Decorin Long Isoform (human, recombinant)

Decorin is an extracellular matrix protein and member of the leucine-rich proteoglycan family that influences many cellular functions, including adhesion, growth, differentiation, proliferation, and survival.^1,2 Alternative splicing of DCN pre-mRNA generates five isoforms of varying length.³ Decorin contains a core protein that mediates ligand binding and is composed of a cysteine-rich domain covalently linked to a chondroitin or dermatan sulfate glycosaminoglycan chain and a leucine-rich repeat (LRR) domain that can bind up to three N-linked oligosacchaides.^4,5 The core protein is flanked by an N-terminal signal peptide and propeptide domain, which regulate decorin secretion, and a C-terminal domain that is truncated in mutant forms of DCN. Decorin is secreted as a monomer and expressed by endothelial cells and cancer cells in a variety of tissues.¹ It is induced by autophagic stimuli, including mTOR inhibition and nutrient deprivation, and downregulated by the adhesion protein periostin.^6,7 Decorin binds to and sequesters a variety of molecules, including extracellular matrix proteins, growth factors and their receptors, cytokines, enzymes, hormones, and lipoproteins.⁴ It also enhances integrin-collagen interactions, promoting angiogenesis.⁸ Intravenous administration of the decorin core protein reduces tumor growth and lung metastases in an MTLn3 mouse xenograft model.⁹ Decreased decorin tumor levels are associated with low disease-free and overall survival rates in patients with spindle cell sarcomas.⁸ Frameshift mutations in DCN have been associated with congenital stromal corneal dystrophy, a condition characterized by corneal opacity.⁵ Cayman's Decorin Long Isoform (human, recombinant) protein consists of 354 amino acids, has a calculated molecular weight of 39.4 kDa, and a predicted N-terminus of Gly17 after signal peptide cleavage. Differential glycosylation of decorin results in the presence of multiple protein bands causing the observed smear at approximately 45 kDa and higher when observed by SDS-PAGE under reducing conditions.

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1. Zhang, W., Ge, Y., Cheng, Q., et al. Decorin is a pivotal effector in the extracellular matrix and tumour microenvironment. Oncotarget 9(4), 5480-5491 (2018).

2. Neill, T., Schaefer, L., and Iozzo, R.V. Decorin: A guardian from the matrix. Am. J. Pathol. 181(2), 380-387 (2012).

3. McKee, M.D., and Cole, W.G. Bone matrix and mineralization. Pediatric Bone 9-37 (2012).

4. Sainio, A.O., and Järveläinen, H.T. Decorin-mediated oncosuppression - a potential future adjuvant therapy for human epithelial cancers. Br. J. Pharmacol. 176(1), 5-15 (2019).

5. Bredrup, C., Knappskog, P.M., Majewski, J., et al. Congenital stromal dystrophy of the cornea caused by a mutation in the decorin gene. Invest. Ophthalmol. Vis. Sci. 46(2), 420-426 (2005).

6. Gubbiotti, M.A., Neill, T., Frey, H., et al. Decorin is an autophagy-inducible proteoglycan and is required for proper in vivo autophagy. Matrix Biol. 48, 14-25 (2015).

7. Ishiba, T., Nagahara, M., Nakagawa, T., et al. Periostin suppression induces decorin secretion leading to reduced breast cancer cell motility and invasion. Sci. Rep. 4, 7069 (2014).

8. Bi, X.-L., and Yang, W. Biological functions of decorin in cancer. Chin. J. Cancer 32(5), 266-269 (2013).

9. Goldoni, S., Seidler, D.G., Heath, J., et al. An antimetastatic role for decorin in breast cancer. Am. J. Pathol. 173(3), 844-855 (2008).