AJP - Gastrointestinal and Liver Physiology, Vol 268, Issue 2 224-G231, Copyright © 1995 by American Physiological Society

ARTICLES

Vitamin A trafficking in Caco-2 cells stably transfected with cellular retinol binding proteins

T. W. Lissoos, A. E. Davis and M. S. Levin
Department of Medicine, Washington University School of Medicine, St. Louis, Missouri 63110.

During intestinal vitamin A absorption, retinol is esterified by long-chain fatty acids and secreted in chylomicron particles. Stable transfectants of the human intestinal Caco-2 cell line overexpressing cellular retinol binding protein II (CRBP II) or coexpressing CRBP II and CRBP were established to study their role in intestinal vitamin A trafficking. Compared with control cell lines, retinol uptake increased up to twofold by overexpression of CRBP II and up to 2.9-fold by coexpression of CRBP and CRBP II. Retinyl ester synthesis was increased proportionate to the increase in retinol absorption in all cell lines. Retinyl ester secretion was directly correlated with retinyl ester synthesis in control and CRBP II-transfected cell lines. However, transfection with CRBP increased the proportion secreted. Expression of CRBP and CRBP II also affected the polarity of retinyl ester secretion by increasing the proportion secreted basolaterally. Thus these studies provide evidence that intestinal retinol uptake, retinyl ester synthesis, and retinyl ester secretion are correlated with levels of CRBP and CRBP II and that the effects of CRBP on retinyl ester secretion can be distinguished from those of CRBP II.

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