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The effects of phosphoproteins on collagen self-assembly in tail tendon and incision dentin from rats |
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| Authors: | Robert A Gelman Kathleen M Conn John D Termine |
| Institution: | 1. Laboratory of Biochemistry, National Institute of Dental Research, Building 30, Room 211, National Institutes of Health, Bethesda, MD 20205 U.S.A.;2. Laboratory of Biological Structure, National Institute of Dental Research, Building 30, Room 211, National Institutes of Health, Bethesda, MD 20205 U.S.A. |
| Abstract: | 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. |
| Keywords: | Phosphoprotein Collagen self-assembly Dentin tail tendon (Rat) Hepes Tes To whom requests for reprints should be addressed |
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