Lysyl oxidase: Properties, regulation and multiple functions in biology

Matrix Biology

Volumn 16, Issue 7, 1998, Pages 387-398

  Smith Mungo, Lynda I ^a   Kagan, Herbert M ^a  

^a BOSTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINE OXIDASE (FLAVIN CONTAINING); ANGIOTENSIN; COLLAGEN; COPPER; ELASTIN; ENZYME PRECURSOR; FIBROBLAST GROWTH FACTOR; GLYCOSYLATED PROTEIN; PLATELET DERIVED GROWTH FACTOR; PROTEIN LYSINE 6 OXIDASE; RETINOIC ACID; SCLEROPROTEIN; TRANSFORMING GROWTH FACTOR BETA;

CONNECTIVE TISSUE; COPPER METABOLISM; ENZYME MECHANISM; ENZYME REGULATION; ENZYME RELEASE; ENZYME SYNTHESIS; FIBROSIS; GENE; MOLECULAR CLONING; PRIORITY JOURNAL; PROTEIN CROSS LINKING; REVIEW; SERUM; SHEAR STRESS;

SIGANUS;

EID: 0031893071     PISSN: 0945053X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0945-053X(98)90012-9     Document Type: Short Survey

References (79)

1. Ando, J., Tsuboi, H., Korenaga, R., Takahashi, K., Kosaki, K., Isshiki, M., Tojo, T., Takada, Y. and Kamiya, A.: Differential display and cloning of shear stress-responsive messenger RNAs in human endothelial cells. Biochem. Biophys. Res. Commun. 225: 347-351, 1996.
2. Boak, A.M., Roy, R., Berk, J., Taylor, L., Polgar, P., Goldstein, R H. and Kagan, H.M.: Regulation of lysyl oxidase expression in lung fibroblasts by transforming growth factor-beta 1 and prostaglandin E2. Am. J. Resp. Cell Mol. Biol. 11: 751-755, 1994.
3. Boyd, C.D., Mariani, T. J., Kim, Y. and Csiszar, K.: The size heterogeneity of human lysyl oxidase mRNA is due to alternate polyadenylation site and not alternate exon usage. Mol. Biol. Reports 21: 95-103, 1995.
4. Casey, M.L. and MacDonald, P.C.: Lysyl oxidase (ras recision gene) expression in human amnion: ontogeny and cellular localization. J. Clin. Endocrin. Metab. 82: 167-172, 1997.
5. Chang, Y.S., Svinarich, D.M., Yang, T.P. and Krawetz, S.A.: The mouse lysyl oxidase gene (Lox) resides on chromosome 18. Cytogenet. Cell Genet. 63: 47-49, 1993.
6. Chanoki, M., Ishii, M., Kobayashi, H., Fushida, H., Yashiro, N., Hamada, T. and Ooshima, A.: Increased expression of lysyl oxidase in skin with scleroderma. Br. J. Dermatol. 133: 710-715, 1995.
7. Contente, S., Csiszar, K., Kenyon, K. and Friedman, R.M.: Structure of the mouse lysyl oxidase gene. Genomics 16: 395-400, 1993.
8. Contente, S., Kenyon, K., Rimoldi, D. and Friedman, R.M.: Expression of gene rrg is associated with reversion of NIH 3T3 transformed by LTR-c-H-ras. Science 249: 796-798, 1990.
9. Cronshaw, A.D., Fothergill-Gilmore, L.A. and Hulmes, D.J.S.: The proteolytic prosessing of the precursor of LO. Biochem. J. 306: 279-284, 1995.
10. Csiszar, K., Entersz, I., Trackman, P.C., Samid, D. and Boyd, C.D.: Functional analysis of the promoter and first intron of the human lysyl oxidase gene. Mol. Biol. Reports 23: 97-108, 1996.
11. Davidson, J.M., Zoia, O. and Liu, J.M.: Modulation of transforming growth factor-β1 stimulated elastin and collagen production and proliferation in porcine vascular smooth muscle cells and skin fibroblasts by basic fibroblast growth factor-α and insulin-like growth factor-I. J. Cell. Phys. 155: 149-156, 1993.
12. Dimaculangan, D.D., Chawla, A., Boak, A., Kagan, H.M. and Lazar, M.A.: Retinoic acid prevents downregulation of ras recision gene/lysyl oxidase early in adipocyte differentiation. Differentiation 58: 47-52, 1994.
13. Dove, J.E., Smith, A.J.,. Kuchar, J., Brown, D.E., Dooley, D.M. and Klinman, J.P.: Identification of the quinone cofactor in a lysyl oxidase from Pichia pastoris. FEBS Lett. 398: 231-234, 1996.
