Expression, purification and bioactivity of recombinant human bone morphogenetic protein-4,-9,-10,-11 and-14 produced in Escherichia coli for tissue engineering applications

Bone morphogenetic
proteins
(BMPs) are cytokines
from the TGF-b 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 BMP-4, 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.