Mutations in matrilin-3 have been associated with common skeletal diseases like osteoarthritis as well as with the rare chondrodysplasias MED and SEMD. We have previously shown that the mutations p.R116W and p.C299S, associated with MED and SEMD, respectively, cause retention of matrilin-3 within th
Interaction during fibril formation of soluble collagen with cartilage proteinpolysaccharide
โ Scribed by Joseph Disalvo; Maxwell Schubert
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1966
- Tongue
- English
- Weight
- 676 KB
- Volume
- 4
- Category
- Article
- ISSN
- 0006-3525
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โฆ Synopsis
Precipitation of soluble forms of collagen from solutions containing the soluble proteinpolysaccharide (PP-L) of bovine nasal cartilage, followed by centrifugation at 100,OOO g, resulted in the formation of coherent elastic pellets whose wet weights increased with the concentration of PP-L in the initial solution. Dry weights and uronic acid contents of these pellets showed that the amount of water held in the wet pellet was nearly constant for any one kind and concentration of collagen, and ranged from 20 to 100 mg./mg. PP-L in the pellet. Soluble collagens from four different sources and PP-L from three kinds of cartilage showed similar effects. Precipitation of soluble collagen in the presence of hyaluronate or dextran yielded pellets of much smaller size than those formed in the presence of PP-L. The presence of chondroitin sulfate had only a slight effect on wet pellet weights. Wet weights of pellets formed in the presence of PP-L decreased with increasing ionic strength. A model involving entanglement between insoluble collagen fibrils and the relatively stiff chondroitin sulfate chains of branched PP-L seems qualitatively capable of accounting for these results.
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