Bone Morphogenetic Proteins (BMPs)
Bone Morphogenetic Proteins or BMPs have been studied on some level for decades. The science behind BMPs has focused on whether a single protein of recombinant human BMP can promote bone regeneration. New bone formation is required to achieve a successful spinal fusion. Without bone growth, a patient will not obtain a solid fusion and the pain that was the main reason behind having the surgery in the first place will not be relieved.
Breaking Down BMP
Bone is made up of about 65-70% mineral and 30-35% organic matrix. In 1965, Dr. Marshall Urist discovered that by demineralizing bone and placing only the organic matrix part of the bone into the muscle of rats, he could promote new bone formation.
This discovery led to the extended research that proved that a series of proteins found in bone matrix, collectively known as BMPs, are responsible for the bone formation observed by Urist. This ability to promote bone growth at an ectopic (non-bony) site in an adult animal has become the definitive test to determine if a material is classified as osteoinductive (induces bone growth).
The different members of the BMP family have slightly different amino acid structures. The structure of BMP-2 has been shown to be (the same) across a range of species.
Naturally occurring BMP found in bone is only available in trace amounts. It has been estimated that nanogram levels of BMPs are found in each gram of dry bone. To provide clinically useful amounts of isolated, human BMP, hundreds of kilograms of bone would be needed. Therefore, human donor bone supply limitations prevent clinically useful BMP extracted from human bone from being a viable option for routine medical use.
To solve the problems of limited amounts of available human and animal extracted BMPs, and to ensure the uniformity of the vital components, the preferred method for obtaining BMP is to manufacture a recombinant version of a naturally occurring BMP using well established molecular biology techniques.
