Identifiers

LOXL4; FLJ21889; LOXC

External IDs

OMIM: 607318 MGI: 1914823 HomoloGene: 12977

Gene ontology
Molecular Function:	• protein-lysine 6-oxidase activity • scavenger receptor activity • copper ion binding • oxidoreductase activity • metal ion binding
Cellular Component:	• extracellular region • membrane

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_032211 (mRNA)
NP_115587 (protein)

NM_053083 (mRNA)
NP_444313 (protein)

Location

Chr 10: 100 - 100.02 Mb

Chr 19: 42.65 - 42.67 Mb

Pubmed search

[1]

[2]

Lysyl oxidase-like 4, also known as LOXL4, is a human gene.^[1]

This gene encodes a member of the lysyl oxidase gene family. The prototypic member of the family is essential to the biogenesis of connective tissue, encoding an extracellular copper-dependent amine oxidase that catalyses the first step in the formation of crosslinks in collagens and elastin. A highly conserved amino acid sequence at the C-terminus end appears to be sufficient for amine oxidase activity, suggesting that each family member may retain this function. The N-terminus is poorly conserved and may impart additional roles in developmental regulation, senescence, tumor suppression, cell growth control, and chemotaxis to each member of the family.^[1]

[edit] References

^ ^a ^b Entrez Gene: LOXL4 lysyl oxidase-like 4.

[edit] Further reading

Molnar J, Fong KS, He QP, et al. (2003). "Structural and functional diversity of lysyl oxidase and the LOX-like proteins.". Biochim. Biophys. Acta 1647 (1-2): 220–4. PMID 12686136.
Ito H, Akiyama H, Iguchi H, et al. (2001). "Molecular cloning and biological activity of a novel lysyl oxidase-related gene expressed in cartilage.". J. Biol. Chem. 276 (26): 24023–9. doi:10.1074/jbc.M100861200. PMID 11292829.
Asuncion L, Fogelgren B, Fong KS, et al. (2002). "A novel human lysyl oxidase-like gene (LOXL4) on chromosome 10q24 has an altered scavenger receptor cysteine rich domain.". Matrix Biol. 20 (7): 487–91. PMID 11691588.
Mäki JM, Tikkanen H, Kivirikko KI (2002). "Cloning and characterization of a fifth human lysyl oxidase isoenzyme: the third member of the lysyl oxidase-related subfamily with four scavenger receptor cysteine-rich domains.". Matrix Biol. 20 (7): 493–6. PMID 11691589.
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.
Holtmeier C, Görögh T, Beier U, et al. (2003). "Overexpression of a novel lysyl oxidase-like gene in human head and neck squamous cell carcinomas.". Anticancer Res. 23 (3B): 2585–91. PMID 12894545.
Kim MS, Kim SS, Jung ST, et al. (2004). "Expression and purification of enzymatically active forms of the human lysyl oxidase-like protein 4.". J. Biol. Chem. 278 (52): 52071–4. doi:10.1074/jbc.M308856200. PMID 14551188.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
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.
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.". Cell 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.
Shieh TM, Lin SC, Liu CJ, et al. (2007). "Association of expression aberrances and genetic polymorphisms of lysyl oxidase with areca-associated oral tumorigenesis.". Clin. Cancer Res. 13 (15 Pt 1): 4378–85. doi:10.1158/1078-0432.CCR-06-2685. PMID 17671119.