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Journal of Cell Science, Vol 11, 393-402, Copyright © 1972 by Company of Biologists
Submitted on December 16, 1971
1 Strangeways Research Laboratory, Cambridge, England
2 Strangeways Research Laboratory, Cambridge, England; Department of Pathology, Tennis Court Road, Cambridge, England
3 Department of Medicine, Columbia University College of Physicians and Surgeons, New York, N. Y., U.S.A.
Retinol, bound non-specifically to serum proteins in organ culture medium, caused the degradation of the extracellular matrix of chick limb-bone rudiments. The loss of polymeric material was demonstrated histologically and measured chemically.
Retinol, at the same concentration, bound specifically to retinol-binding protein, produced no significant effect. The addition of prealbumin to this system was also without discernible effect.
The addition of apo-RBP to medium containing free retinol prevented the normal hypervitaminous A effects.
The results indicate that the retinol-RBP complex has a high stability, sufficient to prevent the uptake, by the plasma or lysosomal membranes, of the amount of retinol needed for physical changes to occur.
It is suggested that retinol-binding protein may serve to transport retinol to selected sites, whilst protecting biological membranes against a general non-specific effect of the vitamin's surface active properties.
Submitted on December 16, 1971
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