The proteoglycan content and the axial periodicity of collagen in tendon.
The glycosaminoglycan content and the axial periodicity of collagen was determined in various regions of the rabbit flexor digitorum profundus tendon. This tendon, which passes from the calf to the toes round the inner side of the ankle, contains a thickened sesamoid-like pad where it is subjected to friction and pressure. Other regions of the tendon are subject only to longitudinal tension. In tensional areas the axial periodicity of collagen was of the order of 62 nm and the tissue contained less than 0.2% proteoglycan on a dry weight basis. In the sesamoid-like region, however, the axial periodicity was a significant 13-15% less, and the proteoglycan constituted about 3.5% of the dry weight. Also, in the tensional areas the predominant glycosaminoglycan was dermatan sulphate, whereas in the sesamoid the predominant glycosaminoglycan was chondroitin sulphate. The possible interrelationships between collagen axial peroidicity and proteoglycan content in this tissue are discussed.
D000818:Animals; D003094:Collagen / Q000032:analysis*; D005260:Female; D006025:Glycosaminoglycans / Q000032:analysis*; D006595:Hexosamines / Q000032:analysis; D006603:Hexuronic Acids / Q000032:analysis; D008297:Male; D010507:Periodicity; D011487:Protein Conformation; D011817:Rabbits; D013710:Tendons / Q000032:analysis* / Q000648:ultrastructure
D006025:Glycosaminoglycans; D006595:Hexosamines; D006603:Hexuronic Acids; D003094:Collagen