1969
DOI: 10.1016/0005-2795(69)90080-4
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Collagen-protein-polysaccharide interactions in human intervertebral disc

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Cited by 25 publications
(10 citation statements)
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References 14 publications
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“…Therefore, our data are in agreement with those of Steven et al (14), Mathews (IS), and Mashburn and Hoffman ( 1 7 ) in that there are both ionic and covalent bonds between collagen and acid mucopolysaccharide. Under our electrophoretic conditions, the separation of the toluidine blue positive acid mucopolysaccharides from the proteins indicated that the bonds between the acid mucopolysaccharides and the proteins are due to ionic interactions in most of the fractions that we obtained (ie., Al, A2, A3, T1, TZ, and R ) exceptions being T3 and Tq.…”
supporting
confidence: 93%
See 1 more Smart Citation
“…Therefore, our data are in agreement with those of Steven et al (14), Mathews (IS), and Mashburn and Hoffman ( 1 7 ) in that there are both ionic and covalent bonds between collagen and acid mucopolysaccharide. Under our electrophoretic conditions, the separation of the toluidine blue positive acid mucopolysaccharides from the proteins indicated that the bonds between the acid mucopolysaccharides and the proteins are due to ionic interactions in most of the fractions that we obtained (ie., Al, A2, A3, T1, TZ, and R ) exceptions being T3 and Tq.…”
supporting
confidence: 93%
“…(12)(13)(14) extracted and fractionated the proteins from human articular, costal, and intervertebral cartilages. Recently, Steven et at?.…”
mentioning
confidence: 99%
“…There is now an overwhelming body of evidence (191,201,202,205,206,311) to support the view originally proposed by Meyer (215) that the long-chain matrix polymers with their regular anionic spacings provide the essential molecular template for the precise orderly deposition of collagen precursors and their regular sequential arrangement into collagen fibrils. Thus, enzymatic dissolution of the matrix would also inhibit new collagen formation.…”
Section: March 1979mentioning
confidence: 78%
“…More specifically, electron microscopy show a precise molecular alignment of proteoglycans along collagen chains (191). Ionic interactions between positively charged lysine and arginine residues of polymeric collagen and negatively charged glycosaminoglycan and proteoglycan sulfonic acid groups, together with the formation of hydrogen bonds, offer a probable explanation for this "adhesiveness" (311). The enzymatic degradation of such vital cross-linking bonds in the immediate vicinity of neoplastic cells could result in the dissolution and "microscopic disappearance" of this essential molecular scaffolding.…”
Section: March 1979mentioning
confidence: 99%
“…Ascorbate deficiency significantly reduces hydroxylation of proline and lysine to hydroxyproline and hydroxylysine respectively, thereby interfering with the required collagen cross-linking. Additionally the strength of the intercellular matrix also depends upon the abundance of certain long-chain mucopolysaccharide polymers, the glycosaminoglycans and proteoglycans [117,118]. Normally the intercellular matrix is maintained in steady-state equilibrium with the homeostatic balance between the formation of new macromolecules (polymerization) and decay (depolymerization) of the pre-existing ones.…”
Section: Stabilization Of Intercellular Matrix and "Walling Off" Effectmentioning
confidence: 99%