AOC3

From Wikipedia, the free encyclopedia

Amine oxidase, copper containing 3 (vascular adhesion protein 1)

PDB rendering based on 1pu4.

Available structures: 1pu4, 1us1, 2c10, 2c11

Identifiers

Symbol(s)

AOC3; HPAO; SSAO; VAP-1; VAP1

External IDs

OMIM: 603735 MGI: 1306797 HomoloGene: 2770

Gene ontology
Molecular Function:	• copper ion binding • calcium ion binding • protein binding • amine oxidase activity • oxidoreductase activity • protein homodimerization activity • quinone binding
Cellular Component:	• plasma membrane • cell surface • integral to membrane
Biological Process:	• electron transport • inflammatory response • cell adhesion • amine metabolic process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

n/a

n/a

Refseq

NM_003734 (mRNA)
NP_003725 (protein)

NM_009675 (mRNA)
NP_033805 (protein)

Location

Chr 17: 38.26 - 38.26 Mb

n/a

Pubmed search

[1]

[2]

Amine oxidase, copper containing 3 (vascular adhesion protein 1), also known as AOC3, is a human gene.^[1]

Copper amine oxidases catalyze the oxidative conversion of amines to aldehydes in the presence of copper and quinone cofactor. The product is a major protein on the adipocyte plasma membrane. It has adhesive properties and also has functional monoamine oxidase activity. A pseudogene for this gene has been described and is located approximately 9-kb downstream.^[1]

[edit] References

^ ^a ^b Entrez Gene: AOC3 amine oxidase, copper containing 3 (vascular adhesion protein 1).

[edit] Further reading

Lalor PF, Lai WK, Curbishley SM, et al. (2006). "Human hepatic sinusoidal endothelial cells can be distinguished by expression of phenotypic markers related to their specialised functions in vivo.". World J. Gastroenterol. 12 (34): 5429–39. PMID 17006978.
Bustelo XR, Barbacid M (1992). "Tyrosine phosphorylation of the vav proto-oncogene product in activated B cells.". Science 256 (5060): 1196–9. PMID 1375396.
Andersson B, Wentland MA, Ricafrente JY, et al. (1996). "A "double adaptor" method for improved shotgun library construction.". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
Zhang X, McIntire WS (1997). "Cloning and sequencing of a copper-containing, topa quinone-containing monoamine oxidase from human placenta.". Gene 179 (2): 279–86. PMID 8972912.
Yu W, Andersson B, Worley KC, et al. (1997). "Large-scale concatenation cDNA sequencing.". Genome Res. 7 (4): 353–8. PMID 9110174.
Smith DJ, Salmi M, Bono P, et al. (1998). "Cloning of vascular adhesion protein 1 reveals a novel multifunctional adhesion molecule.". J. Exp. Med. 188 (1): 17–27. PMID 9653080.
Lalor PF, Edwards S, McNab G, et al. (2002). "Vascular adhesion protein-1 mediates adhesion and transmigration of lymphocytes on human hepatic endothelial cells.". J. Immunol. 169 (2): 983–92. PMID 12097405.
Salmi M, Stolen C, Jousilahti P, et al. (2003). "Insulin-regulated increase of soluble vascular adhesion protein-1 in diabetes.". Am. J. Pathol. 161 (6): 2255–62. PMID 12466139.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
Singh B, Tschernig T, van Griensven M, et al. (2003). "Expression of vascular adhesion protein-1 in normal and inflamed mice lungs and normal human lungs.". Virchows Arch. 442 (5): 491–5. doi:10.1007/s00428-003-0802-6. PMID 12700900.
Zhang Q, Mashima Y, Noda S, et al. (2004). "Characterization of AOC2 gene encoding a copper-binding amine oxidase expressed specifically in retina.". Gene 318: 45–53. PMID 14585497.
Conklin DJ, Cowley HR, Wiechmann RJ, et al. (2004). "Vasoactive effects of methylamine in isolated human blood vessels: role of semicarbazide-sensitive amine oxidase, formaldehyde, and hydrogen peroxide.". Am. J. Physiol. Heart Circ. Physiol. 286 (2): H667–76. doi:10.1152/ajpheart.00690.2003. PMID 14715500.
Koskinen K, Vainio PJ, Smith DJ, et al. (2004). "Granulocyte transmigration through the endothelium is regulated by the oxidase activity of vascular adhesion protein-1 (VAP-1).". Blood 103 (9): 3388–95. doi:10.1182/blood-2003-09-3275. PMID 14726375.
Olivé M, Unzeta M, Moreno D, Ferrer I (2004). "Overexpression of semicarbazide-sensitive amine oxidase in human myopathies.". Muscle Nerve 29 (2): 261–6. doi:10.1002/mus.10550. PMID 14755492.
Forster-Horváth C, Döme B, Paku S, et al. (2005). "Loss of vascular adhesion protein-1 expression in intratumoral microvessels of human skin melanoma.". Melanoma Res. 14 (2): 135–40. PMID 15057044.
Aboulaich N, Vainonen JP, Strålfors P, Vener AV (2005). "Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes.". Biochem. J. 383 (Pt 2): 237–48. doi:10.1042/BJ20040647. PMID 15242332.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
Boomsma F, Pedersen-Bjergaard U, Agerholm-Larsen B, et al. (2005). "Association between plasma activities of semicarbazide-sensitive amine oxidase and angiotensin-converting enzyme in patients with type 1 diabetes mellitus.". Diabetologia 48 (5): 1002–7. doi:10.1007/s00125-005-1716-4. PMID 15830186.
Li HY, Lee WJ, Chen MJ, Chuang LM (2005). "Change in vascular adhesion protein-1 and metabolic phenotypes after vertical banded gastroplasty for morbid obesity.". Obes. Res. 13 (5): 855–61. PMID 15919838.
Airenne TT, Nymalm Y, Kidron H, et al. (2005). "Crystal structure of the human vascular adhesion protein-1: unique structural features with functional implications.". Protein Sci. 14 (8): 1964–74. doi:10.1110/ps.051438105. PMID 16046623.