The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

LOX  -  lysyl oxidase

Bos taurus

Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of LOX


High impact information on LOX


Biological context of LOX


Anatomical context of LOX

  • Accelerated calcification represses the expression of elastic fiber components and lysyl oxidase in cultured bovine aortic smooth muscle cells [10].
  • The addition of LO to VSMC elevated the levels of intracellular H(2)O(2), enhanced stress fiber formation, and focal adhesion assembly, is consistent with the induction of the chemotactic response [6].
  • In vitro transcription of the cloned lysyl oxidase cDNA and cell-free translation of its mRNA transcript yielded a 47-kDa protein in the absence and a 50-kDa glycosylated protein in the presence of pancreatic membranes, each of which were immunoprecipitated with antibody against the 32-kDa bovine enzyme [11].
  • A possible pathway by which LO can enter cell nuclei was explored in the present study [12].
  • Primary bovine chondrocytes were seeded in alginate and collagen synthesis was assessed in the presence and absence of beta-aminopropronitrile (BAPN), a potent inhibitor of the enzyme lysyl oxidase and collagen cross-link formation [13].

Associations of LOX with chemical compounds


Other interactions of LOX

  • TE, FBN1, and LO mRNA levels, assessed by reverse transcription-polymerase chain reaction, were also decreased by exposure to 10 mM beta-GP [10].
  • Such stereospecificity and proton exchange uniquely differentiates lysyl oxidase from all but an aortic semicarbazide-sensitive amine oxidase among the pro-S-specific copper-dependent amine oxidases analyzed thus far [9].
  • These results suggest that heparin may modulate the oxidation and thus the insolubilization of extracellular collagen fibers, possibly under conditions where elastin fiber synthesis is not affected, and that the tight binding of lysyl oxidase to collagen is not completely related to the expression of enzyme activity toward this substrate [17].
  • Special reference is made to cytochrome c oxidase, lysyl oxidase, superoxide dismutase and endoplasmic reticulum enzymes and to their role in the expression of disease [18].

Analytical, diagnostic and therapeutic context of LOX

  • Northern blots screened with lysyl oxidase cDNA probes identified hybridizing species of 5.8 and 4.5 kb in mRNA of rat aorta and lung, while dot blot analyses were negative for lysyl oxidase mRNA in preparations of rat brain, liver, kidney, and heart [5].
  • Although this domain contains the characteristic paired lysine residues found in other cross-linking domains of elastin, protein sequence analysis indicated that the first but not the second lysine had been oxidized by lysyl oxidase [14].
  • Evidence for pyrroloquinolinequinone as the carbonyl cofactor in lysyl oxidase by absorption and resonance Raman spectroscopy [19].
  • Such similarity also exists between the peptide maps of the aortic enzyme and the urea-extractable lysyl oxidase of bovine cartilage, as well as with the peptide maps of a catalytically quiescent protein resolved from the aortic enzyme by gel exclusion chromatography [20].
  • Lysyl oxidase mRNA expression was investigated with semi-quantitative RT-PCR, whilst expression of cytochrome P450 17alpha-hydroxylase and cytochrome P450 side-chain cleavage mRNA was examined using real time PCR [21].


