- Lysyl oxidase
Lysyl oxidase, also known as LOX, is a human
gene .cite web | title = Entrez Gene: LOX lysyl oxidase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4015| accessdate = ]PBB_Summary
section_title =
summary_text = 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.cite web | title = Entrez Gene: LOX lysyl oxidase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4015| accessdate = ]Lysyl oxidase is an extracellular
enzyme that catalyzes formation ofaldehydes fromlysine residues incollagen andelastin 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 incross-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 aorticaneurysms . These abnormalities correlated well with decreased cross-linking of collagen and elastin.ee also
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oxidase References
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Further reading
PBB_Further_reading
citations =
*cite journal | author=Csiszar K |title=Lysyl oxidases: a novel multifunctional amine oxidase family. |journal=Prog. Nucleic Acid Res. Mol. Biol. |volume=70 |issue= |pages= 1–32 |year= 2001 |pmid= 11642359 |doi=
*cite journal | author=Kagan HM, Li W |title=Lysyl oxidase: properties, specificity, and biological roles inside and outside of the cell. |journal=J. Cell. Biochem. |volume=88 |issue= 4 |pages= 660–72 |year= 2003 |pmid= 12577300 |doi= 10.1002/jcb.10413
*cite journal | author=Svinarich DM, Twomey TA, Macauley SP, "et al." |title=Characterization of the human lysyl oxidase gene locus. |journal=J. Biol. Chem. |volume=267 |issue= 20 |pages= 14382–7 |year= 1992 |pmid= 1352776 |doi=
*cite journal | author=Mariani TJ, Trackman PC, Kagan HM, "et al." |title=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). |journal=Matrix |volume=12 |issue= 3 |pages= 242–8 |year= 1992 |pmid= 1357535 |doi=
*cite journal | author=Murawaki Y, Kusakabe Y, Hirayama C |title=Serum lysyl oxidase activity in chronic liver disease in comparison with serum levels of prolyl hydroxylase and laminin. |journal=Hepatology |volume=14 |issue= 6 |pages= 1167–73 |year= 1992 |pmid= 1683640 |doi=
*cite journal | author=Hämäläinen ER, Jones TA, Sheer D, "et al." |title=Molecular cloning of human lysyl oxidase and assignment of the gene to chromosome 5q23.3-31.2. |journal=Genomics |volume=11 |issue= 3 |pages= 508–16 |year= 1992 |pmid= 1685472 |doi=
*cite journal | author=Konishi A, Iguchi H, Ochi J, "et al." |title=Increased lysyl oxidase activity in culture medium of nonparenchymal cells from fibrotic livers. |journal=Gastroenterology |volume=89 |issue= 4 |pages= 709–15 |year= 1985 |pmid= 2863189 |doi=
*cite journal | author=Kuivaniemi H, Ala-Kokko L, Kivirikko KI |title=Secretion of lysyl oxidase by cultured human skin fibroblasts and effects of monensin, nigericin, tunicamycin and colchicine. |journal=Biochim. Biophys. Acta |volume=883 |issue= 2 |pages= 326–34 |year= 1986 |pmid= 2874833 |doi=
*cite journal | author=Reiser KM, Hennessy SM, Last JA |title=Analysis of age-associated changes in collagen crosslinking in the skin and lung in monkeys and rats. |journal=Biochim. Biophys. Acta |volume=926 |issue= 3 |pages= 339–48 |year= 1988 |pmid= 3120785 |doi=
*cite journal | author=Järveläinen H, Halme T, Rönnemaa T |title=Effect of cortisol on the proliferation and protein synthesis of human aortic smooth muscle cells in culture. |journal=Acta Med. Scand. Suppl. |volume=660 |issue= |pages= 114–22 |year= 1982 |pmid= 6127904 |doi=
*cite journal | author=Kuivaniemi H, Savolainen ER, Kivirikko KI |title=Human placental lysyl oxidase. Purification, partial characterization, and preparation of two specific antisera to the enzyme. |journal=J. Biol. Chem. |volume=259 |issue= 11 |pages= 6996–7002 |year= 1984 |pmid= 6144680 |doi=
*cite journal | author=Lien YH, Stern R, Fu JC, Siegel RC |title=Inhibition of collagen fibril formation in vitro and subsequent cross-linking by glucose. |journal=Science |volume=225 |issue= 4669 |pages= 1489–91 |year= 1984 |pmid= 6147899 |doi=
*cite journal | author=Yasutake A, Powers JC |title=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. |journal=Biochemistry |volume=20 |issue= 13 |pages= 3675–9 |year= 1981 |pmid= 6912069 |doi=
*cite journal | author=Kim Y, Boyd CD, Csiszar K |title=A new gene with sequence and structural similarity to the gene encoding human lysyl oxidase. |journal=J. Biol. Chem. |volume=270 |issue= 13 |pages= 7176–82 |year= 1995 |pmid= 7706256 |doi=
*cite journal | author=Hämäläinen ER, Kemppainen R, Pihlajaniemi T, Kivirikko KI |title=Structure of the human lysyl oxidase gene. |journal=Genomics |volume=17 |issue= 3 |pages= 544–8 |year= 1993 |pmid= 7902322 |doi= 10.1006/geno.1993.1369
*cite journal | author=Forbes EG, Cronshaw AD, MacBeath JR, Hulmes DJ |title=Tyrosine-rich acidic matrix protein (TRAMP) is a tyrosine-sulphated and widely distributed protein of the extracellular matrix. |journal=FEBS Lett. |volume=351 |issue= 3 |pages= 433–6 |year= 1994 |pmid= 8082810 |doi=
*cite journal | author=Csiszar K, Mariani TJ, Gosin JS, "et al." |title=A restriction fragment length polymorphism results in a nonconservative amino acid substitution encoded within the first exon of the human lysyl oxidase gene. |journal=Genomics |volume=16 |issue= 2 |pages= 401–6 |year= 1993 |pmid= 8100215 |doi= 10.1006/geno.1993.1203
*cite journal | author=Vetter U, Weis MA, Mörike M, "et al." |title=Collagen crosslinks and mineral crystallinity in bone of patients with osteogenesis imperfecta. |journal=J. Bone Miner. Res. |volume=8 |issue= 2 |pages= 133–7 |year= 1993 |pmid= 8442432 |doi=
*cite journal | author=Panchenko MV, Stetler-Stevenson WG, Trubetskoy OV, "et al." |title=Metalloproteinase activity secreted by fibrogenic cells in the processing of prolysyl oxidase. Potential role of procollagen C-proteinase. |journal=J. Biol. Chem. |volume=271 |issue= 12 |pages= 7113–9 |year= 1996 |pmid= 8636146 |doi=
*cite journal | author=Khakoo A, Thomas R, Trompeter R, "et al." |title=Congenital cutis laxa and lysyl oxidase deficiency. |journal=Clin. Genet. |volume=51 |issue= 2 |pages= 109–14 |year= 1997 |pmid= 9111998 |doi=External links
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