Tendon collagens: extracellular matrix composition in shear stress and tensile components of flexor tendons.

Abstract

Outer synovial tissues were separated from the remainder of avian flexor tendon and the collagens characterized biochemically and compared with those of the internal portion of tendon and sheath. The collagen content of tendon synovium was 23%, whereas that of tendon and sheath were 78% and 73%, respectively, based on dry weight. Four genetic types of collagen were found in the pepsin solubilized matrices: in the synovium, types I (78%) and III (19%) predominated; types V and possibly VI were present as minor collagens. Purified synovial type V collagen was a heterotrimer, with chain composition [alpha 1(V)]2 alpha 2(V). In contrast, the internal portion of tendon and sheath were comprised of only type I collagen. There was a large amount (41%) of ethanol extractable, noncollagenous material present in synovium, a part of which was proteoglycans. In addition, collagen cross-links of these tissues were quantified: the internal tendon had an abundant concentration of pyridinoline; synovium exhibited high amounts of labile, reducible cross-links, particularly dihydroxylysinonorleucine. In the case of sheath, lysine aldehyde-derived cross-links appeared to be predominant. These results indicate that each tissue has its own collagen type distribution as well as cross-linking pattern reflecting their maturational and functional differences.