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Identification of important interactions between subchondral bone ...

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CHAPTER 2: Introduction<br />

18<br />

Fig. 3. Schematic drawing <strong>of</strong> a long<br />

<strong>bone</strong>. A femur <strong>bone</strong> divided in sections:<br />

epiphyses, metaphyses, and a diaphysis.<br />

The different types <strong>of</strong> <strong>bone</strong> are shown;<br />

cortex (hard) and trabecular (spongy)<br />

<strong>bone</strong>. The proximal epiphysis (femur<br />

head) and the distal epiphysis are<br />

covered with cartilage to provide a<br />

smooth friction (during movement). The<br />

figure was produced by Madsen, S.H.<br />

The weight bearing <strong>bone</strong>s, such as the femur and tibia that comprises the knee, have two<br />

opposite and <strong>important</strong> functions. The first is to resist loading, thus the <strong>bone</strong> must be stiff. The<br />

second is to be flexible to withstand shock, compression and tension by energy absorption and<br />

deformation 21 . The stiffness is achieved by mineralization and flexibility is achieved by a suitable<br />

organic matrix composition. However, if the <strong>bone</strong> matrix is too mineralized, it will become brittle<br />

and more prone to fractures, whereas if it is under-mineralized, the <strong>bone</strong> will be too flexible and<br />

will crack more readily. Therefore, the functionality <strong>of</strong> the <strong>bone</strong> highly depends on the ratio <strong>of</strong><br />

organic and inorganic matrices 21 .<br />

In mammalian <strong>bone</strong>, the inorganic part <strong>of</strong> the matrix (50-70%) consist <strong>of</strong><br />

hydroxyapatite crystals [3Ca 3(PO 4) 2·(OH) 2], which are layered on and within collagen fibres,<br />

ensuring <strong>bone</strong> matrix stiffness (mineralization). The crystals tend to orient in the same direction<br />

as the collagen fibres. The organic part <strong>of</strong> the matrix (20-40%) consists mainly <strong>of</strong> collagen type I<br />

(approximately 90%), but also glycoproteins, proteoglycans, and non-collagenous proteins. The<br />

collagen type I molecule is a triple helix (described further in section 2.3.4), which is assembled<br />

into fibres, providing the tensile strength <strong>of</strong> the matrix. The orientation <strong>of</strong> the collagen fibres<br />

determines the microscopic structure <strong>of</strong> the <strong>bone</strong>. During <strong>bone</strong> development or fracture healing,<br />

where <strong>bone</strong> is formed very rapidly, there is no preferential organization <strong>of</strong> the collagen fibres; this<br />

type <strong>of</strong> <strong>bone</strong> is called woven <strong>bone</strong> (fig. 4) 17 . Woven <strong>bone</strong> is characterized by irregular bundles <strong>of</strong><br />

collagen fibres and calcification, which occur in irregularly distributed patches. Woven <strong>bone</strong> is<br />

progressively replaced by mature lamellar <strong>bone</strong> (fig. 4) during the remodelling process that

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