AI Article Synopsis
- Wnt proteins are crucial for development and disease but are difficult to study due to their hydrophobic nature, requiring detergents for purification.
- Researchers discovered that Wnt3a can be purified alongside a glycoprotein called afamin, forming a stable 1:1 complex that remains soluble and biologically active.
- This afamin-Wnt complex can facilitate the study of various Wnt ligands and their signaling pathways more effectively, addressing challenges researchers have faced previously.
Article Abstract
Wnt plays important role during development and in various diseases. Because Wnts are lipidated and highly hydrophobic, they can only be purified in the presence of detergents, limiting their use in various in vitro and in vivo assays. We purified N-terminally tagged recombinant Wnt3a secreted from cells and accidentally discovered that Wnt3a co-purified with a glycoprotein afamin derived from the bovine serum included in the media. Wnt3a forms a 1:1 complex with afamin, which remains soluble in aqueous buffer after isolation, and can induce signaling in various cellular systems including the intestical stem cell growth assay. By co-expressing with afamin, biologically active afamin-Wnt complex can be easily obtained in large quantity. As afamin can also solubilize Wnt5a, Wnt3, and many more Wnt subtypes, afamin complexation will open a way to put various Wnt ligands and their signaling mechanisms under a thorough biochemical scrutiny that had been difficult for years.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4775226 | PMC |
| http://dx.doi.org/10.7554/eLife.11621 | DOI Listing |
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