14. Feres-Filho, E.J., Choi, Y.J., Han, X., Takala, T.E. and Trackman, P.C.: Pre- and post-translational regulation of lysyl oxidase by transforming growth factor-beta 1 in osteoblastic MC3T3-E1 cells. J. Biol. Chem. 270: 30797-30803, 1995.
15. Feres-Filho, E. ., Menassa, G.B. and Trackman, P.C.: Regulation of lysyl oxidase by basic fibroblast growth factor in osteoblastic MC3T3-E1 cells. J. Biol. Chem. 271: 6411-6416, 1996.
16. Gacheru, S., McGee, C., Uriu-Hare, J.Y., Kosonen, T., Packman, S., Tinker, D., Krawetz, S.A., Reiser, K., Keen, C.L. and Rucker, R.B.: Expression and accumulation of LO, elastin, and type I procollagen in human Menkes and mottled mouse fibroblasts. Arch. Biochem. Biophys. 301: 325-329, 1993.
17. Gacheru, S.N., Thomas, K.M., Murray, S.A., Csiszar, K., Smith-Mungo, L.I. and Kagan, H. M.: Transcriptional and post-transcriptional control of lysyl oxidase expression in vascular smooth muscle cells: effects of TGF-beta 1 and serum deprivation. J. Cell. Biochem. 65: 395-407, 1997.
18. Gacheru, S.N., Trackman, P.C. and Kagan, H.M.: Evidence for a functional role for histidine in lysyl oxidase catalysis. J. Biol. Chem. 263: 16704-16708, 1988.
19. Gacheru, S.N., Trackman, P.C., Shah, M.A., O'Gara, C.Y., Spacciapoli, P., Greenaway, F.T. and Kagan, H.M.: Structural and catalytic properties of copper in lysyl oxidase. J. Biol. Chem 265: 19022-19027, 1990.
20. Green, R.S., Lieb, M.E., Weintraub, A.S., Gacheru, S.N., Rosenfield, C.L., Shah, S., Kagan, H.M. and Taubman, M.B.: Identification of lysyl oxidase and other platelet-derived growth factor-inducible genes in vascular smooth muscle cells by differential screening. Lab. Invest. 73: 476-482, 1995.
21. Hamalainen, E.-R., Jones, T.A., Sheer, D., Taskinen, K., Pihlajaniemi, T. and Kivirikko, K.: Molecular cloning of human lysyl oxidase and assignment of the gene to chromosome 5q23.3-31.2. Genomics 11: 508-516, 1991.
22. Hamalainen, E.R., Kemppainen, R., Kuivaniemi, H., Tromp, G., Vaheri, A., Pihlajaniemi, T. and Kivirikko, K.I.: Quantitative polymerase chain reaction of lysyl oxidase mRNA in malignantly transformed human cell lines demonstrates that their low lysyl oxidase activity is due to low quantities of its mRNA and low levels of transcription of the respective gene. J. Biol. Chem. 270: 21590-21593, 1995.
23. Hamalainen, E.-R., Kemppainen, R., Pihlajaniemi, T. and Kivirikko, K.: Structure of the human lysyl oxidase gene. Genomics 17: 544-548, 1993.
24. Janes, S.M., Palcic, M.M., Seaman, C.H., Smith, A.J., Brown, D.E., Dooley, D.M., Mure, M. and Klinman, J.P.: Identification of topaquinone and its consensus sequence in copper amine oxidases. Biochemistry 31: 12147-12147, 1992.
25. Jourdan-Le Saux, C., Gleyzal, C., Garnier, J.M., Peraldi, M., Sommer, P. and Grimaud, J.A.: Lysyl oxidase cDNA of myofibroblast from mouse fibrotic liver. Biochem. Biophys. Res. Commun. 199: 587-592, 1994.
26. Jourdan-LeSaux, C., Gleyzal, C., Raccurt, M. and Sommer, P.: Functional analysis of the lysyl oxidase promoter in myofibroblast-like clones of 3T6 fibroblast. J. Cell. Biochem. 64: 328-341, 1997.
27. Kagan, H.M.: Characterization and regulation of LO. In: Biology of the Extracellular Matrix, ed. by Mecham, R.P., Vol 1: Regulation of Matrix Accumulation, Academic Press, Orlando, FL, 1986, pp: 321-398.
