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.
Article navigation
Research Article|
April 01 1977
The proteoglycan content and the axial periodicity of collagen in tendon
Biochem J (1977) 163 (1): 145-151.
Citation
G C Gillard, M J Merrilees, P G Bell-Booth, H C Reilly, M H Flint; The proteoglycan content and the axial periodicity of collagen in tendon. Biochem J 1 April 1977; 163 (1): 145–151. doi: https://doi.org/10.1042/bj1630145
Download citation file:
Close
Sign in
Don't already have an account? Register
Sign in to your personal account
You could not be signed in. Please check your email address / username and password and try again.
Biochemical Society Member Sign in
Sign InSign in via your Institution
Sign in via your InstitutionCited By
Related Articles
Comprehensive assessment of cavernosography with 320-row dynamic volume CT versus conventional cavernosography in erectile dysfunction patients caused by venous leakage
Biosci Rep (May, 2017)
Chemistry of collagen cross-linking: biochemical changes in collagen during the partial mineralization of turkey leg tendon
Biochem J (March, 1997)
Catabolism of aggrecan, decorin and biglycan in tendon
Biochem J (August, 2000)
Evidence for glucose-mediated covalent cross-linking of collagen after glycosylation in vitro
Biochem J (February, 1985)