Abstract
Bone comprises a unique calcified extracellular matrix which is the most abundant source of connective tissue components. It is mainly composed of type I collagen (90% of the organic matrix), which differs from the type I collagen present in other connective tissues by several posttranslational modifications. The non-collagenous component (10% of the organic matrix) has been extensively characterized in the past 15 years, due to progress in protein biochemistry and molecular biology techniques, as reviewed by Gehron-Robey (1989). In particular, the alternate use of dissociating (EDTA) and nondissociating buffers leads to the differentiation of a mineral phase (hydroxyapatite crystals) and an organic phase (collagenous matrix), between which the proteins are distributed. The population of proteins present in bone is composed of exogenous and endogenous proteins (listed in Table 1). Exogenous proteins are synthesized in other organs, circulate in blood and tissue fluids, and are trapped in bone matrix because of their affinity for hydroxyapatite. Endogenous proteins are synthesized by the bone-forming cells - the osteoblasts - and incorporated into the complex three-dimensional scaffolding of bone matrix. These bone matrix proteins have raised considerable interest as they are thought to play an important role in several aspects of bone physiology (Fig. 1).
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Delmas, P.D., Malaval, L. (1993). The Proteins of Bone. In: Physiology and Pharmacology of Bone. Handbook of Experimental Pharmacology, vol 107. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-77991-6_19
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