spacer gif spacer gif spacer gif spacer gif spacer gif
 QUICK SEARCH:   [advanced]


spacer gif
     Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents    


This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by DINGLE, J. T.
Right arrow Articles by GOODMAN, D. S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by DINGLE, J. T.
Right arrow Articles by GOODMAN, D. S.

Journal of Cell Science, Vol 11, 393-402, Copyright © 1972 by Company of Biologists

Submitted on December 16, 1971

The Effect of Retinol and of Retinol-Binding Protein on Embryonic Skeletal Tissue In Organ Culture

J. T. DINGLE 1, HONOR B. FELL 2, and D. S. GOODMAN 3

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




This article has been cited by other articles:


Home page
EndocrinologyHome page
Y. Kawashima-Ohya, Y. Kuruta, W. Yan, T. Kawamoto, M. Noshiro, and Y. Kato
Retinol-Binding Protein Is Produced by Rabbit Chondrocytes and Responds to Parathyroid Hormone (PTH)/PTH-Related Peptide-Cyclic Adenosine Monophosphate Pathway
Endocrinology, March 1, 1999; 140(3): 1075 - 1081.
[Abstract] [Full Text]


Home page
fake Crit Rev Oral Biol MedHome page
B. A. Dale, J. Salonen, and A. H. Jones
New Approaches And Concepts in The Study of Differentiation of Oral Epithelia
Critical Reviews in Oral Biology & Medicine, January 1, 1990; 1(3): 167 - 190.
[Abstract] [Full Text] [PDF]




© The Company of Biologists Ltd 1972