LOXL1

Lysyl oxidase homolog 1, also known as LOXL1, is an enzyme which in humans is encoded by the LOXL1 gene.^[4][5]

LOXL1
Identifiers
Aliases	LOXL1, LOL, LOXL, lysyl oxidase like 1
External IDs	OMIM: 153456 MGI: 106096 HomoloGene: 4074 GeneCards: LOXL1
Gene location (Mouse) Chr. Chromosome 9 (mouse)^[1] Band 9 B|9 31.65 cM Start 58,195,021 bp^[1] End 58,220,469 bp^[1]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in thoracic aorta ascending aorta stromal cell of endometrium right coronary artery urethra left coronary artery saphenous vein retinal pigment epithelium gallbladder anterior pituitary Top expressed in ascending aorta aortic valve calvaria ankle external carotid artery vas deferens body of femur internal carotid artery left lung cervix More reference expression data BioGPS More reference expression data
Gene ontology Molecular function oxidoreductase activity copper ion binding oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor metal ion binding protein-lysine 6-oxidase activity Cellular component cytoplasm extracellular matrix extracellular region basement membrane acrosomal vesicle extracellular space collagen-containing extracellular matrix Biological process protein deamination aorta development response to lipopolysaccharide extracellular matrix organization peptidyl-lysine oxidation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 4016 16949 Ensembl n/a ENSMUSG00000032334 UniProt Q08397 P97873 RefSeq (mRNA) NM_005576 NM_010729 RefSeq (protein) NP_005567 NP_034859 Location (UCSC) n/a Chr 9: 58.2 – 58.22 Mb PubMed search ^[2] ^[3]
Wikidata
View/Edit Human View/Edit Mouse

Function

This gene encodes a member of the lysyl oxidase gene family. The prototypic member of the family is essential to the biogenesis of connective tissue, encoding an extracellular copper-dependent amine oxidase that catalyses the first step in the formation of crosslinks in collagens and elastin. A highly conserved amino acid sequence at the C-terminus end appears to be sufficient for amine oxidase activity, suggesting that each family member may retain this function. The N-terminus is poorly conserved and may impart additional roles in developmental regulation, senescence, tumor suppression, cell growth control, and chemotaxis to each member of the family.^[4]

Clinical significance

Polymorphisms of the LOXL1 gene are associated with pseudoexfoliation syndrome, a disease where the extracellular matrix contains abnormal amounts of cross-linked, amyloid-like fibrillar material and glycoproteins. When this happens in the eye, exfoliation glaucoma results.^[6][7]

Interactions

LOXL1 has been shown to interact with FBLN5.^[8]

See also

• LOXL2
• LOXL3
• LOXL4

References

1. GRCm38: Ensembl release 89: ENSMUSG00000032334 - Ensembl, May 2017
2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
3. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Entrez Gene: LOXL1 lysyl oxidase-like 1".
5. Kenyon K, Modi WS, Contente S, Friedman RM (September 1993). "A novel human cDNA with a predicted protein similar to lysyl oxidase maps to chromosome 15q24-q25". The Journal of Biological Chemistry. 268 (25): 18435–7. doi:10.1016/S0021-9258(17)46643-9. PMID 7689553.
6. Schlötzer-Schrehardt U, Naumann GO (2006). "Ocular and systemic pseudoexfoliation syndrome". Am. J. Ophthalmol. 141 (5): 921–937. doi:10.1016/j.ajo.2006.01.047. PMID 16678509.
7. Thorleifsson G, Magnusson KP, Sulem P, Walters GB, Gudbjartsson DF, Stefansson H, Jonsson T, Jonasdottir A, Jonasdottir A, Stefansdottir G, Masson G, Hardarson GA, Petursson H, Arnarsson A, Motallebipour M, Wallerman O, Wadelius C, Gulcher JR, Thorsteinsdottir U, Kong A, Jonasson F, Stefansson K (2007). "Common sequence variants in the LOXL1 gene confer susceptibility to exfoliation glaucoma". Science. 317 (5843): 1397–400. Bibcode:2007Sci...317.1397T. doi:10.1126/science.1146554. PMID 17690259. S2CID 22289307.
8. Liu X, Zhao Y, Gao J, Pawlyk B, Starcher B, Spencer JA, Yanagisawa H, Zuo J, Li T (Feb 2004). "Elastic fiber homeostasis requires lysyl oxidase-like 1 protein". Nat. Genet. United States. 36 (2): 178–82. doi:10.1038/ng1297. ISSN 1061-4036. PMID 14745449.

