描述：
BMP2 is one of at least 20 structurally and functionally related BMPs, which are
members of the transforming growth factor β (TGFβ) superfamily. BMPs were
originally indentified as protein regulators of cartilage and bone formation. However,
they are also involved in embryogenesis and morphogenesis of various tissues
and organs. BMPs regulate the growth, differentiation, chemotaxis, and apoptosis
of various cell types, including mesenchymal cells, epithelial cells, hematopoietic
cells, and neuronal cells. Similarly to other TGFβ family proteins, BMPs are highly
conserved across animal species. At the amino acid sequence level, mature human,
mouse, and rat BMP2 are 100% identical, while mature human BMP2 and zebrafish
BMP2a are 85% identical. Zebrafish have another homolog of BMP2a, BMP2b, which
is 88% identical to BMP2a in the mature region and corresponds to the swirl mutant.
The combined expression pattern of zBMP2a/2b/4 coincides with areas where BMP2/4
expression would be found in other vertebrates. Biologically active BMP2a is a disulfide
linked homodimer of the carboxyterminal 115 amino acid residues that contains the
characteristic seven conserved cysteine residues involved in the formation of the cysteine
knot and the single interchain disulfide bond. Cellular responses to BMP2a have been
shown to be mediated by the formation of heteroogliomeric complexes of type I and
type II serine/threonine kinase receptors. In contrast to the TGFβ type I receptor,
which does not bind the ligand in the absence of the TGFβ receptor type II, both BMP
receptor type I’s can bind BMP2 with high affinity in the absence of BMP receptor type II.
原厂资料：
BMP2 is one of at least 20 structurally and functionally related BMPs, which are
members of the transforming growth factor β (TGFβ) superfamily. BMPs were
originally indentified as protein regulators of cartilage and bone formation. However,
they are also involved in embryogenesis and morphogenesis of various tissues
and organs. BMPs regulate the growth, differentiation, chemotaxis, and apoptosis
of various cell types, including mesenchymal cells, epithelial cells, hematopoietic
cells, and neuronal cells. Similarly to other TGFβ family proteins, BMPs are highly
conserved across animal species. At the amino acid sequence level, mature human,
mouse, and rat BMP2 are 100% identical, while mature human BMP2 and zebrafish
BMP2a are 85% identical. Zebrafish have another homolog of BMP2a, BMP2b, which
is 88% identical to BMP2a in the mature region and corresponds to the swirl mutant.
The combined expression pattern of zBMP2a/2b/4 coincides with areas where BMP2/4
expression would be found in other vertebrates. Biologically active BMP2a is a disulfide
linked homodimer of the carboxyterminal 115 amino acid residues that contains the
characteristic seven conserved cysteine residues involved in the formation of the cysteine
knot and the single interchain disulfide bond. Cellular responses to BMP2a have been
shown to be mediated by the formation of heteroogliomeric complexes of type I and
type II serine/threonine kinase receptors. In contrast to the TGFβ type I receptor,
which does not bind the ligand in the absence of the TGFβ receptor type II, both BMP
receptor type I’s can bind BMP2 with high affinity in the absence of BMP receptor type II.
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