PEDF (human, recombinant)

Pigment epithelium-derived factor (PEDF) is a secreted glycoprotein encoded by the SERPINF1 gene.¹ It is a non-inhibitory member of the serine-protease inhibitor (SERPIN) superfamily that has anti-angiogenic and neurotrophic activities. PEDF is a 418-amino acid protein comprised of an N-terminal region important for its neurotrophic activity, three β-sheets and ten α-helices that make up an α/β core serpin domain, and a C-terminal region containing a glycosylation site.^1,2 It has an asymmetrical charge distribution with the basic region involved in glycosaminoglycan binding and the acidic region binding to collagen I.² PEDF is ubiquitously expressed and localized to the extracellular matrix but can also be found in the cytoplasm and nucleus of retinal pigment epithelial cells and certain cancer cell lines.^1,3 It contains biologically active peptides, including a 34-amino acid peptide (amino acids 44-77), which contains a laminin receptor binding site and has anti-angiogenic, bone mineralization, and apoptotic activities, and a 44-amino acid peptide (amino acids 78-121), which contains a PNPLA2 binding site and promotes neuronal differentiation and inhibits vascular permeability.^1,4,5 PEDF also interacts with collagen I for its anti-angiogenic activity, as well as with sulfated (heparin) and non-sulfated (hyaluronan) glycosaminoglycans, which are important for PNPLA2 receptor binding and activation of caspases, respectively.^1,2 Its expression is reduced in a variety of cancer cell lines and solid tumors, and the reduction is associated with metastasis and poor prognosis.² Mutations in SERPINF1 are responsible for the hereditary bone dysplasia disorder osteogenesis imperfecta type VI, which is characterized by bone fragility, deformity, and growth deficiency.⁶ Cayman’s PEDF (human, recombinant) protein consists of 410 amino acids, has a calculated molecular weight of 45.8 kDa, and a predicted N-terminus of Gln20 after signal peptide cleavage.

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1. Kawaguchi, T., Yamagishi, S.-I., and Sata, M. Structure-function relationships of PEDF. Curr. Mol. Med. 10(3), 302-311 (2010).

2. Filleur, S., Nelius, T., de Riese, W., et al. Characterization of PEDF: A multi-functional serpin family protein. J. Cell. Biochem. 106(5), 769-775 (2009).

3. Tombran-Tink, J., Aparicio, S., Xu, X., et al. PEDF and the serpins: Phylogeny, sequence conservation, and functional domains. J. Struct. Biol. 151(2), 130-150 (2005).

4. Belinsky, G.S., Sreekumar, B., Andrejecsk, J.W., et al. Pigment epithelium–derived factor restoration increases bone mass and improves bone plasticity in a model of osteogenesis imperfecta type VI via Wnt3a blockade. The FASEB Journal 30(8), 2837-2848 (2016).

5. Bernard, A., Gao-Li, J., Franco, C.-A., et al. Laminin receptor involvement in the anti-angiogenic activity of pigment epithelium-derived factor. The Journal of Biological Chemisty 284(16), 10480-10490 (2009).

6. Marini, J.C., and Blissett, A.R. New genes in bone development: What’s new in osteogenesis imperfecta. J. Clin. Endocrinol. Metab. 98(8), 3095-3103 (2013).