描述：
BMP-3, also known as osteogenin, the most abundant BMP in adult bone, is one of at
least 15 structurally and functionally related BMPs, which are members of the TGFβ
superfamily. BMPs were originally identified as protein regulators of cartilage and bone
formation. They have since been shown to be involved in embryogenesis and morphogenesis
of various tissues and organs. BMPs also regulate the growth, differentiation, chemotaxis,
and apoptosis of various cell types. Similar to most other TGF-β family proteins, BMPs are
highly conserved across animal species. At the amino acid sequence level, mature human
and rat BMP-3 are 98% identical. BMP3 is synthesized as a large precursor protein that is
cleaved at the dibasic cleavage site (RXXR) to release the carboxyterminal domain.
Biologically active BMP-3 is a disulfidelinked homodimer of the carboxyterminal 110
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.
The role of BMP-3 in bone is contradictory since, unlike osteogenin purified from bone,
recombinant BMP-3 has not shown osteogenic function. Several studies indicate that BMP-3
is an inhibitor of osteogenic BMPs. BMP-3 dorsalizes Xenopus embryos, the opposite effect
of BMP-2 or 4, which cause ventralization. BMP-3 inhibits alkaline phosphatase production
and induction of osteoblastic target genes in undifferentiated mesenchymal and osteogenic
cell lines that have been treated with BMP-2. BMP-3 also induces the expression of TGFβ /activin responsive genes, but not BMPresponsive genes. Since the inhibitory effect is
not due to direct competition with osteogenic BMPs, it has been suggested
that BMP-3 activates signaling through an activin pathway, resulting in antagonism of
osteogenesis induced by other BMPs.
原厂资料：
BMP-3, also known as osteogenin, the most abundant BMP in adult bone, is one of at
least 15 structurally and functionally related BMPs, which are members of the TGFβ
superfamily. BMPs were originally identified as protein regulators of cartilage and bone
formation. They have since been shown to be involved in embryogenesis and morphogenesis
of various tissues and organs. BMPs also regulate the growth, differentiation, chemotaxis,
and apoptosis of various cell types. Similar to most other TGF-β family proteins, BMPs are
highly conserved across animal species. At the amino acid sequence level, mature human
and rat BMP-3 are 98% identical. BMP3 is synthesized as a large precursor protein that is
cleaved at the dibasic cleavage site (RXXR) to release the carboxyterminal domain.
Biologically active BMP-3 is a disulfidelinked homodimer of the carboxyterminal 110
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.
The role of BMP-3 in bone is contradictory since, unlike osteogenin purified from bone,
recombinant BMP-3 has not shown osteogenic function. Several studies indicate that BMP-3
is an inhibitor of osteogenic BMPs. BMP-3 dorsalizes Xenopus embryos, the opposite effect
of BMP-2 or 4, which cause ventralization. BMP-3 inhibits alkaline phosphatase production
and induction of osteoblastic target genes in undifferentiated mesenchymal and osteogenic
cell lines that have been treated with BMP-2. BMP-3 also induces the expression of TGFβ /activin responsive genes, but not BMPresponsive genes. Since the inhibitory effect is
not due to direct competition with osteogenic BMPs, it has been suggested
that BMP-3 activates signaling through an activin pathway, resulting in antagonism of
osteogenesis induced by other BMPs.
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