Lysyl oxidase

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Lysyl oxidase
Identifiers
Symbol(s) LOX; MGC105112
External IDs OMIM: 153455 MGI: 96817 HomoloGene: 1741
EC number 1.4.3.13
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 4015 16948
Ensembl ENSG00000113083 ENSMUSG00000024529
Uniprot P28300 Q3TLP7
Refseq NM_002317 (mRNA)
NP_002308 (protein)		 NM_010728 (mRNA)
NP_034858 (protein)
Location Chr 5: 121.43 - 121.44 Mb Chr 18: 52.65 - 52.65 Mb
Pubmed search [1] [2]

Lysyl oxidase, also known as LOX, is a human gene.[1]

The protein encoded by this gene is an extracellular copper enzyme that initiates the crosslinking of collagens and elastin. The enzyme catalyzes oxidative deamination of the epsilon-amino group in certain lysine and hydroxylysine residues of collagens and lysine residues of elastin. In addition to crosslinking extracellular matrix proteins, the encoded protein may have a role in tumor suppression.[1]

Lysyl oxidase is an extracellular enzyme that catalyzes formation of aldehydes from lysine residues in collagen and elastin precursors. These aldehydes are highly reactive, and undergo spontaneous chemical reactions with other lysyl oxidase-derived aldehyde residues, or with unmodified lysine residues. This results in cross-linking collagen and elastin, which is essential for stabilization of collagen fibrils and for the integrity and elasticity of mature elastin.

Complex cross-links are formed in collagen (pyrodininolines derived from three lysine residues) and in elastin (desmosines derived from four lysine residues) that differ in structure.

The importance of lysyl oxidase-derived cross-linking was established from animal studies in which lysyl oxidase was inhibited either by nutritional copper-deficiency or by supplementation of diets with β-aminopropionitrile (BAPN), an inhibitor of lysyl oxidase. This resulted in lathyrism, characterized by poor bone formation and strength, hyperextensible skin, weak ligaments, and increased occurrence of aortic aneurysms. These abnormalities correlated well with decreased cross-linking of collagen and elastin.

Contents

[edit] See also

[edit] References

  • Alberts, Bruce (2002). Molecular biology of the cell. New York: Garland Science. ISBN 0-8153-3218-1. 
  1. ^ a b Entrez Gene: LOX lysyl oxidase.

