BMP-3b, also known as GDF-10, belongs to the transforming growth factor beta (TGF-beta ) superfamily which includes the TGF-beta s, bone morphogenetic proteins (BMPs), growth differentiation factors (GDFs), Activins, Inhibins, Leftys, Nodal, Mullerian inhibitory substance (MIS) and the glial cell line-derived neurotrophic factors (GDNFs) (1). TGF-beta family members are synthesized and secreted as homodimeric or heterodimeric prepropeptides that are cleaved by proprotein convertases such as furin to generate the carboxy-terminal mature dimeric protein that contains the characteristic conserved cysteine residues involved in the formation of the cysteine knot domain. Within pro-BMP-3b, three dibasic cleavage sites have been identified. Mature BMP-3B is a disulfide-linked homodimer of the C-terminal 110 amino acids. Among TGF-beta family members, BMP-3b is most closely related to BMP-3, sharing 83% and 30% amino acid sequence identity in their mature and pro regions, respectively (2, 3). BMP-3b is highly conserved across animal species, the aa sequence of mature human BMP-3b is 98% identical with that of the mouse or rat proteins (2, 3). BMP-3b is expressed in developing skeletal structures of the craniofacial region and the vertebral column, as well as in the adult trachea, aorta, and most abundantly in the cerebellum and uterus (2‑4). Interestingly, in the knock-out mice, no obvious abnormalities have been found in these tissues (4). The biological function of BMP-3b is yet unknown, however studies have implicated it in the differentiation of osteoblasts, augmenting BMP-2 activity (5, 6).
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