The effects of phosphoproteins on collagen self-assembly in tail tendon and incision dentin from rats.
Phosphoproteins retard the rate at which collagen molecules undergo self-assembly into fibrils. The inhibition appears to be dependent on the amount of phosphoprotein present, with increasing phosphoprotein concentrations resulting in greater inhibition. Prior treatment of the phosphoprotein with calcium markedly increases the resultant inhibitory effect. Dentin phosphoproteins are considerably more effective than phosvitin in retarding collagen self-assembly, with retardation times for these hard tissue extracellular matrix proteins being 25-30 times greater than control values.
D000818:Animals; D003094:Collagen / Q000096:biosynthesis / Q000378:metabolism*; D003804:Dentin; D010750:Phosphoproteins / Q000494:pharmacology*; D010774:Phosvitin / Q000494:pharmacology; D051381:Rats; D013623:Tail
D010750:Phosphoproteins; D003094:Collagen; D010774:Phosvitin