[edit] Further reading

  • Csiszar K (2001). "Lysyl oxidases: a novel multifunctional amine oxidase family.". Prog. Nucleic Acid Res. Mol. Biol. 70: 1–32. PMID 11642359. 
  • Kagan HM, Li W (2003). "Lysyl oxidase: properties, specificity, and biological roles inside and outside of the cell.". J. Cell. Biochem. 88 (4): 660–72. doi:10.1002/jcb.10413. PMID 12577300. 
  • Svinarich DM, Twomey TA, Macauley SP, et al. (1992). "Characterization of the human lysyl oxidase gene locus.". J. Biol. Chem. 267 (20): 14382–7. PMID 1352776. 
  • Mariani TJ, Trackman PC, Kagan HM, et al. (1992). "The complete derived amino acid sequence of human lysyl oxidase and assignment of the gene to chromosome 5 (extensive sequence homology with the murine ras recision gene).". Matrix 12 (3): 242–8. PMID 1357535. 
  • Murawaki Y, Kusakabe Y, Hirayama C (1992). "Serum lysyl oxidase activity in chronic liver disease in comparison with serum levels of prolyl hydroxylase and laminin.". Hepatology 14 (6): 1167–73. PMID 1683640. 
  • Hämäläinen ER, Jones TA, Sheer D, et al. (1992). "Molecular cloning of human lysyl oxidase and assignment of the gene to chromosome 5q23.3-31.2.". Genomics 11 (3): 508–16. PMID 1685472. 
  • Konishi A, Iguchi H, Ochi J, et al. (1985). "Increased lysyl oxidase activity in culture medium of nonparenchymal cells from fibrotic livers.". Gastroenterology 89 (4): 709–15. PMID 2863189. 
  • Kuivaniemi H, Ala-Kokko L, Kivirikko KI (1986). "Secretion of lysyl oxidase by cultured human skin fibroblasts and effects of monensin, nigericin, tunicamycin and colchicine.". Biochim. Biophys. Acta 883 (2): 326–34. PMID 2874833. 
  • Reiser KM, Hennessy SM, Last JA (1988). "Analysis of age-associated changes in collagen crosslinking in the skin and lung in monkeys and rats.". Biochim. Biophys. Acta 926 (3): 339–48. PMID 3120785. 
  • Järveläinen H, Halme T, Rönnemaa T (1982). "Effect of cortisol on the proliferation and protein synthesis of human aortic smooth muscle cells in culture.". Acta Med. Scand. Suppl. 660: 114–22. PMID 6127904. 
  • Kuivaniemi H, Savolainen ER, Kivirikko KI (1984). "Human placental lysyl oxidase. Purification, partial characterization, and preparation of two specific antisera to the enzyme.". J. Biol. Chem. 259 (11): 6996–7002. PMID 6144680. 
  • Lien YH, Stern R, Fu JC, Siegel RC (1984). "Inhibition of collagen fibril formation in vitro and subsequent cross-linking by glucose.". Science 225 (4669): 1489–91. PMID 6147899. 
  • Yasutake A, Powers JC (1981). "Reactivity of human leukocyte elastase and porcine pancreatic elastase toward peptide 4-nitroanilides containing model desmosine residues. Evidence that human leukocyte elastase is selective for cross-linked regions of elastin.". Biochemistry 20 (13): 3675–9. PMID 6912069. 
  • Kim Y, Boyd CD, Csiszar K (1995). "A new gene with sequence and structural similarity to the gene encoding human lysyl oxidase.". J. Biol. Chem. 270 (13): 7176–82. PMID 7706256. 
  • Hämäläinen ER, Kemppainen R, Pihlajaniemi T, Kivirikko KI (1993). "Structure of the human lysyl oxidase gene.". Genomics 17 (3): 544–8. doi:10.1006/geno.1993.1369. PMID 7902322. 
  • Forbes EG, Cronshaw AD, MacBeath JR, Hulmes DJ (1994). "Tyrosine-rich acidic matrix protein (TRAMP) is a tyrosine-sulphated and widely distributed protein of the extracellular matrix.". FEBS Lett. 351 (3): 433–6. PMID 8082810. 
  • Csiszar K, Mariani TJ, Gosin JS, et al. (1993). "A restriction fragment length polymorphism results in a nonconservative amino acid substitution encoded within the first exon of the human lysyl oxidase gene.". Genomics 16 (2): 401–6. doi:10.1006/geno.1993.1203. PMID 8100215. 
  • Vetter U, Weis MA, Mörike M, et al. (1993). "Collagen crosslinks and mineral crystallinity in bone of patients with osteogenesis imperfecta.". J. Bone Miner. Res. 8 (2): 133–7. PMID 8442432. 
  • Panchenko MV, Stetler-Stevenson WG, Trubetskoy OV, et al. (1996). "Metalloproteinase activity secreted by fibrogenic cells in the processing of prolysyl oxidase. Potential role of procollagen C-proteinase.". J. Biol. Chem. 271 (12): 7113–9. PMID 8636146. 
  • Khakoo A, Thomas R, Trompeter R, et al. (1997). "Congenital cutis laxa and lysyl oxidase deficiency.". Clin. Genet. 51 (2): 109–14. PMID 9111998. 
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CH-NH2 oxidoreductases (EC 1.4) - primarily amino acid oxidoreductases
1.4.1 - NAD/NADP acceptor
1.4.3 - oxygen acceptor
1.4.4 - disulfide acceptor
1.4.99 - other acceptors
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