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Description

Bone morphogenetic protein 10 (UniProt: O95393, also known as BMP-10) is encoded by the BMP10 gene (Gene ID: 27302) in human. BMP-10 is a disulfide-linked homodimeric protein that is synthesized with a signal peptide (aa 1-21) and a propeptide (aa 22-316) that are subsequently cleaved off to generate the mature form (aa 317-424). It can act as a homodimer or can heterodimerize with BMP-9 to serve as a high affinity ligand for endothelial receptor activin-receptor-like kinase 1 (ALK1) that plays a key role in vascular remodeling. Both BMP-9 and 10 are shown to be present in blood and their levels are elevated in mice around birth, which suggests that they play an active role in pre- and postnatal development. They are reported to be essential for proper closure of the ductus arteriosus. BMP-10 is also essential for maintaining the proliferative activity of embryonic cardiomyocytes. It prevents the premature activation of the negative cell cycle regulator CDKN1C/p57KIP. BMP-9 and 10 share about 65% sequence identity and studies with either BMP-9 or BMP-10 knockout mice have shown that plasma from these KO mice lack the ability to activate ALK-1-transfected 3T3 cells, which suggests that most of the biological activity resides in the circulating heterodimeric form. In mammals, the major organ for BMP-9 production is the liver and BMP-10 is produced in the cardiac tissue. (Ref.: Tillet, E., et al. (2018). J. Biol. Chem. 293(28), 10963-10974, Levet, S., et al. (2015). Proc. Natl. Acad. Sci. USA. 112(25), E3207-3215).