Rabbit annulus fibrosus and nucleus pulposus were analysed for hydroxyproline, chondroitin sulphate, keratan sulphate and dermatan sulphate. Tissue proteoglycans were stained for electron microscopy with Cupromeronic blue, used in the critical electrolyte concentration mode, with and without prior digestion by chondroitinase AC or ABC, hyaluronidase or keratanase. Collagen bands, a—e were demonstrated with UO2++.
A chondroitin sulphate proteoglycan was found orthogonally associated with loosely packed collagen fibrils in annulus fibrosus at the d and e bands. The close metabolic and structural analogies with the dermatan sulphate proteoglycans previously shown to be located at collagen d-e bands in tendon, skin, etc. (Scott and Haigh (1985) Biosci. Rep.5:71–81), are discussed.
Tightly packed annulus collagen fibrils were surrounded by axially oriented proteoglycan filaments, mostly without specific locations.
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October 01 1986
Proteoglycan-collagen interactions in intervertebral disc. A chondroitin sulphate proteoglycan associates with collagen fibrils in rabbit annulus fibrosus at the d-e bands
J. E. Scott;
J. E. Scott
1Chemical Morphology, Cell and Structural Biology, Chemistry Building, University of Manchester, Manchester M139PL
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M. Haigh
M. Haigh
1Chemical Morphology, Cell and Structural Biology, Chemistry Building, University of Manchester, Manchester M139PL
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Publisher: Portland Press Ltd
Received:
October 28 1986
Online ISSN: 1573-4935
Print ISSN: 0144-8463
© 1986 Plenum Publishing Corporation
1986
Biosci Rep (1986) 6 (10): 879–888.
Article history
Received:
October 28 1986
Citation
J. E. Scott, M. Haigh; Proteoglycan-collagen interactions in intervertebral disc. A chondroitin sulphate proteoglycan associates with collagen fibrils in rabbit annulus fibrosus at the d-e bands. Biosci Rep 1 October 1986; 6 (10): 879–888. doi: https://doi.org/10.1007/BF01116241
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