Expression, purification and osteogenic bioactivity of recombinant human BMP-4,-9,-10,-11 and-14

• Type: Article in International Scientific Journal
• Date: 2009

Authors

Bessa, PC (Author) Other; Cerqueira, MT (Author) Other; Rada, T (Author) Other; Gomes, ME (Author) Other; Neves, NM (Author) Other; Nobre, A (Author) Other; Rui Reis (Author) Other; Casal, M (Author) Other

Journal

Title: Protein Expression and Purification

Vol. 63

Pages: 89-94

ISSN: 1046-5928

Publisher: Elsevier

Indexing

ISI Web of Knowledge - 36 Citations

Scopus - 40 Citations

Other information

Authenticus ID: P-003-NNJ

DOI: 10.1016/j.pep.2008.09.014

Abstract (EN): Bone morphogenetic proteins (BMPs) are cytokines from the TGF-beta superfamily, with important roles during embryonic development and in the induction of bone and cartilage tissue differentiation in the adult body. In this contribution, we report the expression of recombinant human BMPA, BMP-9, BMP-10, BMP-11 (or growth differentiation factor-11, GDF-11) and BMP-14 (GDF-5), using Escherichia coli pET-25b vector. BMPs were overexpressed, purified by affinity his-tag chromatography and shown to induce the expression of early markers of bone differentiation (e.g. smad-1, smad-5, runx2/cbfa1, dlx5, osterix, osteopontin, bone sialoprotein and alkaline phosphatase) in C2C12 cells and in human adipose stem cells. The described approach is a promising method for producing large amounts of different recombinant BMPs that show potential for novel biomedical applications.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 6