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Figure?19-47?Type IX collagen.????(A) Schematic drawing of type IX collagen molecules binding in a periodic pattern to the surface of a type-II-collagen-containing fibril. (B) Electron micrograph of a rotary-shadowed type-II-collagen-containing fibril in cartilage sheathed in type IX collagen molecules; an individual type IX collagen molecule is shown in (C). (B and C, from L. Vaughan et al., J. Cell Biol. 106:991-997.) Figure?19-48?The shaping of the extracellular matrix by cells.????This micrograph shows a region between two pieces of embryonic chick heart (rich in fibroblasts as well as heart muscle cells) that has grown in culture on a collagen gel for four days. A dense tract of aligned collagen fibers has formed between the explants, presumably as a result of the fibroblasts in the explants tugging on the collagen. (D. Stopak and A.K. Harris, Dev. Biol. 90:383-398) Figure?19-49?A network of elastic fibers.????These scanning electron micrographs show a low-power view of a segment of a dogs aorta (A) and a high-power view of the dense network of longitudinally oriented elastic fibers in the outer layer of the same blood vessel (B). All of the other components have been digested away with enzymes and formic acid. (K.S. Haas et al., Anat. Rec. 230:86-96.) Elastin Figure?19-50?Stretching a network of elastin molecules.????The molecules are joined together by covalent bonds (indicated in red) to generate a cross-linked network. In the model shown each elastin molecule in the network can expand and contract as a random coil, so that the entire assembly can stretch and recoil like a rubber band. Figure?19-51?The structure of a fibronectin dimer.????As shown schematically in (A), the two polypeptide chains are similar but generally not identical. They are joined by two disulfide bonds near the carboxyl terminus. Each chain is almost 2500 amino acid residues long and is folded into five or six rodlike domains connected by flexible polypeptide segments. Individual do
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