Cloning and characterization of a human type II receptor for bone morphogenetic proteins.

Abstract

Bone morphogenetic proteins (BMPs) are members of the transforming growth factor ,B superfamily. Bone morphogenetic proteins (BMPs) are a family of proteins that induce bone formation at extraskeletal sites in vivo (reviewed in refs. 1-3). BMPs act on osteoblasts and chondrocytes (4) as well as other cell types, including neural cells (5, 6), and they play important roles in the embryonal development (3). More than a dozen proteins belong to the BMP family, including BMP-2 to -6, osteogenic protein (OP)-1 (also termed BMP-7), OP-2 (BMP-8), and growth/differentiation factors 5 to 7.BMPs belong to the transforming growth factor ,B (TGF-f3) superfamily, which includes TGF-,3s, activins/inhibins, Miillerian inhibiting substance (MIS), and glial cell line-derived neurotrophic factor (GDNF) (7). TGF-13s and activins transduce their signals through the formation of heteromeric complexes of two different types of serine(threonine) kinase

Expression of transforming growth factor‐β superfamily receptors in rat eyes

“…These researchers supplied the affinity purified antibodies to our research group (Franzén et al 1993;ten Dijke et al 1994b). It has been confirmed and reported previously that all the antibodies do not cross-react with each other biochemically (ten Rosenzweig et al 1995). Frozen sections 6 mm thick were cut and placed on poly-L-lysine-coated slides.…”

“…The antigens were peptides corresponding to the amino acid residues in the human receptors: TbR-I peptide, amino acid residues 158-179; ActR-I, amino acid residues 151-172; ActR-IB, amino acid residues 153-171; BMPR-IA, amino acid residues 181-202; BMPR-IB, amino acid residues 151-168; ALK-1, amino acid residues 145-166; TbR-II, amino acid residues 545-566; ActR-II, amino acid residues 492-510 (ten Yamashita et al 1995). Two types of antisera to BMPR-II, generated against two types of peptides corresponding to the amino acid residues 185-202 and 534-556, were used (SMN and NRR, respectively) (Rosenzweig et al 1995). A truncated form of BMPR-II which is detected by SMN but not NRR has been reported (Liu et al 1995).…”

“…zono et al 1994b). The type II receptor family has 5 members Rosenzweig et al 1995;Yamashita et al 1995Yamashita et al , 1996.…”

The BMP signaling and in vivo bone formation

“…Three type I receptors have been shown to bind BMP ligands, type IA and IB BMP receptors (BMPR-IA or ALK-3 and BMPR-IB or ALK-6) and type IA activin receptor (ActR-IA or ALK-2) (Koenig et al, 1994;ten Dijke et al, 1994;Macias-Silva et al, 1998). Three type II receptors for BMPs have also been identified and they are type II BMP receptor (BMPR-II) and type II and IIB activin receptors (ActR-II and ActR-IIB) (Yamashita et al, 1995;Nohno et al, 1995;Rosenzweig et al, 1995;Kawabata et al, 1995). Whereas BMPR-IA, IB, and II are specific to BMPs, ActR-IA, II, and IIB are also signaling receptors for activins.…”

A Kinase Domain-truncated Type I Receptor Blocks Bone Morphogenetic Protein-2-induced Signal Transduction in C2C12 Myoblasts

“…The structure of the type I receptor is conserved in all type I receptors of the TGF-␤ superfamily, suggesting that the BMP signals are transduced by the BMP type I receptor like those of TGF-␤. Two type I receptors (BMPR-IA and BMPR-IB) and one type II receptor (BMPR-II) have been identified for BMP-2 and BMP-4 (21)(22)(23)(24)(25)(26)(27). BMP-7 can interact with activin type I and type II receptors in addition to BMP-2/BMP-4 receptors (26,28).…”