Proteoglycan: collagen interactions in connective tissues. Ultrastructural, biochemical, functional and evolutionary aspects.
Electron histochemical investigations of mammalian and echinoderm tissues, using cupromeronic blue to stain proteoglycans (PGs) specifically in critical electrolyte concentration methods, showed that collagen fibrils are associated with keratan sulphate and chondroitin (dermatan) sulphate ('tadpole') PGs at the a, c, d and e bands on the fibril surface, giving rise to the 'one proteoglycan: one binding site' hypothesis. Intra-fibrillar PGs have been observed, distributed in a regular way which suggests that collagen fibrils are aggregates of 'protofibrils', some of which carry PGs at their surfaces. A scheme for remodelling of collagen fibrils, based on recycling of these protofibrils, is outlined. The choice of which tadpole PG to use to carry out a given function is decided to a considerable extent by the availability of oxygen to the relevant tissue element.
Scott
J E
JE
Chemical Morphology, Cell and Structural Biology, Manchester University, UK.
D000818:Animals; D005075:Biological Evolution; D002417:Cattle; D003094:Collagen / Q000502:physiology*; D003238:Connective Tissue / Q000737:chemistry* / Q000648:ultrastructure; D003315:Cornea / Q000737:chemistry / Q000648:ultrastructure; D003871:Dermatan Sulfate / Q000032:analysis / Q000502:physiology; D007403:Intervertebral Disc / Q000737:chemistry / Q000648:ultrastructure; D007632:Keratan Sulfate / Q000032:analysis / Q000502:physiology; D011487:Protein Conformation; D011509:Proteoglycans / Q000502:physiology*; D011817:Rabbits; D013314:Stress, Mechanical; D013710:Tendons / Q000737:chemistry / Q000648:ultrastructure
D011509:Proteoglycans; D003871:Dermatan Sulfate; D003094:Collagen; D007632:Keratan Sulfate