28. Kagan, H.M., Reddy, V.B., Narasimhan, N. and Csizsar, K.: Catalytic properties and structural components of LO. In: The Molecular Biology and Pathology of Elastic Tissues, Wiley, Chichester (Ciba Foundation Symposium 192), 1995a, pp. 100-121.
29. Kagan, H.M., Reddy, V.B., Panchenko, M., Thomas, K., Narasimhan, N., Boak, A.M. and Gacheru, S.N.: Expression of lysyl oxidase from cDNA constructs in mammalian cells: The propeptide region is not essential to the folding and secretion of the functional enzyme. J. Cell. Biochem. 58: 1-10, 1995b.
30. Kagan, H.M. and Trackman, P.C.: Properties and function of LO. Am. J. Resp. Cell Mol. Biol. 5: 206-210, 1991.
31. Kagan, H.M., Williams, M.A., Williamson, P.R. and Anderson, J.M.: Influence of sequence and charge on the specificity of lysyl oxidase toward protein and synthetic peptide substrates. J. Biol. Chem. 259: 11203-11207, 1984.
32. Kemppainen, R., Hamalainen, E.R., Kuivaniemi, H., Tromp, G., Pihlajaniemi, T. and Kivirikko, K.I.: Expression of mRNAs for lysyl oxidase and type III procollagen in cultured fibroblasts from patients with the Menkes and occipital horn syndromes as determined by quantitative polymerase chain reaction. Arch. Biochem. Biophys. 328: 101-106, 1996.
33. Kenyon, K., Contente, S., Trackman, P.C., Tang, J., Kagan, H. and Friedman, R.M.: A suppressor of the phenotypic expression of ras encodes lysyl oxidase. Science 253: 802, 1991.
34. Kenyon, K., Modi, W.S., Contente, S. and Friedman, R.M.: A novel human cDNA with a predicted protein similar to lysyl oxidase maps to chromosome 15q24-q25. J. Biol. Chem. 268: 18435-18437, 1993.
35. Khakoo, A., Thomas, R., Trompeter, R., Duffy, P., Price, R. and Pope, F.M.: Congenital cutis laxa and lysyl oxidase deficiency. Clin. Genet. 51: 109-114, 1997.
36. Kim, Y., Boyd, C.D. and Csiszar, K.: A new gene with sequence and structural similarity to the gene encoding human lysyl oxidase. J. Biol. Chem. 270: 7176-7182, 1995.
37. Kuivaniemi, H., Korhonen, R.M., Vaheri, A. and Kivirikko, K.I.: Deficient production of lysyl oxidase in cultures of malignantly transformed human cells. FEBS Lett. 195: 261-264, 1986.
38. Lawrence, R., Hartmann, D.J. and Sonenshein, G.E.: Transforming growth factor-β1 stimulates type V collagen expression in bovine vascular smooth muscle cells. J. Biol. Chem. 269: 9603-9609, 1994.
39. Lazarus, H.M., Cruikshank, W.W., Narasimhan, N., Kagan, H.M. and Center, D M.: Induction of human monocyte motility by LO. Matrix Biol. 14: 727-731, 1995.
40. Li, W., Chou, I.N., Boak, A. and Kagan, H.M.: Downregulation of lysyl oxidase in cadmium-resistant fibroblasts. Am. J. Respir. Cell Molec. Biol. 13: 418-425, 1995.
41. Li, W., Nellaiappan, K., Strassmaier, T., Graham, L., Thomas, K.M. and Kagan, H.M.: Localization and activity of lysyl oxidase within nuclei of fibrogenic cells. Proc. Natl. Acad. Sci. USA, 94: 12817-12822, 1997.
42. Lossie, A.C., Buckwalter, M.S. and Camper, S.A.: Lysyl oxidase (Lox) maps between Grl-1 and Adrb-2 on mouse chromosome 18. Mamm. Genome 4: 177-178, 1993.
43. Mariani, T.J., Trackman, P.C., Kagan, H.M., Eddy, R.L., Shows, T.B., Boyd, C.D. and Deak, S.B.: 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: 242-248, 1992.
44. Massagué, J., Attisano, L. and Wrana, J.L.: The TGF-β family and its composite receptors. Trends Cell Biol. 4: 172-177, 1994.
45. Matsuzaki, R., Fukui, T., Sato, H., Ozaki, Y. and Tanizawa, K.: Generation of the topa quinone cofactor in bacterial monoamine oxidase by cupric ion-dependent autooxidation of a specific tyrosyl residue. FEBS Lett. 351: 360-364, 1994.
