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5 In the cardiovascular system, the half-life of collagen is on the order of 15–90 days. Regardless of the specific half-life, maintenance of physiologic levels of collagen depends on a delicate balance between continual synthesis and degradation, the kinetics of which is complex but may be assumed to be of first order (Niedermuller et al. 1977; Gelman et al. 1979). Degradation can be accomplished by blood-plasma-borne serine proteases, the extracellular release of matrix metalloproteinases (MMPs), as, for example, by macrophages or via intracellular lysosomal activity within phagocytotic fibroblasts (Ten Cate and Deporter 1975).

Two unique amino acids, desmosine and isodesmosine, are largely responsible for the formation of distributed covalent cross-links between the 5 In contrast, many cellular proteins have half-lives of hours or days (Alberts et al. 2008). 5. The Extracellular Matrix 21 relatively loose and unstructured chains. , nondissipative or recoverable) response over large deformations (indeed, elastin appears to be the most elastic protein in the body). Moreover, a high concentration of nonpolar hydrophobic amino acids renders elastin one of the most chemically, thermally, and protease-resistant proteins in the body.

Although his analysis was not correct, the basic idea was extremely important. For more on “Wolff’s law of bone remodeling,” see Chap. 4 as well as Roesler (1987). Indeed, we will return many times to this observation that mechanical loads control tissue structure and function, which has given rise to the very important area of research called mechanobiology. Many other savants were interested in biomechanical applications. They include R. Hooke (1635–1703), L. Euler (1707–1783), T. M. Poiseuille (1799–1869), and H.

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