描述:
Human BMP-7, also known as osteogenic protein -1 (OP-1), and BMP-2 are members of
the BMP subgroup of the TGF-β superfamily and signal through heterodimeric complexes
composed of type I and type II BMP receptors. BMP-2 and BMP-7 influence a variety of
morphogenic processes, particularly during skeletal and renal development.The human
BMP-2 cDNA encodes a 396 amino acid (aa) precursor that contains a 23 aa signal sequence,
a 259 propeptide, and a 114 aa mature protein. The human BMP-7 cDNA encodes a 431 aa
precursor that contains a 29 aa signal sequence, a 263 aa propeptide, and a 139 aa mature
protein. BMP propeptides are removed by proteolysis, enabling mature BMPs to form active
disulfide linked homodimers or heterodimers. Human and mouse BMP-2 and BMP-7 are 100%
and 98% identical, respectively, at the amino acid level. Human BMP-2 shares 85% aa sequence
identity with human BMP-4 and less than 51% aa sequence identity with other BMPs. Human
BMP-7 shares approximately 60%-70% aa sequence identity with BMP-5, -6, and -8, and less
than 50% aa sequence identity with other BMPs. BMP-2 and BMP-7 are coexpressed in some
embryonic tissues and associate into a functional 38 kDa osteogenic dimer. In in vitro osteoblast
differentiation assays and in vivo bone formation models, a BMP-2/BMP-7 heterodimer is
significantly more potent than either homodimer. Considering that BMP-2 preferentially binds
BMPRIA/ALK-3 and BMPRIB/ALK-6, while BMP-7 is selective for ALK-2, the observed increase in
heterodimer activity may be due to the triggering of additional receptor subtypes.
原厂资料:
Human BMP-7, also known as osteogenic protein -1 (OP-1), and BMP-2 are members of
the BMP subgroup of the TGF-β superfamily and signal through heterodimeric complexes
composed of type I and type II BMP receptors. BMP-2 and BMP-7 influence a variety of
morphogenic processes, particularly during skeletal and renal development.The human
BMP-2 cDNA encodes a 396 amino acid (aa) precursor that contains a 23 aa signal sequence,
a 259 propeptide, and a 114 aa mature protein. The human BMP-7 cDNA encodes a 431 aa
precursor that contains a 29 aa signal sequence, a 263 aa propeptide, and a 139 aa mature
protein. BMP propeptides are removed by proteolysis, enabling mature BMPs to form active
disulfide linked homodimers or heterodimers. Human and mouse BMP-2 and BMP-7 are 100%
and 98% identical, respectively, at the amino acid level. Human BMP-2 shares 85% aa sequence
identity with human BMP-4 and less than 51% aa sequence identity with other BMPs. Human
BMP-7 shares approximately 60%-70% aa sequence identity with BMP-5, -6, and -8, and less
than 50% aa sequence identity with other BMPs. BMP-2 and BMP-7 are coexpressed in some
embryonic tissues and associate into a functional 38 kDa osteogenic dimer. In in vitro osteoblast
differentiation assays and in vivo bone formation models, a BMP-2/BMP-7 heterodimer is
significantly more potent than either homodimer. Considering that BMP-2 preferentially binds
BMPRIA/ALK-3 and BMPRIB/ALK-6, while BMP-7 is selective for ALK-2, the observed increase in
heterodimer activity may be due to the triggering of additional receptor subtypes.