Lysyl oxidase

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 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.

ee also

* 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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