46. Mello, M.L., Contente, S., Vidai, B.C., Planding, W. and Schenck, U.: Modulation of ras transformation affecting chromatin supraorganization as assessed by image analysis. Exp. Cell Res. 220: 374-382, 1995.
47. Mello, M.L.S. and Russo, J.: Image analysis of Feulgen-stained c-H-ras-transformed NIH/3T3 cells. Biochem. Cell Biol. 68: 1026-1031, 1990.
48. Mock, B.A., Contente, S., Kenyon, K., Friedman, R.M. and Kozak C.A.: The gene for lysyl oxidase maps to mouse chromosome 18. Genomics 14: 822-823, 1992.
49. Nagan, N. and Kagan, H.M.: Modulation of lysyl oxidase activity toward peptidyl lysine by vicinal dicarboxylic amino acid residues. Implications for collagen crosslinking. J. Biol. Chem. 269: 22366-22371, 1994.
50. Ouzzine, M., Boyd, A. and Hulmes, D.J.: Expression of active, human lysyl oxidase in Escherichia coli. FEBS Lett. 399: 215-219, 1996
51. Panchenko M.V., Stetler-Stevenson, W.G., Trubetskoy, O.V., Gacheru, S.N. and Kagan, H.M.: Metalloproteinase activity secreted by fibrogenic cells in the processing of prolysyl oxidase. Potential role of procollagen C-proteinase. J. Biol. Chem. 271: 7113-7119, 1996.
52. Peyrol, S., Raccurt, M., Gerard, F., Gleyzal, C. Grimaud, J.A. and Sommer, P.: Lysyl oxidase gene expression in the stromal reaction to in situ and invasive ductal breast carcinoma. Am. J. Path. 150: 497-507, 1997.
53. Pinnell, S.R. and Martin, G.R.: The cross-linking of collagen and elastin: enzymatic conversion of lysine in peptide linkage to a-aminoadipic-d-semialdehyde (allysine) by an extract from bone. Proc. Natl. Acad. Sci. USA 61: 708-714, 1968.
54. Quaglino, D., Fornieri, C., Nanney, L.B. and Davidson, J.M.: Extracellular matrix modifications in rat tissues of different ages. Correlations between elastin and collagen type I mRNA expression and lysyl-oxidase activity. Matrix 13: 481-490, 1993.
55. Ritzenthaler, J.D., Goldstein, R.H., Fine, A., Lichtler, A., Rowe, D.W. and Smith, B.D.: Transforming growth factor B activation elements in the distal promoter regions of the rat a 1 type I collagen gene. Biochem. J. 280: 157-162, 1991.
56. Rossi, P., Karsenty, G., Roberts, A.B., Roche, N.S., Sporn, M.B. and de Crombrugghe, B.: A nuclear factor 1 binding site mediates the transcriptional activation of a type I collagen promoter by transforming growth factor B. Cell 52: 405-414, 1988.
57. Roy, R., Polgar, P., Wang, Y., Goldstein, R.H., Taylor, L. and Kagan, H.M.: Regulation of lysyl oxidase and cyclooxygenase expression in human lung fibroblasts: interactions among TGF-β, IL-1β, and prostaglandin E. J. Cell. Biochem. 62: 411-417, 1996.
58. Rucker, R.B., Romero-Chapman, N., Wong, T., Lee, J., Steinberg, F.M., McGee, C., Clegg, M.S., Reiser, K., Kosonen, T., Uriu-Hare, J.Y., Murphy, J. and Keen, C.L.: Modulation of lysyl oxidase by dietary copper in rats. J. Nutr. 126: 51-60, 1996.
59. Saito, H., Papaconstantinou, J., Sato, H. and Goldstein, S.: Regulation of a novel gene encoding a lysyl oxidase-related protein in cellular adhesion and senescence. J. Biol. Chem. 272: 8157-8160, 1997.
60. 2 aerosol. Am. Rev. Resp. Dis. 129: 619-624, 1984.
61. Shah, M.A., Seaman, C.H., Palcic, M.M. and Kagan, H.M.: Kinetics and stereospecificity of the lysyl oxidase reaction. J. Biol. Chem. 268: 11573-11579, 1993.
62. Stanley, C.J., Gharaee-Kermani, M., Sarkar, R., Welling, T.H., Kriegel, A., Ford, J.W., Stanley, J.C. and Phan, S.H.: Transforming growth factor-beta 1 increases lysyl oxidase enzyme activity and mRNA in rat aortic smooth muscle cells. J. Vasc. Surg. 25: 446-452, 1997.
