ArticleAMB Express2020
Human bone morphogenetic protein-2 (hBMP-2) characterization by physical-chemical, immunological and biological assays.
Article in AMB Express, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 14 citations in OpenAlex.
- Comparative osteogenic performance of Chinese hamster ovary cell-derived versus Escherichia coli-derived recombinant human bone morphogenetic protein-2.Bone & joint research · 2026Article
- Synthesis ofMolecules (Basel, Switzerland) · 2026Article
- Engineering bone tissue with mRNA: from molecular design and delivery to clinical applications.Materials today (Kidlington, England) · 2025Article
- Enhancement of In Vivo Bone Regeneration by the Carbohydrate Derivative DP2.Pharmaceuticals (Basel, Switzerland) · 2025Article
- DP2, a Carbohydrate Derivative, Enhances In Vitro Osteoblast Mineralisation.Pharmaceuticals (Basel, Switzerland) · 2023Article
- Assessment of Escherichia coli-derived Recombinant Human Bone Morphogenic Protein-2 on Fertilization and Early Embryonic Development in Rats.Pharmaceutical research · 2023Article
- Regulatory of miRNAs in tri-lineage differentiation of C3H10T1/2.Stem cell research & therapy · 2022Review
- Modulation of osteogenic differentiation by Escherichia coli-derived recombinant bone morphogenetic protein-2.AMB Express · 2022Article
- Article
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Authors and funding
11 authors at 5 institutions in 1 country.
Funding
Abstract
Commercially available preparations of methionyl-human BMP-2 and CHO-derived hBMP-2, which belongs to the transforming growth factor β (TGF-β) superfamily, were used for a complete characterization. This protein is an extremely efficient osteoinductor that plays an important role during bone regeneration and embryonic development. Characterization was carried out via SDS-PAGE and Western blotting, followed by reversed-phase HPLC, size-exclusion HPLC and MALDI-TOF-MS. The classical in vitro bioassay, based on the induction of alkaline phosphatase activity in C2C12 cells, confirmed that hBMP-2 biological activity is mostly related to the dimeric form, being ~ 4-fold higher for the CHO-derived glycosylated form when compared with the E. coli counterpart. The E. coli-derived met-hBMP-2 has shown, by MALDI-TOF-MS, a large presence of the bioactive dimer. A more complex molecular mass (MM) distribution was found for the CHO-derived product, whose exact MM has never been reported because of its variable glycosylation. A method based on RP-HPLC was set up, allowing a quantitative and qualitative hBMP-2 determination even directly on ongoing culture media. Considering that hBMP-2 is highly unstable, presenting moreover an extremely high aggregate value, we believe that these data pave the way to a necessary characterization of this important factor when synthesized by DNA recombinant techniques in different types of hosts.
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