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The Journal of Bone and Joint Surgery (American) 85:34-38 (2003)
© 2003 The Journal of Bone and Joint Surgery, Inc.

Basic Science

Signal Transduction of Bone Morphogenetic Proteins in Osteoblast Differentiation

Peter ten Dijke, PhD, Jingyuan Fu, MS, Peter Schaap, PhD and Bernard A.J. Roelen, PhD

Corresponding author: Peter ten Dijke, PhD
Division of Cellular Biochemistry, The Netherlands Cancer Institute, Plesmanlaan, 121 1066 CX Amsterdam, The Netherlands. E-mail address: p.t.dijke@nki.nl

In support of their research or preparation of this manuscript, one or more of the authors received support from the Netherlands Organization for Scientific Research (ALW 809.67.024) and an EU TMR network grant (ERB FMRX-CT98-0216). No commercial entity paid or directed, or agreed to pay or direct, any benefits to any research fund, foundation, educational institution, or other charitable or nonprofit organization with which the authors are affiliated or associated.

The first 150 words of the full text of this article appear below.

Bone morphogenetic proteins (BMPs) were initially identified by their ability to induce ectopic cartilage and bone formation 1 . Upon cDNA cloning of BMP-2, BMP-3, and BMP-4, the predicted amino acid sequences revealed that BMPs (except BMP-1, which is a member of the astacin family of metalloproteases) are members of the transforming growth factor-ß (TGF-ß) superfamily 2 , to which the TGF-ßs, activins, nodal, and Müllerian inhibiting substance (MIS)/anti-Müllerian hormone (AMH) also belong 3 . The structure of TGF-ß family members, at least thirty-four of which are present in the human genome 4 , consists of an amino-terminal signal sequence, a pro-domain, and their carboxy-terminal mature peptide that is released upon furin-mediated cleavage ( Fig. 1 , A ). The mature domain is highly conserved and has a characteristic 7-cysteine motif. The mature domain forms homodimers or heterodimers that are in most cases covalently linked by one disulphide bond. The BMP/growth and differentiation factors . . . [Full Text of this Article]


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