Autotaxin, also known as ENPP-2, is a secreted glycoprotein which belongs to the ectonucleotide pyrophosphatase/phosphodiesterase (NPP) family [1,2]. Generally, NPPs can hydrolyze phosphates from nucleotides. Autotaxin exhibits the unique lysophospholipase D activity [3]. The mature protein includes two somatomedin-B-like (SMB) cysteine knot domains, a catalytic domain, and an inactive C-terminal nuclease-like domain with an EF-hand-like motif that is important in cell motility, and a region involved in autotaxin secretion [1,4,5]. There are three isoforms identified in mouse and human [6,7]. Most circulating autotaxin is the β form which contains 863 amino acid. Autotaxin contributes to the predominant extracellular source of the phospholipid LPA (lysophosphatidic acid) from LPC (lysophosphatidylcholine) [8-11]. Autotaxin can also produce minor amounts of sphingosine 1-phosphate and cyclic phosphatidic acid which can antagonize many of the tumorigenic properties of LPA [9,12].
Autotaxin stimulates tumor cell motility and enhances invasion and metastasis. It’s upregulated in melanoma, glioblastoma, breast and lung carcinoma, follicular lymphoma and other cancers [2,8,11]. Autotaxin production by adipocytes enhances pre-adipocyte proliferation and may be elevated in obesity [11, 13].
Autotaxin is present in blood, urine, saliva, seminal and cerebrospinal fluids [2, 3]. In addition, plasma autotaxin is cleared by the liver which is elevated in liver disease [3, 14]. Normal serum or plasma autotaxin concentration is reported to be slightly higher in females than in males, and highest in pregnant females [2, 14].
REFERENCE
- Cimpean, Anisoara, et al. “Substrate-specifying determinants of the nucleotide pyrophosphatases/phosphodiesterases NPP1 and NPP2.” Biochemical Journal1 (2004): 71-77.
- Okudaira, Shinichi, Hiroshi Yukiura, and Junken Aoki. “Biological roles of lysophosphatidic acid signaling through its production by autotaxin.” Biochimie6 (2010): 698-706.
- Umezu-Goto, Makiko, et al. “Autotaxin has lysophospholipase D activity leading to tumor cell growth and motility by lysophosphatidic acid production.” J cell biol2 (2002): 227-233.
- Hausmann, Jens, et al. “Structural basis of substrate discrimination and integrin
binding by autotaxin.” Nature Structural and Molecular Biology 18.2 (2011): 198.
- Dennis, Jameel, et al. “Phosphodiesterase-Iα/autotaxin’s MORFO domain regulates oligodendroglial process network formation and focal adhesion ” Molecular and Cellular Neuroscience 37.2 (2008): 412-424.
- van Meeteren, Laurens A., and Wouter H. Moolenaar. “Regulation and biological activities of the autotaxin–LPA axis.” Progress in lipid research2 (2007): 145-160.
- Giganti, Adeline, et al. “Murine and Human Autotaxin α, β, and γ Isoforms GENE ORGANIZATION, TISSUE DISTRIBUTION, AND BIOCHEMICAL CHARACTERIZATION.” Journal of Biological Chemistry12 (2008): 7776-7789.
- Gijsbers, Rik, et al. “The hydrolysis of lysophospholipids and nucleotides by autotaxin (NPP2) involves a single catalytic site.” FEBS letters1-3 (2003): 60-64.
- Tsuda, Satomi, et al. “Cyclic phosphatidic acid is produced by autotaxin in
blood.” Journal of Biological Chemistry 281.36 (2006): 26081-26088.
- Ferry, Gilles, et al. “Functional invalidation of the autotaxin gene by a single amino acid mutation in mouse is lethal.” FEBS letters18 (2007): 3572-3578.
- Van Meeteren, Laurens A., et al. “Autotaxin, a secreted lysophospholipase D, is essential for blood vessel formation during development.” Molecular and cellular biology13 (2006): 5015-5022.
- Tania, Mousumi, et al. “Autotaxin: a protein with two faces.” Biochemical and
biophysical research communications 401.4 (2010): 493-497.
- Ferry, Gilles, et al. “Autotaxin is released from adipocytes, catalyzes
lysophosphatidic acid synthesis, and activates preadipocyte proliferation up-
regulated expression with adipocyte differentiation and obesity.” Journal of
Biological Chemistry 278.20 (2003): 18162-18169.
- Nakamura, Kazuhiro, et al. “Validation of an autotaxin enzyme immunoassay
in human serum samples and its application to hypoalbuminemia
differentiation.” Clinica chimica acta 388.1-2 (2008): 51-58.
Catalogue number: 31770
Elisa: 96-well