63. Siegel, R.C.: Biosynthesis of collagen crosslinks: increased activity of purified lysyl oxidase with reconstituted collagen fibrils. Proc. Natl. Acad. Sci. USA 71: 4826-4830, 1974.
64. Sommer, P., Gleyzal, C., Raccurt, M., Delbourg, M., Serrar, M., Joazeiro, P., Peyrol, S., Kagan, H., Trackman, P.C. and Grimaud, J.A.: Transient expression of lysyl oxidase by liver myofibroblasts in murine schistosomiasis. Lab. Invest. 69: 460-470, 1993.
65. Svinarich, D.M., Twomey, T.A., Macauley, S.P., Krebs, C.J., Yang, T.P. and Krawetz, S.A.: Characterization of the human lysyl oxidase gene locus. J. Biol. Chem. 267: 14382-14387, 1992.
66. Tan, R.S.-P., Taniguchi, T. and Harada, H.: Identification of the lysyl oxidase gene as target of the antioncogenic transcription factor, IRE-1, and its possible role in tumor suppression. Canc. Res. 56: 2417-2421, 1996.
67. Trackman, P.C., Bedell-Hogan, D., Tang, J. and Kagan, H.M.: Post-translational glycosylation and proteolytic processing of a lysyl oxidase precursor. J. Biol. Chem. 267: 8666-8671, 1992.
68. Trackman, P.C., Pratt, A.M., Wolanski, A., Tang, S.-S., Offner, G.D., Troxler, R. and Kagan, H.: Cloning of rat aorta lysyl oxidase cDNA: complete codons and predicted amino acid sequence. Biochemistry 29: 4863-4870, 1990.
69. Trackman, P.C., Pratt, A.M., Wolanski, A., Tang, S.-S., Offner, G.D., Troxler, R. and Kagan, H.: Cloning of rat aorta lysyl oxidase cDNA: complete codons and predicted amino acid sequence. Biochemistry 30: 8282, 1991.
70. Vulpe, C., Levinson, B., Whitney, S., Packman, S. and Gitschier, J.: Isolation of a candidate gene for Menkes disease and evidence that it encodes a copper-transporting ATPase. Nat. Genet. 3: 7-13, 1993.
71. Wakasaki, H. and Ooshima, A.: Immunohistochemical localization of lysyl oxidase with monoclonal antibodies. Lab. Invest. 63: 377-384, 1990.
72. Wang, S.X., Mure, M., Medzihradszky, K.F., Burlingame, A.L., Brown, D., Dooley, D.M., Smith, A.J., Kagan, H.M. and Klinman, J.P.: A crosslinked cofactor in LO: redox function for amino acid side chains. Science 273: 1078-1064, 1996.
73. Werman, M.J., Barat, E. and Bhathena, S.J.: Gender, dietary copper and carbohydrate source influence cardiac collagen and lysyl oxidase in weanling rats. J. Nutr. 125: 857-863, 1995.
74. Williamson, P.R. and Kagan H.M.: Reaction pathway of bovine aortic LO. J. Biol. Chem. 261: 9477-9482, 1986.
75. Williamson, P.R. and Kagan, H.M.: a-Proton abstraction and carbanion formation in the mechanism of action of LO. J. Biol. Chem. 262: 8196-8201, 1987.
76. Wolffe, A.P.: Histone deacetylase- a regulator of transcription. Science 272: 371-372, 1996.
77. Wu, Y., Rich, C.B., Lincecum, J., Trackman, P.C., Kagan, H.M. and Foster, J.A.: Characterization and developmental expression of chick aortic LO. J. Biol. Chem. 267: 24199-24206, 1992.
78. Yeowell, H.N., Marshall, M.K., Walker, L.C., Ha, V. and Pinnell, S.R.: Regulation of lysyl oxidase mRNA in dermal fibroblasts from normal donors and patients with inherited connective tissue disorders. Arch. Biochem. Biophys. 308: 299-305, 1994.
79. Zhu, L., Dagher, E., Johnson, D.J., Bedell-Hogan, D., Keeley, F.W., Kagan, H.M. and Rabinovitch, M.: A developmentally regulated program restricting insolubilization of elastin and formation of laminae in the fetal lamb ductus arteriosus. Lab. Invest. 68: 321-331, 1993.