Further reading

• Csiszar K (2001). "Lysyl oxidases: a novel multifunctional amine oxidase family". Prog. Nucleic Acid Res. Mol. Biol. Progress in Nucleic Acid Research and Molecular Biology. 70: 1–32. doi:10.1016/S0079-6603(01)70012-8. ISBN 978-0-12-540070-1. 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. S2CID 23651213.
• Molnar J, Fong KS, He QP, Hayashi K, Kim Y, Fong SF, Fogelgren B, Szauter KM, Mink M, Csiszar K (2003). "Structural and functional diversity of lysyl oxidase and the LOX-like proteins". Biochim. Biophys. Acta. 1647 (1–2): 220–4. doi:10.1016/s1570-9639(03)00053-0. PMID 12686136.
• Kenyon K, Modi WS, Contente S, Friedman RM (1993). "A novel human cDNA with a predicted protein similar to lysyl oxidase maps to chromosome 15q24-q25". J. Biol. Chem. 268 (25): 18435–7. doi:10.1016/S0021-9258(17)46643-9. PMID 7689553.
• 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. doi:10.1074/jbc.270.13.7176. PMID 7706256.
• Goy A, Gilles F, Remache Y, Zelenetz AD (2000). "Physical linkage of the lysyl oxidase-like (LOXL1) gene to the PML gene on human chromosome 15q22". Cytogenet. Cell Genet. 88 (1–2): 22–4. doi:10.1159/000015477. PMID 10773658. S2CID 41968837.
• Jung ST, Kim MS, Seo JY, Kim HC, Kim Y (2004). "Purification of enzymatically active human lysyl oxidase and lysyl oxidase-like protein from Escherichia coli inclusion bodies". Protein Expr. Purif. 31 (2): 240–6. doi:10.1016/S1046-5928(03)00217-1. PMID 14550642.
• Liu X, Zhao Y, Gao J, Pawlyk B, Starcher B, Spencer JA, Yanagisawa H, Zuo J, Li T (2004). "Elastic fiber homeostasis requires lysyl oxidase-like 1 protein". Nat. Genet. 36 (2): 178–82. doi:10.1038/ng1297. PMID 14745449.
• Noblesse E, Cenizo V, Bouez C, Borel A, Gleyzal C, Peyrol S, Jacob MP, Sommer P, Damour O (2004). "Lysyl oxidase-like and lysyl oxidase are present in the dermis and epidermis of a skin equivalent and in human skin and are associated to elastic fibers". J. Invest. Dermatol. 122 (3): 621–30. doi:10.1111/j.0022-202X.2004.22330.x. PMID 15086544.
• Thomassin L, Werneck CC, Broekelmann TJ, Gleyzal C, Hornstra IK, Mecham RP, Sommer P (2006). "The Pro-regions of lysyl oxidase and lysyl oxidase-like 1 are required for deposition onto elastic fibers". J. Biol. Chem. 280 (52): 42848–55. doi:10.1074/jbc.M506832200. PMID 16251195.
• Cenizo V, André V, Reymermier C, Sommer P, Damour O, Perrier E (2007). "LOXL as a target to increase the elastin content in adult skin: a dill extract induces the LOXL gene expression". Exp. Dermatol. 15 (8): 574–81. doi:10.1111/j.1600-0625.2006.00442.x. PMID 16842595. S2CID 10622527.
• Thorleifsson G, Magnusson KP, Sulem P, Walters GB, Gudbjartsson DF, Stefansson H, Jonsson T, Jonasdottir A, Jonasdottir A, Stefansdottir G, Masson G, Hardarson GA, Petursson H, Arnarsson A, Motallebipour M, Wallerman O, Wadelius C, Gulcher JR, Thorsteinsdottir U, Kong A, Jonasson F, Stefansson K (2007). "Common sequence variants in the LOXL1 gene confer susceptibility to exfoliation glaucoma". Science. 317 (5843): 1397–400. Bibcode:2007Sci...317.1397T. doi:10.1126/science.1146554. PMID 17690259. S2CID 22289307.
• Damji KF (2007). "Progress in understanding pseudoexfoliation syndrome and pseudoexfoliation-associated glaucoma". Can. J. Ophthalmol. 42 (5): 657–8. doi:10.3129/I07-158. PMID 17891191.