  1. Irreversible inhibition of lysyl oxidase by homocysteine thiolactone and its selenium and oxygen analogues. Implications for homocystinuria. Liu, G., Nellaiappan, K., Kagan, H.M. J. Biol. Chem. (1997) [Pubmed]
  2. A crosslinked cofactor in lysyl oxidase: redox function for amino acid side chains. Wang, S.X., Mure, M., Medzihradszky, K.F., Burlingame, A.L., Brown, D.E., Dooley, D.M., Smith, A.J., Kagan, H.M., Klinman, J.P. Science (1996) [Pubmed]
  3. Ultrastructural immunolocalization of lysyl oxidase in vascular connective tissue. Kagan, H.M., Vaccaro, C.A., Bronson, R.E., Tang, S.S., Brody, J.S. J. Cell Biol. (1986) [Pubmed]
  4. Characterization of the native lysine tyrosylquinone cofactor in lysyl oxidase by Raman spectroscopy. Wang, S.X., Nakamura, N., Mure, M., Klinman, J.P., Sanders-Loehr, J. J. Biol. Chem. (1997) [Pubmed]
  5. Cloning of rat aorta lysyl oxidase cDNA: complete codons and predicted amino acid sequence. Trackman, P.C., Pratt, A.M., Wolanski, A., Tang, S.S., Offner, G.D., Troxler, R.F., Kagan, H.M. Biochemistry (1990) [Pubmed]
  6. Hydrogen peroxide-mediated, lysyl oxidase-dependent chemotaxis of vascular smooth muscle cells. Li, W., Liu, G., Chou, I.N., Kagan, H.M. J. Cell. Biochem. (2000) [Pubmed]
  7. Modulation of lysyl oxidase substrate specificity by the oleate anion. Losty, T.A., Miller, D.S., O'Dell, B.L. Proc. Soc. Exp. Biol. Med. (1985) [Pubmed]
  8. High-performance liquid chromatographic quantification of allysine as bis-p-cresol derivative in elastin. Umeda, H., Kawamorita, K., Suyama, K. Amino Acids (2001) [Pubmed]
  9. Kinetics and stereospecificity of the lysyl oxidase reaction. Shah, M.A., Scaman, C.H., Palcic, M.M., Kagan, H.M. J. Biol. Chem. (1993) [Pubmed]
  10. Accelerated calcification represses the expression of elastic fiber components and lysyl oxidase in cultured bovine aortic smooth muscle cells. Sugitani, H., Wachi, H., Mecham, R.P., Seyama, Y. J. Atheroscler. Thromb. (2002) [Pubmed]
  11. Post-translational glycosylation and proteolytic processing of a lysyl oxidase precursor. Trackman, P.C., Bedell-Hogan, D., Tang, J., Kagan, H.M. J. Biol. Chem. (1992) [Pubmed]
  12. Fully processed lysyl oxidase catalyst translocates from the extracellular space into nuclei of aortic smooth-muscle cells. Nellaiappan, K., Risitano, A., Liu, G., Nicklas, G., Kagan, H.M. J. Cell. Biochem. (2000) [Pubmed]
  13. Collagen fibrillogenesis by chondrocytes in alginate. Wong, M., Siegrist, M., Gaschen, V., Park, Y., Graber, W., Studer, D. Tissue engineering. (2002) [Pubmed]
  14. Identification of an elastin cross-linking domain that joins three peptide chains. Possible role in nucleated assembly. Brown-Augsburger, P., Tisdale, C., Broekelmann, T., Sloan, C., Mecham, R.P. J. Biol. Chem. (1995) [Pubmed]
  15. Beta-substituted ethylamine derivatives as suicide inhibitors of lysyl oxidase. Tang, S.S., Simpson, D.E., Kagan, H.M. J. Biol. Chem. (1984) [Pubmed]
  16. Reaction of lysyl oxidase with trans-2-phenylcyclopropylamine. Shah, M.A., Trackman, P.C., Gallop, P.M., Kagan, H.M. J. Biol. Chem. (1993) [Pubmed]
  17. Inhibition by heparin of the oxidation of lysine in collagen by lysyl oxidase. Gavriel, P., Kagan, H.M. Biochemistry (1988) [Pubmed]
  18. Copper deficiency in ruminants. McMurray, C.H. Ciba Found. Symp. (1980) [Pubmed]
  19. Evidence for pyrroloquinolinequinone as the carbonyl cofactor in lysyl oxidase by absorption and resonance Raman spectroscopy. Williamson, P.R., Moog, R.S., Dooley, D.M., Kagan, H.M. J. Biol. Chem. (1986) [Pubmed]
  20. Evidence for structural similarities in the multiple forms of aortic and cartilage lysyl oxidase and a catalytically quiescent aortic protein. Sullivan, K.A., Kagan, H.M. J. Biol. Chem. (1982) [Pubmed]
  21. Effect of copper and thiomolybdates on bovine theca cell differentiation in vitro. Kendall, N.R., Marsters, P., Guo, L., Scaramuzzi, R.J., Campbell, B.K. J. Endocrinol. (2006) [Pubmed]
WikiGenes - Universities