Site-related variations in glycosaminoglycan content and swelling properties of bovine flexor tendon.
The presence of morphologically distinct tissues within the adult bovine deep flexor tendon presented a model which we examined for correlations between proteoglycan content and tissue swelling properties. The proximal portion which experiences only tensile forces contained low levels of glycosaminoglycan (0.2% glycosaminoglycan hexosamine as percentage of dry weight) that were evenly distributed throughout its length and thickness. Collagen accounted for 80% of tissue mass, and collagen fibers formed parallel arrays running longitudinal to the direction of tensile force. In equilibrium bulk swelling tests, the properties of proximal tissue were uniform throughout the tissue and typical of collagenous tissues in which the response to equilibration in low ionic strength buffers or acid pH is dominated by the collagen network. The anterior aspect of the distal deep flexor tendon articulates with the stiff paratendinous sheath and sesamoid bones and is subjected to compressive and frictional forces in addition to longitudinal tensile forces. Along this anterior surface and extending partially into the tendon is tissue that resembles fibrocartilage with collagen fibers organized as a random network. Greatest glycosaminoglycan hexosamine contents (2-3% of dry weight) were found in the distal surface layer, and large proteoglycans were concentrated at the site receiving direct compressive and frictional loads. Equilibrium bulk swelling tests on distal tissue showed that the articulating surface layer possessed unique material properties. Distal surface layers swelled when counter ions were washed from the tissue, whereas lowered pH had little effect on distal tissue volume. Swelling properties of distal tissue correlated directly with proteoglycan content and were similar to swelling properties of articular cartilage. These results suggest that the articulating layer of distal flexor tendon is adapted for a unique set of mechanical requirements and that an elevated proteoglycan content at the site of compressive and frictional forces contributes to meeting these functional needs.
D000818:Animals; D001696:Biomechanical Phenomena; D002417:Cattle; D002499:Centrifugation, Density Gradient; D003094:Collagen / Q000032:analysis; D004591:Electrophoresis, Polyacrylamide Gel; D006025:Glycosaminoglycans / Q000032:analysis*; D006595:Hexosamines / Q000032:analysis; D008297:Male; D009929:Organ Size; D011509:Proteoglycans / Q000032:analysis; D013710:Tendons / Q000032:analysis / Q000033:anatomy & histology / Q000502:physiology*; D013718:Tensile Strength
D006025:Glycosaminoglycans; D006595:Hexosamines; D011509:Proteoglycans; D003094:Collagen